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Müller TD, Adriaenssens A, Ahrén B, Blüher M, Birkenfeld AL, Campbell JE, Coghlan MP, D'Alessio D, Deacon CF, DelPrato S, Douros JD, Drucker DJ, Figueredo Burgos NS, Flatt PR, Finan B, Gimeno RE, Gribble FM, Hayes MR, Hölscher C, Holst JJ, Knerr PJ, Knop FK, Kusminski CM, Liskiewicz A, Mabilleau G, Mowery SA, Nauck MA, Novikoff A, Reimann F, Roberts AG, Rosenkilde MM, Samms RJ, Scherer PE, Seeley RJ, Sloop KW, Wolfrum C, Wootten D, DiMarchi RD, Tschöp MH. Glucose-dependent insulinotropic polypeptide (GIP). Mol Metab 2025; 95:102118. [PMID: 40024571 PMCID: PMC11931254 DOI: 10.1016/j.molmet.2025.102118] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 12/06/2024] [Revised: 02/06/2025] [Accepted: 02/24/2025] [Indexed: 03/04/2025] Open
Abstract
BACKGROUND Glucose-dependent insulinotropic polypeptide (GIP) was the first incretin identified and plays an essential role in the maintenance of glucose tolerance in healthy humans. Until recently GIP had not been developed as a therapeutic and thus has been overshadowed by the other incretin, glucagon-like peptide 1 (GLP-1), which is the basis for several successful drugs to treat diabetes and obesity. However, there has been a rekindling of interest in GIP biology in recent years, in great part due to pharmacology demonstrating that both GIPR agonism and antagonism may be beneficial in treating obesity and diabetes. This apparent paradox has reinvigorated the field, led to new lines of investigation, and deeper understanding of GIP. SCOPE OF REVIEW In this review, we provide a detailed overview on the multifaceted nature of GIP biology and discuss the therapeutic implications of GIPR signal modification on various diseases. MAJOR CONCLUSIONS Following its classification as an incretin hormone, GIP has emerged as a pleiotropic hormone with a variety of metabolic effects outside the endocrine pancreas. The numerous beneficial effects of GIPR signal modification render the peptide an interesting candidate for the development of pharmacotherapies to treat obesity, diabetes, drug-induced nausea and both bone and neurodegenerative disorders.
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Affiliation(s)
- Timo D Müller
- Institute for Diabetes and Obesity, Helmholtz Munich, Germany; German Center for Diabetes Research, DZD, Germany; Walther-Straub Institute for Pharmacology and Toxicology, Ludwig-Maximilians-University Munich (LMU), Germany.
| | - Alice Adriaenssens
- Centre for Cardiovascular and Metabolic Neuroscience, Department of Neuroscience, Physiology, and Pharmacology, University College London, London, UK
| | - Bo Ahrén
- Department of Clinical Sciences, Lund, Lund University, Lund, Sweden
| | - Matthias Blüher
- Medical Department III-Endocrinology, Nephrology, Rheumatology, University of Leipzig Medical Center, Leipzig, Germany; Helmholtz Institute for Metabolic, Obesity and Vascular Research (HI-MAG) of the Helmholtz Zentrum München at the University of Leipzig and University Hospital Leipzig, Leipzig, Germany
| | - Andreas L Birkenfeld
- Department of Internal Medicine IV, University Hospital Tübingen, Tübingen 72076, Germany; Institute of Diabetes Research and Metabolic Diseases of the Helmholtz Centre Munich, Tübingen, Germany; German Center for Diabetes Research, Neuherberg, Germany
| | - Jonathan E Campbell
- Duke Molecular Physiology Institute, Duke University, Durham, NC, USA; Department of Medicine, Division of Endocrinology, Duke University, Durham, NC, USA; Department of Pharmacology and Cancer Biology, Duke University, Durham, NC, USA
| | - Matthew P Coghlan
- Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285, USA
| | - David D'Alessio
- Department of Medicine, Division of Endocrinology, Duke University, Durham, NC, USA; Duke Molecular Physiology Institute, Duke University, Durham, NC, USA
| | - Carolyn F Deacon
- School of Biomedical Sciences, Ulster University, Coleraine, UK; Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark
| | - Stefano DelPrato
- Interdisciplinary Research Center "Health Science", Sant'Anna School of Advanced Studies, Pisa, Italy
| | | | - Daniel J Drucker
- The Lunenfeld-Tanenbaum Research Institute, Mt. Sinai Hospital, and the Department of Medicine, University of Toronto, Toronto, Ontario, Canada
| | - Natalie S Figueredo Burgos
- Centre for Cardiovascular and Metabolic Neuroscience, Department of Neuroscience, Physiology, and Pharmacology, University College London, London, UK
| | - Peter R Flatt
- Diabetes Research Centre, School of Biomedical Sciences, Ulster University, Coleraine, Northern Ireland BT52 1SA, UK
| | - Brian Finan
- Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285, USA
| | - Ruth E Gimeno
- Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285, USA
| | - Fiona M Gribble
- Institute of Metabolic Science-Metabolic Research Laboratories & MRC-Metabolic Diseases Unit, University of Cambridge, Cambridge, UK
| | - Matthew R Hayes
- Department of Biobehavioral Health Sciences, School of Nursing, University of Pennsylvania, Philadelphia, PA, USA; Department of Psychiatry, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA
| | - Christian Hölscher
- Neurodegeneration Research Group, Henan Academy of Innovations in Medical Science, Xinzheng, China
| | - Jens J Holst
- Department of Biomedical Sciences and the Novo Nordisk Foundation Centre for Basic Metabolic Research, University of Copenhagen, Copenhagen, Denmark
| | - Patrick J Knerr
- Indianapolis Biosciences Research Institute, Indianapolis, IN, USA
| | - Filip K Knop
- Center for Clinical Metabolic Research, Herlev and Gentofte Hospital, University of Copenhagen, Hellerup, Denmark; Clinical Research, Steno Diabetes Center Copenhagen, Herlev, Denmark; Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
| | - Christine M Kusminski
- Touchstone Diabetes Center, University of Texas Southwestern Medical Center, Dallas, TX, USA
| | - Arkadiusz Liskiewicz
- Institute for Diabetes and Obesity, Helmholtz Munich, Germany; German Center for Diabetes Research, DZD, Germany; Department of Physiology, Faculty of Medical Sciences in Katowice, Medical University of Silesia, Katowice, Poland
| | - Guillaume Mabilleau
- Univ Angers, Nantes Université, ONIRIS, Inserm, RMeS UMR 1229, Angers, France; CHU Angers, Departement de Pathologie Cellulaire et Tissulaire, Angers, France
| | | | - Michael A Nauck
- Diabetes, Endocrinology and Metabolism Section, Department of Internal Medicine I, St. Josef-Hospital, Ruhr-University Bochum, Bochum, Germany
| | - Aaron Novikoff
- Institute for Diabetes and Obesity, Helmholtz Munich, Germany; German Center for Diabetes Research, DZD, Germany
| | - Frank Reimann
- Institute of Metabolic Science-Metabolic Research Laboratories & MRC-Metabolic Diseases Unit, University of Cambridge, Cambridge, UK
| | - Anna G Roberts
- Centre for Cardiovascular and Metabolic Neuroscience, Department of Neuroscience, Physiology, and Pharmacology, University College London, London, UK
| | - Mette M Rosenkilde
- Department of Biomedical Sciences, Faculty of Health and Medical Sciences University of Copenhagen, Copenhagen, Denmark
| | - Ricardo J Samms
- Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285, USA
| | - Philip E Scherer
- Touchstone Diabetes Center, University of Texas Southwestern Medical Center, Dallas, TX, USA
| | - Randy J Seeley
- Department of Surgery, University of Michigan, Ann Arbor, MI, USA
| | - Kyle W Sloop
- Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285, USA
| | - Christian Wolfrum
- Institute of Food, Nutrition and Health, ETH Zurich, 8092, Schwerzenbach, Switzerland
| | - Denise Wootten
- Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia; ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC, Australia
| | | | - Matthias H Tschöp
- Helmholtz Munich, Neuherberg, Germany; Division of Metabolic Diseases, Department of Medicine, Technical University of Munich, Munich, Germany
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Mu C, Shen J, Wang H, Yu K, Su Y, Zhu W. Casein Hydrolysate Enhances Upper Gastrointestinal Chemosensing and Gastric Acid Secretion in Pigs. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2025; 73:7857-7866. [PMID: 40105791 DOI: 10.1021/acs.jafc.5c01141] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 03/20/2025]
Abstract
Gastric chemosensing and gastric acid secretion affect nutrient utilization. Dietary peptides influence intestinal amino acid utilization, yet their regulation of gastric chemosensing and gastric acid secretion remains unknown. Herein, a pig model was employed to study the gastric response to dietary peptide-enriched casein hydrolysate versus intact casein. A total of 16 crossbred pigs (Duroc × Landrace × Yorkshire; 19.09 ± 0.61 kg; 63 ± 2 days of age) were randomly assigned to either an intact casein supplementation diet (n = 8) or a hydrolyzed casein supplementation diet (n = 8) for 28 days. Results showed that casein hydrolysate increased hydrochloric acid concentrations, parietal cell numbers, and H+-K+-ATPase activities in the stomach. Gastric chemosensing was upregulated, as indicated by the increased expression of peptide and amino acid chemosensors (G Protein-Coupled Receptor 92 and Calcium-Sensing Receptor) in the dorsum of the tongue, gastric corpus, and antrum. Signaling pathways involved in gastric acid secretion were also enhanced by casein hydrolysate, including extracellular stimuli (histamine, gastrin, and acetylcholine), their receptors, and intracellular signaling molecules. The upregulated gastric acid secretion was accompanied by lower amino acid concentrations in the gastric digesta and increased pepsin activity. These results demonstrate that casein hydrolysate enhances gastric chemosensing and gastric acid secretion, providing a promising nutritional strategy for regulating amino acid digestion.
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Affiliation(s)
- Chunlong Mu
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
| | - Junhua Shen
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
- National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China
| | - Huisong Wang
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
- National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China
| | - Kaifan Yu
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
- National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China
| | - Yong Su
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
- National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China
| | - Weiyun Zhu
- Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
- National Center for International Research on Animal Gut Nutrition, Nanjing Agricultural University, Nanjing 210095, China
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Dao GM, Kowalski GM, Bruce CR, O'Neal DN, Smart CE, Zaharieva DP, Hennessy DT, Zhao S, Morrison DJ. The Glycemic Impact of Protein Ingestion in People With Type 1 Diabetes. Diabetes Care 2025; 48:509-518. [PMID: 39951019 DOI: 10.2337/dci24-0096] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 10/28/2024] [Accepted: 01/07/2025] [Indexed: 03/23/2025]
Abstract
In individuals with type 1 diabetes, carbohydrate is commonly recognized as the primary macronutrient influencing postprandial glucose levels. Accumulating evidence indicates that protein ingestion also contributes to the increment in postprandial glucose levels, despite endocrine and metabolic responses different from those with carbohydrate ingestion. However, findings regarding protein ingestion's glycemic effect in people with type 1 diabetes are equivocal, with the magnitude of glycemic response seemingly dependent on the rate of absorption and composition of protein ingested. Therefore, the aim of this article is to outline the physiological mechanisms by which ingested protein influences blood glucose regulation in individuals with type 1 diabetes and provide clinical implications on use of dietary protein in the context of glycemic management. Specifically, protein ingestion raises plasma amino acid levels, which directly or indirectly (via gut hormones) stimulates glucagon secretion. Together with the increase in gluconeogenic precursors and an absent endogenous insulin response in individuals with type 1 diabetes, this provides a synergistic physiological environment for increased endogenous glucose production and subsequently increasing circulating glucose levels for several hours. While there is a dearth of well-controlled studies in this area, we provide clinical implications and directions for future research regarding the potential for using ingestion of fast-absorbing protein (such as whey protein) as a tool to prevent and mitigate overnight- and exercise-induced hypoglycemia in people with type 1 diabetes.
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Affiliation(s)
- Giang M Dao
- Institute for Physical Activity and Nutrition, School of Medicine, Deakin University, Geelong, Victoria, Australia
| | - Greg M Kowalski
- Institute for Physical Activity and Nutrition, School of Medicine, Deakin University, Geelong, Victoria, Australia
| | - Clinton R Bruce
- Institute for Physical Activity and Nutrition, School of Exercise and Nutrition Sciences, Deakin University, Geelong, Victoria, Australia
| | - David N O'Neal
- Department of Medicine, The University of Melbourne, Melbourne, Victoria, Australia
| | - Carmel E Smart
- Department of Pediatrics Diabetes and Endocrinology, John Hunter Children's Hospital, Newcastle, New South Wales, Australia
| | - Dessi P Zaharieva
- Division of Pediatric Endocrinology, Department of Pediatrics, Stanford University, Stanford, CA
| | - Declan T Hennessy
- Institute for Physical Activity and Nutrition, School of Exercise and Nutrition Sciences, Deakin University, Geelong, Victoria, Australia
- Department of Medicine, The University of Melbourne, Melbourne, Victoria, Australia
| | - Sam Zhao
- Department of Medicine, The University of Melbourne, Melbourne, Victoria, Australia
| | - Dale J Morrison
- Department of Medicine, The University of Melbourne, Melbourne, Victoria, Australia
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Pauk M, Amigo-Benavent M, Patel B, Jakeman PM, Carson BP. Comparative response of casein protein hydrolysate-fed young and older human serum on in vitro muscle protein metabolism and myotube size. Am J Physiol Cell Physiol 2025; 328:C595-C603. [PMID: 39804777 DOI: 10.1152/ajpcell.00117.2024] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/20/2024] [Revised: 12/18/2024] [Accepted: 12/18/2024] [Indexed: 01/16/2025]
Abstract
In this study, we used an ex vivo-in vitro model to assess the effect of feeding older (50-70 yr) adults a casein protein hydrolysate (CPH) compared with nonbioactive nonessential amino acid (NEAA) supplement on muscle protein synthesis (MPS) and markers of muscle protein breakdown (MPB). As a secondary objective, to assess any attenuation with aging, we compared the anabolic response to CPH-fed serum from older and young adults. Serum from seven healthy older and seven young men following overnight fast and 60-min postprandial ingestion of CPH or NEAA (0.33 g·kg-1 body mass) was used to condition C2C12 myotube media. Analysis by two-way ANOVA of the fed relative to fasted MPS response revealed a main effect for protein type in pmTOR (P = 0.009), p70S6K (P = 0.031), p4E-BP1 (P = 0.047), and MPS (P = 0.041) with a greater response to CPH-fed serum, and interaction effects (age × protein) between young and old serum for pmTOR (P = 0.009) and p70S6K (P = 0.016). In addition, significant changes in myotube diameter (P = 0.049), atrogin-1 (P = 0.004), and MuRF-1 (P = 0.012) in response to CPH-fed compared with fasted serum were observed with no differences between young and old serum. In conclusion, this study demonstrated that CPH-fed serum from both young and older (50-70 yr) adults can stimulate MPS and muscle growth and can suppress biomarkers of muscle protein breakdown processes.NEW & NOTEWORTHY This study extended previously developed coculture models and found that treating skeletal muscle cells with ex vivo human serum following feeding with a casein protein hydrolysate resulted in greater protein signaling, muscle protein synthesis, muscle growth, and lower expression of genes related to muscle protein breakdown compared with feeding with a nonessential amino acid control. These findings were similar using serum from young and older adults.
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Affiliation(s)
- Martina Pauk
- Food for Health Ireland, University of Limerick, Limerick, Ireland
- Department of Physical Education & Sport Sciences, Faculty of Education and Health Sciences, University of Limerick, Limerick, Ireland
- Institute of Musculoskeletal Medicine, University Hospital, LMU Munich, Munich, Germany
- Musculoskeletal University Center Munich, University Hospital, LMU Munich, Munich, Germany
| | | | - Bijal Patel
- Food for Health Ireland, University of Limerick, Limerick, Ireland
- Department of Physical Education & Sport Sciences, Faculty of Education and Health Sciences, University of Limerick, Limerick, Ireland
| | - Philip M Jakeman
- Food for Health Ireland, University of Limerick, Limerick, Ireland
- Department of Physical Education & Sport Sciences, Faculty of Education and Health Sciences, University of Limerick, Limerick, Ireland
- Health Research Institute, University of Limerick, Limerick, Ireland
| | - Brian P Carson
- Food for Health Ireland, University of Limerick, Limerick, Ireland
- Department of Physical Education & Sport Sciences, Faculty of Education and Health Sciences, University of Limerick, Limerick, Ireland
- Health Research Institute, University of Limerick, Limerick, Ireland
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Guccio N, Alcaino C, Miedzybrodzka EL, Santos-Hernández M, Smith CA, Davison A, Bany Bakar R, Kay RG, Reimann F, Gribble FM. Molecular mechanisms underlying glucose-dependent insulinotropic polypeptide secretion in human duodenal organoids. Diabetologia 2025; 68:217-230. [PMID: 39441374 DOI: 10.1007/s00125-024-06293-3] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 06/28/2024] [Accepted: 08/23/2024] [Indexed: 10/25/2024]
Abstract
AIMS/HYPOTHESIS Glucose-dependent insulinotropic polypeptide (GIP) is an incretin hormone secreted by enteroendocrine K cells in the proximal small intestine. This study aimed to explore the function of human K cells at the molecular and cellular levels. METHODS CRISPR-Cas9 homology-directed repair was used to insert transgenes encoding a yellow fluorescent protein (Venus) or an Epac-based cAMP sensor (Epac-S-H187) in the GIP locus in human duodenal-derived organoids. Fluorescently labelled K cells were purified by FACS for RNA-seq and peptidomic analysis. GIP reporter organoids were employed for GIP secretion assays, live-cell imaging of Ca2+ using Fura-2 and cAMP using Epac-S-H187, and basic electrophysiological characterisation. The G protein-coupled receptor genes GPR142 and CASR were knocked out to evaluate roles in amino acid sensing. RESULTS RNA-seq of human duodenal K cells revealed enrichment of several G protein-coupled receptors involved in nutrient sensing, including FFAR1, GPBAR1, GPR119, CASR and GPR142. Glucose induced action potential firing and cytosolic Ca2+ elevation and caused a 1.8-fold increase in GIP secretion, which was inhibited by the sodium glucose co-transporter 1/2 (SGLT1/2) blocker sotagliflozin. Activation of the long-chain fatty acid receptor free fatty acid receptor 1 (FFAR1) induced a 2.7-fold increase in GIP secretion, while tryptophan and phenylalanine stimulated secretion by 2.8- and 2.1-fold, respectively. While CASR knockout blunted intracellular Ca2+ responses, a CASR/GPR142 double knockout was needed to reduce GIP secretory responses to aromatic amino acids. CONCLUSIONS/INTERPRETATION The newly generated human organoid K cell model enables transcriptomic and functional characterisation of nutrient-sensing pathways involved in human GIP secretion. Both calcium-sensing receptor (CASR) and G protein-coupled receptor 142 (GPR142) contribute to protein-stimulated GIP secretion. This model will be further used to identify potential targets for modulation of native GIP secretion in diabetes and obesity.
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Affiliation(s)
- Nunzio Guccio
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Constanza Alcaino
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Emily L Miedzybrodzka
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
- Centre for Regenerative Medicine, Institute for Regeneration and Repair, University of Edinburgh, Edinburgh, UK
| | - Marta Santos-Hernández
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Christopher A Smith
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Adam Davison
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Rula Bany Bakar
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Richard G Kay
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK
| | - Frank Reimann
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK.
| | - Fiona M Gribble
- Institute of Metabolic Science, Addenbrooke's Hospital, University of Cambridge, Cambridge, UK.
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Kapoor DU, Gaur M, Kumar A, Ansari MN, Prajapati B. Bioactive Milk Peptides as a Nutraceutical Opportunity and Challenges. Curr Protein Pept Sci 2025; 26:41-56. [PMID: 39171470 DOI: 10.2174/0113892037319188240806074731] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/26/2024] [Revised: 06/08/2024] [Accepted: 06/14/2024] [Indexed: 08/23/2024]
Abstract
The biotechnology field has witnessed rapid advancements, leading to the development of numerous proteins and peptides (PPs) for disease management. The production and isolation of bioactive milk peptides (BAPs) involve enzymatic hydrolysis and fermentation, followed by purification through various techniques such as ultrafiltration and chromatography. The nutraceutical potential of bioactive milk peptides has gained significant attention in nutritional research, as these peptides may regulate blood sugar levels, mitigate oxidative stress, improve cardiovascular health, gut health, bone health, and immune responses, and exhibit anticancer properties. However, to enhance BAP bioavailability, the encapsulation method can be used to offer protection against protease degradation and controlled release. This article provides insights into the composition, types, production, isolation, bioavailability, and health benefits of BAPs.
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Affiliation(s)
- Devesh U Kapoor
- Department of Pharmaceutics, Dr. Dayaram Patel Pharmacy College, Bardoli 394601, Gujarat, India
| | - Mansi Gaur
- Rajasthan Pharmacy College, Rajasthan University of Health Sciences, Jaipur 302017, Rajasthan, India
| | - Akash Kumar
- Department of Food Technology, SRM University, Delhi NCR, Sonepat, 131029, India
- MMICT & BM (Hotel Management), Maharishi Markandeshwar (Deemed to be University), Mullana, 133207, India
| | - Mohd Nazam Ansari
- Department of Pharmacology and Toxicology, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Alkharj 11942, Saudi Arabia
| | - Bhupendra Prajapati
- Department of Pharmaceutics, Shree S. K. Patel College of Pharmaceutical Education and Research, Ganpat University, Mehsana 384012, India
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Holgersen K, Rasmussen MB, Zamir I, Aunsholt L, Zachariassen G, Sangild PT. Glucose-regulatory hormones and growth in very preterm infants fed fortified human milk. Pediatr Res 2024; 96:713-722. [PMID: 38580842 PMCID: PMC11499248 DOI: 10.1038/s41390-024-03166-8] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 06/14/2023] [Revised: 03/01/2024] [Accepted: 03/15/2024] [Indexed: 04/07/2024]
Abstract
BACKGROUND Bovine colostrum (BC) contains a range of milk bioactive components, and it is unknown how human milk fortification with BC affects glucose-regulatory hormones in very preterm infants (VPIs). This study aimed to investigate the associations between hormone concentrations and fortification type, birth weight (appropriate/small for gestational age, AGA/SGA), milk intake, postnatal age, and body growth. METHODS 225 VPIs were randomized to fortification with BC or conventional fortifier (CF). Plasma hormones were measured before, one and two weeks after start of fortification. ΔZ-scores from birth to 35 weeks postmenstrual age were calculated. RESULTS Compared with CF, infants fortified with BC had higher plasma GLP-1, GIP, glucagon, and leptin concentrations after start of fortification. Prior to fortification, leptin concentrations were negatively associated with growth, while IGF-1 concentrations associated positively with growth during fortification. In AGA infants, hormone concentrations generally increased after one week of fortification. Relative to AGA infants, SGA infants showed reduced IGF-1 and leptin concentrations. CONCLUSION Fortification with BC increased the plasma concentrations of several glucose-regulatory hormones. Concentrations of IGF-1 were positively, and leptin negatively, associated with growth. Glucose-regulatory hormone levels were affected by birth weight, milk intake and postnatal age, but not closely associated with growth in VPIs. IMPACT Little is known about the variation in glucose-regulatory hormones in the early life of very preterm infants (VPIs). This study shows that the levels of glucose-regulatory hormones in plasma of VPIs are highly variable and modified by birth weight (appropriate or small for gestational age, AGA or SGA), the type of fortifier, enteral nutritional intake, and advancing postnatal age. The results confirm that IGF-1 levels are positively associated with early postnatal growth in VPIs, yet the levels of both IGF-1 and other glucose-regulatory hormones appeared to explain only a small part of the overall variation in growth rates.
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MESH Headings
- Humans
- Infant, Newborn
- Milk, Human/chemistry
- Food, Fortified
- Leptin/blood
- Female
- Insulin-Like Growth Factor I/metabolism
- Insulin-Like Growth Factor I/analysis
- Male
- Colostrum/chemistry
- Infant, Premature/growth & development
- Infant, Premature/blood
- Animals
- Cattle
- Glucagon/blood
- Gastric Inhibitory Polypeptide/blood
- Birth Weight
- Glucagon-Like Peptide 1/blood
- Blood Glucose/metabolism
- Blood Glucose/analysis
- Infant Nutritional Physiological Phenomena
- Gestational Age
- Infant, Extremely Premature/blood
- Infant, Extremely Premature/growth & development
- Infant, Very Low Birth Weight/growth & development
- Infant, Very Low Birth Weight/blood
- Infant, Small for Gestational Age
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Affiliation(s)
- Kristine Holgersen
- Hans Christian Andersen Children's Hospital, Odense University Hospital, Odense, Denmark
- Comparative Pediatrics and Nutrition, Department of Veterinary and Animal Sciences, University of Copenhagen, Copenhagen, Denmark
| | - Martin Bo Rasmussen
- Comparative Pediatrics and Nutrition, Department of Veterinary and Animal Sciences, University of Copenhagen, Copenhagen, Denmark
| | - Itay Zamir
- Department of Clinical Sciences, Pediatrics unit, Umeå University, Umeå, Sweden
| | - Lise Aunsholt
- Department of Neonatology, Rigshospitalet, Copenhagen, Denmark
- Department of Clinical Medicine, University of Copenhagen, Copenhagen, Denmark
| | - Gitte Zachariassen
- Hans Christian Andersen Children's Hospital, Odense University Hospital, Odense, Denmark
- Department of Clinical Research, University of Southern Denmark, Odense, Denmark
- Open Patient data Explorative Network, Region of Southern Denmark, Odense, Denmark
| | - Per Torp Sangild
- Hans Christian Andersen Children's Hospital, Odense University Hospital, Odense, Denmark.
- Comparative Pediatrics and Nutrition, Department of Veterinary and Animal Sciences, University of Copenhagen, Copenhagen, Denmark.
- Department of Neonatology, Rigshospitalet, Copenhagen, Denmark.
- Department of Clinical Research, University of Southern Denmark, Odense, Denmark.
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Herrera AW, Bellesi FA, Pilosof AMR. In situ interaction of pea peptides and bile salts under in vitro digestion: Potential impact on lipolysis. Food Res Int 2024; 190:114624. [PMID: 38945578 DOI: 10.1016/j.foodres.2024.114624] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/29/2023] [Revised: 06/06/2024] [Accepted: 06/06/2024] [Indexed: 07/02/2024]
Abstract
The present work evaluated how a native pea protein isolate (PPI) affects the key roles carried out by bile salts (BS) in lipid digestion by means of the in vitro static INFOGEST protocol. Two gastric residence times were evaluated (10 and 60 min), and then the peptides obtained (GPPP) were mixed with BS at physiological concentration in simulated intestinal fluid to understand how they interact with BS both at the bulk and at the interface. Both GPPP give rise to a film with a predominant viscous character that does not constitute a barrier to the penetration of BS, but interact with BS in the bulk duodenal fluid. When the peptides flushing from the stomach after the different gastric residence times undergo duodenal digestion, it was found that for the longer gastric residence time the percentage of soluble fraction in the duodenal phase, that perform synergistically with BS micelles, was twice that of the lower residence time, leading to an increase in the solubilization of oleic acid. These results finally lead to a greater extent of lipolysis of olive oil emulsions. This work demonstrates the usefulness of in vitro models as a starting point to study the influence of gastric residence time of pea protein on its interaction with BS, affecting lipolysis. Pea proteins were shown to be effective emulsifiers that synergistically perform with BS improving the release and bioaccessibility of bioactive lipids as olive oil.
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Affiliation(s)
- Anashareth W Herrera
- ITAPROQ- Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria (1428), Buenos Aires, Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina
| | - Fernando A Bellesi
- ITAPROQ- Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria (1428), Buenos Aires, Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina.
| | - Ana M R Pilosof
- ITAPROQ- Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria (1428), Buenos Aires, Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina
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9
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Abdisa KB, Szerdahelyi E, Molnár MA, Friedrich L, Lakner Z, Koris A, Toth A, Nath A. Metabolic Syndrome and Biotherapeutic Activity of Dairy (Cow and Buffalo) Milk Proteins and Peptides: Fast Food-Induced Obesity Perspective-A Narrative Review. Biomolecules 2024; 14:478. [PMID: 38672494 PMCID: PMC11048494 DOI: 10.3390/biom14040478] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/02/2024] [Revised: 03/30/2024] [Accepted: 04/08/2024] [Indexed: 04/28/2024] Open
Abstract
Metabolic syndrome (MS) is defined by the outcome of interconnected metabolic factors that directly increase the prevalence of obesity and other metabolic diseases. Currently, obesity is considered one of the most relevant topics of discussion because an epidemic heave of the incidence of obesity in both developing and underdeveloped countries has been reached. According to the World Obesity Atlas 2023 report, 38% of the world population are presently either obese or overweight. One of the causes of obesity is an imbalance of energy intake and energy expenditure, where nutritional imbalance due to consumption of high-calorie fast foods play a pivotal role. The dynamic interactions among different risk factors of obesity are highly complex; however, the underpinnings of hyperglycemia and dyslipidemia for obesity incidence are recognized. Fast foods, primarily composed of soluble carbohydrates, non-nutritive artificial sweeteners, saturated fats, and complexes of macronutrients (protein-carbohydrate, starch-lipid, starch-lipid-protein) provide high metabolic calories. Several experimental studies have pointed out that dairy proteins and peptides may modulate the activities of risk factors of obesity. To justify the results precisely, peptides from dairy milk proteins were synthesized under in vitro conditions and their contributions to biomarkers of obesity were assessed. Comprehensive information about the impact of proteins and peptides from dairy milks on fast food-induced obesity is presented in this narrative review article.
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Affiliation(s)
- Kenbon Beyene Abdisa
- Department of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 44, HU-1118 Budapest, Hungary; (K.B.A.)
| | - Emőke Szerdahelyi
- Department of Nutrition, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Somlói út 14-16, HU-1118 Budapest, Hungary;
| | - Máté András Molnár
- Department of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 44, HU-1118 Budapest, Hungary; (K.B.A.)
| | - László Friedrich
- Department of Refrigeration and Livestock Product Technology, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 43-45, HU-1118 Budapest, Hungary
| | - Zoltán Lakner
- Department of Agricultural Business and Economics, Institute of Agricultural and Food Economics, Hungarian University of Agriculture and Life Sciences, Villányi út 29-43, HU-1118 Budapest, Hungary
| | - András Koris
- Department of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 44, HU-1118 Budapest, Hungary; (K.B.A.)
| | - Attila Toth
- Division of Clinical Physiology, Department of Cardiology, Faculty of Medicine, University of Debrecen, Móricz Zsigmond út 22, HU-4032 Debrecen, Hungary
| | - Arijit Nath
- Department of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 44, HU-1118 Budapest, Hungary; (K.B.A.)
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10
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Miltenburg J, Bastiaan-Net S, Hoppenbrouwers T, Wichers H, Hettinga K. Gastric clot formation and digestion of milk proteins in static in vitro infant gastric digestion models representing different ages. Food Chem 2024; 432:137209. [PMID: 37643515 DOI: 10.1016/j.foodchem.2023.137209] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/02/2023] [Revised: 08/03/2023] [Accepted: 08/17/2023] [Indexed: 08/31/2023]
Abstract
Gastric digestion conditions change during infancy from newborn towards more adult digestion conditions, which can change gastric digestion kinetics. However, how these changes in gastric digestion conditions during infancy affect milk protein digestion has not been investigated. Therefore, we aimed to investigate milk protein digestion with static in vitro gastric digestion models representing one-, three- and six-month-old infants. With increasing age, gastric clots and soluble proteins were digested more extensively, which may partly be attributed to the looser gastric clot structure. Larger differences with increasing age were found for heated than unheated milk proteins, which might be caused by the presence of denatured whey proteins. Taken together, these findings show that gastric milk protein digestion increases during infancy. These in vitro gastric digestion models could be used to study how milk protein digestion changes with infant age, which may aid in developing infant formulas for different age stages.
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Affiliation(s)
- Julie Miltenburg
- Food Quality and Design, Wageningen University & Research, Wageningen, The Netherlands
| | - Shanna Bastiaan-Net
- Wageningen Food & Biobased Research, Wageningen University & Research, Wageningen, The Netherlands
| | - Tamara Hoppenbrouwers
- Food Quality and Design, Wageningen University & Research, Wageningen, The Netherlands; Wageningen Food & Biobased Research, Wageningen University & Research, Wageningen, The Netherlands
| | - Harry Wichers
- Wageningen Food & Biobased Research, Wageningen University & Research, Wageningen, The Netherlands
| | - Kasper Hettinga
- Food Quality and Design, Wageningen University & Research, Wageningen, The Netherlands.
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11
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Pal B, Chattopadhyay M. Recent clinical and pharmacological advancements of incretin-based therapy and the effects of incretin on physiology. JOURNAL OF DIABETOLOGY 2024; 15:24-37. [DOI: 10.4103/jod.jod_117_23] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/06/2023] [Accepted: 01/03/2024] [Indexed: 12/11/2024] Open
Abstract
Abstract
A novel therapeutic target for diabetes mellitus is incretin-based therapies, glucagon-like peptide-1, and glucose-dependent insulinotropic polypeptides are released from the gastrointestinal (GI) tract and act on beta cells of pancreatic islets by increasing the secretion of insulin. The management and prevention of diabetes require habitual and pharmacological therapies along with quality and healthy lifestyle. This includes maintaining the body weight, blood glucose level, cardiovascular risk, complexity, and co-morbidities. The utilization of glucagon-like peptide-1 (GLP-1) agonists is an object of research with favorable hemoglobin A1C levels and weight loss in type 1 diabetic patients. However, cost-effectiveness and tolerability, remain significant barriers for patients to using these medications. The risk of suicidal tendencies and thoughts of self-harm have been increased in patients receiving GLP-1 receptor agonists. Tirzepatide treatment showed a potent glucose-lowering effect and promoted weight loss with minimum GI adverse effects in animal studies as well as phase I and II human trials, in comparison with established GLP-1 receptor agonists. The glucose-dependent insulinotropic polypeptide receptor (GIPR) peptide-antagonist effectively blocks the action of gastric-inhibitory-polypeptide (GIP) in vitro and ex vivo in human pancreas and in vivo in rodent models. However, incretin-based therapies have received enormous attention in the last few decades for the treatment of diabetes, obesity, and other repurposing including central nervous system disorders. Therefore, in this article, we demonstrate the overview, physiological, and pharmacological advances of incretin-based pharmacotherapies and their physiological roles. Furthermore, the recent updates of glucagon-like peptide-1 receptor agonist, Glucagon-like peptide-2 receptor agonist, GLP-1/GIP co-agonists, GIP/GLP-1/glucagon triple agonist and GIP-antagonist are also discussed.
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Affiliation(s)
- Bhaskar Pal
- Department of Pharmacology, Charaktala College of Pharmacy, Charaktala, Debipur, West Bengal, India
| | - Moitreyee Chattopadhyay
- Department of Pharmaceutical Technology, Maulana Abul Kalam Azad University of Technology, Nadia, West Bengal, India
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12
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Abstract
The rates of dietary protein digestion and absorption can be significantly increased or decreased by food processing treatments such as heating, gelling and enzymatic hydrolysis, with subsequent metabolic impacts, e.g. on muscle synthesis and glucose homeostasis.This review examines in vivo evidence that industrial and domestic food processing modify the kinetics of amino acid release and absorption following a protein-rich meal. It focuses on studies that used compositionally-matched test meals processed in different ways.Food processing at extremely high temperature at alkaline pH and/or in the presence of reducing sugars can modify amino acid sidechains, leading to loss of bioavailability. Some protein-rich food ingredients are deliberately aggregated, gelled or hydrolysed during manufacture. Hydrolysis accelerates protein digestion/absorption and increases splanchnic utilisation. Aggregation and gelation may slow or accelerate proteolysis in the gut, depending on the aggregate/gel microstructure.Milk, beef and eggs are heat processed prior to consumption to eliminate pathogens and improve palatability. The temperature and time of heating affect protein digestion and absorption rates, and effects are sometimes non-linear. In light of a dietary transition away from animal proteins, more research is needed on how food processing affects digestion and absorption of non-animal proteins.Food processing modifies the microstructure of protein-rich foods, and thereby alters protein digestion and absorption kinetics in the stomach and small intestine. Exploiting this principle to optimise metabolic outcomes requires more human clinical trials in which amino acid absorption rates are measured and food microstructure is explicitly considered, measured and manipulated.
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Affiliation(s)
- Simon M Loveday
- Singapore Institute of Food and Biotechnology Innovation (SIFBI), Agency for Science, Technology and Research (A*STAR), Singapore138673, Singapore
- Riddet Institute Centre of Research Excellence, Massey University, Private Bag 11 222, Palmerston North4442, New Zealand
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13
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Montserrat-de la Paz S, D Miguel-Albarreal A, Gonzalez-de la Rosa T, Millan-Linares MC, Rivero-Pino F. Protein-based nutritional strategies to manage the development of diabetes: evidence and challenges in human studies. Food Funct 2023; 14:9962-9973. [PMID: 37873616 DOI: 10.1039/d3fo02466k] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/25/2023]
Abstract
Type 2 diabetes mellitus (T2DM) is one of the most prevalent diseases in modern society, governed by both genetic and environmental factors, such as nutritional habits. This metabolic disorder is characterized by insulin resistance, which is related to high blood glucose levels, implying negative health effects in humans, hindering the healthy ageing of people. The relationship between food and health is clear, and the ingestion of specific nutrients modulates some physiological processes, potentially implying biologically relevant changes, which can translate into a health benefit. This review aims to summarize human studies published in which the purpose was to investigate the effect of protein ingestion (in native state or as hydrolysates) on human metabolism. Overall, several studies showed how protein ingestion might induce a decrease of glucose concentration in the postprandial state (area under the curve), although it is highly dependent on the source and the dose. Other studies showed no biological effects upon protein consumption, mostly with fish-derived products. In addition, the major challenges and perspectives in this research field are highlighted, suggesting the future directions, towards which scientists should focus on. The dietary intake of proteins has been proven to likely exert a beneficial effect on diabetes-related parameters, which can have a biological relevance in the prevention and pre-treatment of diabetes. However, the number of well-designed human studies carried out to date to demonstrate the effects of specific proteins or protein hydrolysates in vivo is still scarce.
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Affiliation(s)
- Sergio Montserrat-de la Paz
- Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain.
| | - Antonio D Miguel-Albarreal
- Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain.
| | - Teresa Gonzalez-de la Rosa
- Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain.
| | - Maria C Millan-Linares
- Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain.
| | - Fernando Rivero-Pino
- Department of Medical Biochemistry, Molecular Biology, and Immunology, School of Medicine, University of Seville, Av. Sanchez Pizjuan s/n, 41009 Seville, Spain.
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14
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Vivanco-Maroto SM, Gallo V, Miralles B, Recio I. CCK and GLP-1 response on enteroendocrine cells of semi-dynamic digests of hydrolyzed and intact casein. Food Res Int 2023; 171:113047. [PMID: 37330851 DOI: 10.1016/j.foodres.2023.113047] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/13/2022] [Revised: 05/09/2023] [Accepted: 05/23/2023] [Indexed: 06/19/2023]
Abstract
A semi-dynamic gastrointestinal device was employed to explore the link between protein structure and metabolic response upon digestion for two different substrates, a casein hydrolysate and the precursor micellar casein. As expected, casein formed a firm coagulum that remained until the end of the gastric phase while the hydrolysate did not develop any visible aggregate. Each gastric emptying point was subjected to a static intestinal phase where the peptide and amino acid composition changed drastically from that found during the gastric phase. Gastrointestinal digests from the hydrolysate were characterized by a high abundancy of resistant peptides and free amino acids. Although all gastric and intestinal digests from both substrates induced the secretion of cholecystokinin (CCK) and glucagon-like peptide-1 (GLP-1) in STC-1 cells, GLP-1 levels were maximum in response to gastrointestinal digests from the hydrolysate. The enrichment of protein ingredients with gastric-resistant peptides by enzymatic hydrolysis is proposed as strategy to deliver protein stimuli to the distal gastrointestinal tract to control food intake or type 2 diabetes.
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Affiliation(s)
| | - Veronica Gallo
- Instituto de Investigación en Ciencias de la Alimentación, CIAL (CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, Spain
| | - Beatriz Miralles
- Instituto de Investigación en Ciencias de la Alimentación, CIAL (CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, Spain
| | - Isidra Recio
- Instituto de Investigación en Ciencias de la Alimentación, CIAL (CSIC-UAM), Nicolás Cabrera 9, 28049 Madrid, Spain.
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15
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Wang W, Yang W, Dai Y, Liu J, Chen ZY. Production of Food-Derived Bioactive Peptides with Potential Application in the Management of Diabetes and Obesity: A Review. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2023; 71:5917-5943. [PMID: 37027889 PMCID: PMC11966776 DOI: 10.1021/acs.jafc.2c08835] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Subscribe] [Scholar Register] [Received: 12/14/2022] [Revised: 03/12/2023] [Accepted: 03/14/2023] [Indexed: 06/19/2023]
Abstract
The prevalence of diabetes mellitus and obesity is increasing worldwide. Bioactive peptides are naturally present in foods or in food-derived proteins. Recent research has shown that these bioactive peptides have an array of possible health benefits in the management of diabetes and obesity. First, this review will summarize the top-down and bottom-up production methods of the bioactive peptides from different protein sources. Second, the digestibility, bioavailability, and metabolic fate of the bioactive peptides are discussed. Last, the present review will discuss and explore the mechanisms by which these bioactive peptides help against obesity and diabetes based on in vitro and in vivo studies. Although several clinical studies have demonstrated that bioactive peptides are beneficial in alleviating diabetes and obesity, more double-blind randomized controlled trials are needed in the future. This review has provided novel insights into the potential of food-derived bioactive peptides as functional foods or nutraceuticals to manage obesity and diabetes.
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Affiliation(s)
- Weiwei Wang
- College
of Food Science and Engineering, Nanjing
University of Finance and Economics/Collaborative Innovation Center
for Modern Grain Circulation and Safety, Nanjing 210023, China
| | - Wenjian Yang
- College
of Food Science and Engineering, Nanjing
University of Finance and Economics/Collaborative Innovation Center
for Modern Grain Circulation and Safety, Nanjing 210023, China
| | - Yi Dai
- College
of Food Science and Engineering, Nanjing
University of Finance and Economics/Collaborative Innovation Center
for Modern Grain Circulation and Safety, Nanjing 210023, China
| | - Jianhui Liu
- College
of Food Science and Engineering, Nanjing
University of Finance and Economics/Collaborative Innovation Center
for Modern Grain Circulation and Safety, Nanjing 210023, China
| | - Zhen-Yu Chen
- Food
& Nutritional Sciences Programme, School of Life Sciences, The Chinese University of Hong Kong, Shatin, NT, Hong Kong, China
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16
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Evaluation of the Nutritional Quality and In Vivo Digestibility of Probiotic Beverages Enriched with Cricket Proteins. FOOD BIOPROCESS TECH 2023. [DOI: 10.1007/s11947-023-03043-y] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 03/06/2023]
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17
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Akritidou T, Akkermans S, Smet C, Delens V, Van Impe JFM. Effect of food structure and buffering capacity on pathogen survival during in vitro digestion. Food Res Int 2023; 164:112305. [PMID: 36737908 DOI: 10.1016/j.foodres.2022.112305] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/14/2022] [Revised: 12/02/2022] [Accepted: 12/03/2022] [Indexed: 12/23/2022]
Abstract
Even though a plethora of barriers are employed by the human gastrointestinal tract (GIT) to cope with invading pathogens, foodborne diseases are still a common problem. The survival of food pathogens in the GIT is known to depend on food carrier properties. The aim of this study was to investigate the influence of food buffering capacity and food structure on the survival of Salmonella Typhimurium and Listeria monocytogenes during simulated digestion, following contamination of different food model systems that had different combinations of fat and protein content. The results illustrated the strong protective properties of proteins, acting either as a strong buffering agent or as a physical barrier against gastric acidity, for both pathogens. In comparison, fat manifested a lower buffering capacity and weaker protective effects against the two pathogens. Intriguingly, a low fat content was often linked with increased microbial resistance. Nonetheless, both pathogens survived their transit through the simulated GIT in all cases, with S. Typhimurium exhibiting growth during intestinal digestion and L.monocytogenes demonstrating a healthy residual population at the end of the intestinal phase. These results corroborate the need for a deeper understanding regarding the mechanisms with which food affects bacterial survival in the human GIT.
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Affiliation(s)
- Theodora Akritidou
- BioTeC+, Chemical and Biochemical Process Technology and Control, Department of Chemical Engineering, KU Leuven, Ghent, Belgium
| | - Simen Akkermans
- BioTeC+, Chemical and Biochemical Process Technology and Control, Department of Chemical Engineering, KU Leuven, Ghent, Belgium
| | - Cindy Smet
- BioTeC+, Chemical and Biochemical Process Technology and Control, Department of Chemical Engineering, KU Leuven, Ghent, Belgium
| | - Valérie Delens
- BioTeC+, Chemical and Biochemical Process Technology and Control, Department of Chemical Engineering, KU Leuven, Ghent, Belgium
| | - Jan F M Van Impe
- BioTeC+, Chemical and Biochemical Process Technology and Control, Department of Chemical Engineering, KU Leuven, Ghent, Belgium.
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18
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José Karpeggiane de Oliveira M, Diego Brandão Melo A, Alves Marçal D, Alves da Cunha Valini G, Alisson Silva C, Mari Veira A, Zem Fraga A, Righetti Arnaut P, Henrique Reis Furtado Campos P, Sousa dos Santos L, Khun Kyaw Htoo J, Gastmann Brand H, Hauschild L. Effects of lowering dietary protein content without or with increased protein-bound and feed-grade amino acids supply on growth performance, body composition, metabolism, and acute-phase protein of finishing pigs under daily cyclic heat stress. J Anim Sci 2023; 101:skac387. [PMID: 36420675 PMCID: PMC9833036 DOI: 10.1093/jas/skac387] [Citation(s) in RCA: 3] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/19/2022] [Accepted: 11/17/2022] [Indexed: 11/25/2022] Open
Abstract
This study investigated the effects of a low-protein diet with or without an increase in dietary protein and feed-grade amino acids (AAs) on the growth performance, body composition, metabolism, and serum acute-phase proteins of finishing pigs reared in thermoneutrality or cyclic heat stress conditions. A total of 90 gilts (67.7 ± 6.2 kg) were distributed in a 2 × 3 factorial arrangement (two ambient temperatures and three diets). Ambient temperatures (AT) were thermoneutral (TN, 22 °C for 24 h) and cyclic heat stress (CHS, 12 h to 35 °C and 12 h to 22 °C). The evaluated diets (D) were high crude protein (HP); low CP-free AA-supplemented diets (LPAAs); low CP-free AA-supplemented diets and digestible Lys level (+20%), and Lys:AA ratios above recommendations (LPAA+). The experimental period lasted 48 d (two experimental phases: days 0-27 and days 28-48, respectively). CHS pigs had higher skin temperature (P < 0.05) than TN pigs. Pigs in CHS had higher rectal temperature (P < 0.05) than TN pigs until day 38 but similar (P > 0.10) to TN pigs from 38 to 45 d. For the entire experiment, CHS pigs had lower (P < 0.05) final BW, average daily gain and daily feed intake, net energy intake, body lipid, bone mineral, lipid deposition, energy retention, Lys and CP intake, and nitrogen excretion than TN pigs. The level of CP intake impacted nitrogen excretion, nitrogen retention efficiency, and urea as pigs fed HP had the highest values, and pigs fed LPAA had the lowest values (P < 0.05). On day 27, CHS pigs had lower (P < 0.05) free triiodothyronine than TN pigs. LPAA+ pigs had lower (P < 0.05) insulin than LPAA. On day 48, CHS pigs had lower (P < 0.05) thyroxine, albumin, and lactate than TN pigs. On day 27, pigs fed LPAA+ had higher (P < 0.05) lactate than pigs fed HP or LPAA. Both AT and D were enough to stimulate the immune system as CHS pigs had lower (P < 0.05) transferrin and 23-kDa protein levels than TN pigs, and HP pigs had higher haptoglobin than LPAA on day 27. These results confirm the deleterious effects of high AT on performance, body composition, metabolism, and immune system stimulation in finishing pigs. These data also show that a diet with low levels of CP can be provided to pigs in CHS without affecting performance and body composition while reducing nitrogen excretion. However, the use of a diet with an AA level above the requirements obtained by increasing intact protein and free AA did not attenuate the impact of CHS on performance and body composition of pigs.
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Affiliation(s)
- Marllon José Karpeggiane de Oliveira
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Antonio Diego Brandão Melo
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Danilo Alves Marçal
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Graziela Alves da Cunha Valini
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Cleslei Alisson Silva
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Alini Mari Veira
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Alícia Zem Fraga
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | - Pedro Righetti Arnaut
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
| | | | - Luan Sousa dos Santos
- Department of Animal Nutrition and Pastures, Federal Rural University of Rio de Janeiro, Seropédica, Rio de Janeiro, Brazil
| | | | | | - Luciano Hauschild
- Department of Animal Science, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil
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19
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Sakata Y, Yago T, Mori S, Seto N, Matsunaga Y, Nakamura H, Tominaga T, Miyaji K, Takeda Y. Time Courses of Gastric Volume and Content after Different Types of Casein Ingestion in Healthy Men: A Randomized Crossover Study. J Nutr 2022; 152:2367-2375. [PMID: 36774103 DOI: 10.1093/jn/nxac158] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/25/2022] [Revised: 06/03/2022] [Accepted: 07/11/2022] [Indexed: 11/14/2022] Open
Abstract
BACKGROUND Few studies have evaluated differences in the curd-forming ability of casein on gastric volume and content directly after ingestion in humans. OBJECTIVES This study evaluated the time course of gastric volume and curd conditions in the stomach after protein ingestion. METHODS This was an open-labeled, randomized crossover trial. Ten healthy men [age: 33.4 ± 7.3 y; BMI (kg/m2): 21.9 ± 0.9] received 350 g of 3 isonitrogenous and isocaloric protein drinks containing 30 g micellar casein (MCN), sodium caseinate (SCN), or whey protein concentrate (WPC). The gastric antrum cross-sectional area (CSA) and curd in the stomach were measured using ultrasonography within 5 h after ingestion. The differences between test foods were tested using the MIXED model and post hoc tests using Fisher's protected least significant difference. RESULTS The incremental AUC of the gastric antrum CSA after MCN ingestion was 1.3-fold and 1.5-fold higher than that after the ingestion of SCN and WPC, respectively (both P < 0.05), but not different between SCN and WPC. The number of participants with curds ≥20 mm with a high echogenicity clot observed in the stomach within 5 h after MCN ingestion was significantly greater than that after the ingestion of other proteins (n = 9 for MCN, n = 2 for SCN, and n = 0 for WPC; bothP < 0.01). The regression line slopes on total plasma amino acid concentration and gastric antrum CSA were significantly different between the participants with and without curds. CONCLUSIONS In contrast to SCN and WPC, MCN ingestion resulted in slow kinetics of gastric antrum CSA. Differences in curd formation of casein in the stomach affect gastric emptying and plasma amino acid absorption kinetics after ingestion in healthy men. This trial was registered at University Hospital Medical Information Network Clinical Trials Registry as UMIN000038388 (https://center6.umin.ac.jp/cgi-open-bin/ctr_e/ctr_view.cgi?recptno=R000043746).
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Affiliation(s)
| | - Takumi Yago
- R&D Division, Morinaga Milk Industry, Kanagawa, Japan
| | - Sadahiro Mori
- Department of Physiological Laboratory, Japanese Red Cross Sagamihara Hospital, Kanagawa, Japan
| | - Namiko Seto
- R&D Division, Morinaga Milk Industry, Kanagawa, Japan
| | - Yutaka Matsunaga
- Department of Sports Sciences, The University of Tokyo, Tokyo, Japan
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20
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Caira S, Picariello G, Renzone G, Arena S, Troise AD, De Pascale S, Ciaravolo V, Pinto G, Addeo F, Scaloni A. Recent developments in peptidomics for the quali-quantitative analysis of food-derived peptides in human body fluids and tissues. Trends Food Sci Technol 2022. [DOI: 10.1016/j.tifs.2022.06.014] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/17/2022]
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21
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Nouri M, Pourghassem Gargari B, Tajfar P, Tarighat-Esfanjani A. A systematic review of whey protein supplementation effects on human glycemic control: A mechanistic insight. Diabetes Metab Syndr 2022; 16:102540. [PMID: 35772356 DOI: 10.1016/j.dsx.2022.102540] [Citation(s) in RCA: 8] [Impact Index Per Article: 2.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 05/14/2022] [Revised: 06/04/2022] [Accepted: 06/07/2022] [Indexed: 10/18/2022]
Abstract
BACKGROUND/AIMS Some studies showed that dietary factors such as whey protein (WP) are effective on glycemic regulation. Due to the current controversy about WP effects and mechanisms of its action on glycemic control, we conducted this systematic review to shed light on the subject. METHODS Web of Science, Medline (Pubmed), and Scopus online databases were searched from 2012 up to February 2022 using the following keywords: "whey protein" and "glycemic control"/"glycemia"/"glucose"/"insulin". The search included original English articles, human clinical trials with WP supplementation and measurement of glucose or insulin as an outcome, studies on healthy individuals/patients with diabetes mellitus (DM)/impaired fasting glucose (IFG). RESULTS Title/abstract of 1991 studies were reviewed. After excluding studies due to inappropriate full title and duplication, and exercising inclusion criteria, 58 studies were reviewed in detail. Ample evidence showed that WP decreased postprandial glucose incremental area under the curve (iAUC) and increased iAUCs of insulin and incretin hormones. WP affects glycemic control mainly through stimulating insulin and incretins secretion, slowing gastric emptying, and appetite suppression. CONCLUSION Although most of the recent evidence showed beneficial effects of WP supplementation on glycemic response, further long-term clinical trials are required which assess the long-term impact of WP supplementation and its exact mechanisms.
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Affiliation(s)
- Maryam Nouri
- Student Research Committee, Student Research Center, Tabriz University of Medical Sciences, Tabriz, IR, Iran; Department of Nutrition Sciences, Varastegan Institute for Medical Sciences, Mashhad, Iran.
| | - Bahram Pourghassem Gargari
- Nutrition Research Center, Faculty of Nutrition and Food Sciences, Tabriz University of Medical Sciences, Tabriz, IR, Iran.
| | - Pedram Tajfar
- Department of Nutrition Sciences, Varastegan Institute for Medical Sciences, Mashhad, Iran.
| | - Ali Tarighat-Esfanjani
- Nutrition Research Center, Faculty of Nutrition and Food Sciences, Tabriz University of Medical Sciences, Tabriz, IR, Iran.
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22
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López-Martínez MI, Miguel M, Garcés-Rimón M. Protein and Sport: Alternative Sources and Strategies for Bioactive and Sustainable Sports Nutrition. Front Nutr 2022; 9:926043. [PMID: 35782926 PMCID: PMC9247391 DOI: 10.3389/fnut.2022.926043] [Citation(s) in RCA: 6] [Impact Index Per Article: 2.0] [Reference Citation Analysis] [Abstract] [Grants] [Track Full Text] [Download PDF] [Journal Information] [Subscribe] [Scholar Register] [Received: 04/22/2022] [Accepted: 05/17/2022] [Indexed: 11/13/2022] Open
Abstract
Nutrition and sport play an important role in achieving a healthy lifestyle. In addition to the intake of nutrients derived from the normal diet, some sport disciplines require the consumption of supplements that contribute positively to improved athletic performance. Protein intake is important for many aspects related to health, and current evidence suggests that some athletes require increased amounts of this nutrient. On the other hand, society's demand for more environmentally friendly products, focus on the search for alternative food sources more sustainable. This review aims to summarize the latest research on novel strategies and sources for greener and functional supplementation in sport nutrition. Alternative protein sources such as insects, plants or mycoproteins have proven to be an interesting substrate due to their high added value in terms of bioactivity and sustainability. Protein hydrolysis has proven to be a very useful technology to revalue by-products, such as collagen, by producing bioactive peptides beneficial on athletes performance and sport-related complications. In addition, it has been observed that certain amino acids from plant sources, as citrulline or theanine, can have an ergogenic effect for this target population. Finally, the future perspectives of protein supplementation in sports nutrition are discussed. In summary, protein supplementation in sports nutrition is a very promising field of research, whose future perspective lies with the search for alternatives with greater bioactive potential and more sustainable than conventional sources.
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Affiliation(s)
- Manuel I. López-Martínez
- Departamento de Bioactividad y Análisis de Alimenos, Instituto de Investigación en Ciencias de la Alimentación (CIAL, Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Madrid, Spain
| | - Marta Miguel
- Departamento de Bioactividad y Análisis de Alimenos, Instituto de Investigación en Ciencias de la Alimentación (CIAL, Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Madrid, Spain
- *Correspondence: Marta Miguel
| | - Marta Garcés-Rimón
- Grupo de Investigación en Biotecnología Alimentaria, Universidad Francisco de Vitoria, Madrid, Spain
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23
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Horstman AMH, Huppertz T. Milk proteins: Processing, gastric coagulation, amino acid availability and muscle protein synthesis. Crit Rev Food Sci Nutr 2022; 63:10267-10282. [PMID: 35611879 DOI: 10.1080/10408398.2022.2078782] [Citation(s) in RCA: 15] [Impact Index Per Article: 5.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/03/2022]
Abstract
It is well-known that the postprandial muscle protein synthetic response to protein ingestion is regulated on various levels, including dietary protein digestion and amino acid (AA) absorption, splanchnic AA retention, the availability of dietary protein-derived AA in the circulation, delivery of AA to the muscle, uptake of AA by the muscle, and intramuscular signaling. AA availability after consumption of dairy products is primarily determined by the rate of gastric emptying of milk proteins, which is mainly linked to coagulation of milk proteins in the stomach. Caseins form gastric coagula, which make their gastric emptying and subsequent postprandial aminoacidemia notably slower than that of whey proteins. Only recently, the role of processing, food structure, preservation and matrix on coagulation herein has been getting attention. In this review we describe various processes, that affect gastric coagulation of caseins and therewith control gastric emptying, such as the conversion to caseinate, heat treatment in the presence of whey proteins, conversion to stirred yoghurt and enzymatic hydrolysis. Modulating product characteristics by processing can be very useful to steer the gastric behavior of protein, and the subsequent digestion and AA absorption and muscle anabolic response to maintain or increase muscle mass.
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Affiliation(s)
| | - Thom Huppertz
- Research & Development, FrieslandCampina, Amersfoort, The Netherlands
- Food Quality and Design, Wageningen University & Research, Wageningen, The Netherlands
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24
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Tessari P, Toffolon A, Vettore M, Iori E, Lante A, Feller E, Rocco EA, Vedovato M, Verlato G, Bellettato M. Neither Incretin or Amino Acid Responses, nor Casein Content, Account for the Equal Insulin Response Following Iso-Lactose Loads of Natural Human and Cow Milk in Healthy Young Adults. Nutrients 2022; 14:nu14081624. [PMID: 35458186 PMCID: PMC9026711 DOI: 10.3390/nu14081624] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/26/2022] [Revised: 04/02/2022] [Accepted: 04/08/2022] [Indexed: 11/16/2022] Open
Abstract
Human milk contains <50% less protein (casein) than cow milk, but is equally effective in insulin secretion despite lower postingestion hyperaminoacidemia. Such potency of human milk might be modulated either by incretins (glucagon-like polypeptide-1,GLP-1); glucose-inhibitory-polypeptide, GIP), and/or by milk casein content. Healthy volunteers of both sexes were fed iso-lactose loads of two low-protein milks, i.e., human [Hum] (n = 8) and casein-deprived cow milk (Cow [↓Cas]) (n = 10), as well as loads of two high-protein milks, i.e., cow (n = 7), and casein-added human-milk (Hum [↑Cas]) (n = 7). Plasma glucose, insulin, C-peptide, incretins and amino acid concentrations were measured for 240′. All milks induced the same transient hyperglycemia. The early [20′−30′] insulin and C-peptide responses were comparable among all milk types apart from the low-protein (Cow [↓Cas]) milk, where they were reduced by <50% (p < 0.05 vs. others). When comparing the two high-protein milks, GLP-1 and GIP [5’−20’] responses with the (Hum [↑Cas]) milk were lower (by ≈2−3 fold, p < 0.007 and p < 0.03 respectively) than those with cow milk, whereas incretin secretion was substantially similar. Plasma amino acid increments largely reflected the milk protein content. Thus, neither casein milk content, nor incretin or amino acid concentrations, can account for the specific potency of human milk on insulin secretion, which remains as yet unresolved.
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Affiliation(s)
- Paolo Tessari
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
- Correspondence:
| | - Alessandro Toffolon
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
| | - Monica Vettore
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
| | - Elisabetta Iori
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
| | - Anna Lante
- Department of Agronomy, Food, Natural Resources, Animals & Environment (DAFNAE), University of Padova, 35123 Padova, Italy;
| | - Emiliano Feller
- Centrale del Latte di Vicenza Spa, via A. Faedo 60, 36100 Vicenza, Italy;
| | - Elisabetta Alma Rocco
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
| | - Monica Vedovato
- Department of Medicine (DIMED), Diabetes and Metabolism Division, University of Padova, 35128 Padova, Italy; (A.T.); (M.V.); (E.I.); (E.A.R.); (M.V.)
| | - Giovanna Verlato
- Department of Pediatrics, Padova City Hospital, via Giustiniani 1, 35128 Padova, Italy;
| | - Massimo Bellettato
- Department of Pediatrics, Vicenza City Hospital, viale Rodolfi, 37, 36100 Vicenza, Italy;
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25
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Duffuler P, Bhullar KS, de Campos Zani SC, Wu J. Bioactive Peptides: From Basic Research to Clinical Trials and Commercialization. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 2022; 70:3585-3595. [PMID: 35302369 DOI: 10.1021/acs.jafc.1c06289] [Citation(s) in RCA: 43] [Impact Index Per Article: 14.3] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 06/14/2023]
Abstract
Chronic diseases, including metabolic diseases, have become a worldwide public health issue. Research regarding the use of bioactive peptides or protein hydrolysates derived from food, as the diet-based strategies for the prevention and mitigation of chronic diseases, has increased exponentially in the past decades. Numerous in vitro and in vivo studies report the efficacy and safety of food-derived bioactive peptides and protein hydrolysates as antihypertensive, anti-inflammatory, antidiabetic, and antioxidant agents. However, despite promising preclinical results, an inadequate understanding of their mechanisms of action and pharmacokinetics restrict their clinical translation. Commercialization of bioactive peptides can be further hindered due to scarce information regarding their efficacy, safety, bitter taste, as well as the lack of a cost-effective method of production. This review provides an overview of the current clinical evidence and challenges to commercial applications of food-derived bioactive peptides and protein hydrolysates for the prevention and alleviation of chronic diseases.
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Affiliation(s)
- Pauline Duffuler
- Department of Agricultural Food & Nutritional Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
| | - Khushwant S Bhullar
- Department of Agricultural Food & Nutritional Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
- Department of Pharmacology, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
| | | | - Jianping Wu
- Department of Agricultural Food & Nutritional Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
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26
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Camastra S, Palumbo M, Santini F. Nutrients handling after bariatric surgery, the role of gastrointestinal adaptation. Eat Weight Disord 2022; 27:449-461. [PMID: 33895917 PMCID: PMC8933374 DOI: 10.1007/s40519-021-01194-5] [Citation(s) in RCA: 18] [Impact Index Per Article: 6.0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 11/18/2020] [Accepted: 04/10/2021] [Indexed: 01/19/2023] Open
Abstract
Bariatric surgery determines a rearrangement of the gastrointestinal tract that influences nutrient handling and plays a role in the metabolic changes observed after surgery. Most of the changes depend on the accelerated gastric emptying observed in Roux-en-Y gastric bypass (RYGB) and, to a lesser extent, in sleeve gastrectomy (SG). The rapid delivery of meal into the jejunum, particularly after RYGB, contributes to the prompt appearance of glucose in peripheral circulation. Glucose increase is the principal determinant of GLP-1 increase with the consequent stimulation of insulin secretion, the latter balanced by a paradoxical glucagon increase that stimulates EGP to prevent hypoglycaemia. Protein digestion and amino acid absorption appear accelerated after RYGB but not after SG. After RYGB, the adaptation of the gut to the new condition participates to the metabolic change. The intestinal transit is delayed, the gut microbioma is changed, the epithelium becomes hypertrophic and increases the expression of glucose transporter and of the number of cell secreting hormones. These changes are not observed after SG. After RYGB-less after SG-bile acids (BA) increase, influencing glucose metabolism probably modulating FXR and TGR5 with an effect on insulin sensitivity. Muscle, hepatic and adipose tissue insulin sensitivity improve, and the gut reinforces the recovery of IS by enhancing glucose uptake and through the effect of the BA. The intestinal changes observed after RYGB result in a light malabsorption of lipid but not of carbohydrate and protein. In conclusion, functional and morphological adaptations of the gut after RYGB and SG activate inter-organs cross-talk that modulates the metabolic changes observed after surgery.Level of evidence Level V, narrative literature review.
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Affiliation(s)
- Stefania Camastra
- Department of Clinical and Experimental Medicine, University of Pisa, Via Roma, 67, 56126, Pisa, Italy. .,Interdepartmental Research Center "Nutraceuticals and Food for Health", University of Pisa, Pisa, Italy.
| | - Maria Palumbo
- Department of Clinical and Experimental Medicine, University of Pisa, Via Roma, 67, 56126, Pisa, Italy
| | - Ferruccio Santini
- Department of Clinical and Experimental Medicine, University of Pisa, Via Roma, 67, 56126, Pisa, Italy.,Interdepartmental Research Center "Nutraceuticals and Food for Health", University of Pisa, Pisa, Italy
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27
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Eugenio FA, van Milgen J, Duperray J, Sergheraert R, Le Floc'h N. Feeding intact proteins, peptides, or free amino acids to monogastric farm animals. Amino Acids 2022; 54:157-168. [PMID: 35106634 DOI: 10.1007/s00726-021-03118-0] [Citation(s) in RCA: 10] [Impact Index Per Article: 3.3] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 09/17/2021] [Accepted: 12/09/2021] [Indexed: 12/13/2022]
Abstract
For terrestrial farm animals, intact protein sources like soybean meal have been the main ingredients providing the required amino acids (AA) to sustain life. However, in recent years, the availability of hydrolysed protein sources and free AA has led to the use of other forms of AA to feed farm animals. The advent of using these new forms is especially important to reduce the negative environmental impacts of animal production because these new forms allow reducing the dietary crude protein content and provide more digestible materials. However, the form in which dietary AA are provided can have an effect on the dynamics of nutrient availability for protein deposition and tissue growth including the efficiency of nutrient utilization. In this literature review, the use of different forms of AA in animal diets is explored, and their differences in digestion and absorption rates are focused on. These differences affect the postprandial plasma appearance of AA, which can have metabolic consequences, like greater insulin response when free AA or hydrolysates instead of intact proteins are fed, which can have a profound effect on metabolism and growth performance. Nevertheless, the use and application of the different AA forms in animal diets are important to achieve a more sustainable and efficient animal production system in the future, as they allow for a more precise diet formulation and reduced negative environmental impact. It is, therefore, important to differentiate the physiological and metabolic effects of different forms of AA to maximize their nutritional value in animal diets.
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Affiliation(s)
- F A Eugenio
- PEGASE, INRAE, Institut Agro, 35590, Saint Gilles, France
- BCF Life Sciences, Boisel, 56140, Pleucadeuc, France
| | - J van Milgen
- PEGASE, INRAE, Institut Agro, 35590, Saint Gilles, France
| | - J Duperray
- BCF Life Sciences, Boisel, 56140, Pleucadeuc, France
| | - R Sergheraert
- BCF Life Sciences, Boisel, 56140, Pleucadeuc, France
| | - N Le Floc'h
- PEGASE, INRAE, Institut Agro, 35590, Saint Gilles, France.
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28
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Whey-Adapted versus Natural Cow's Milk Formulation: Distinctive Feeding Responses and Post-Ingestive c-Fos Expression in Laboratory Mice. Foods 2022; 11:foods11020141. [PMID: 35053873 PMCID: PMC8774298 DOI: 10.3390/foods11020141] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/24/2021] [Revised: 12/23/2021] [Accepted: 01/04/2022] [Indexed: 01/10/2023] Open
Abstract
The natural 20:80 whey:casein ratio in cow’s milk (CM) for adults and infants is adjusted to reflect the 60:40 ratio of human milk, but the feeding and metabolic consequences of this adjustment have been understudied. In adult human subjects, the 60:40 CM differently affects glucose metabolism and hormone release than the 20:80 CM. In laboratory animals, whey-adapted goat’s milk is consumed in larger quantities. It is unknown whether whey enhancement of CM would have similar consequences on appetite and whether it would affect feeding-relevant brain regulatory mechanisms. In this set of studies utilizing laboratory mice, we found that the 60:40 CM was consumed more avidly than the 20:80 control formulation by animals motivated to eat by energy deprivation and by palatability (in the absence of hunger) and that this hyperphagia stemmed from prolongation of the meal. Furthermore, in two-bottle choice paradigms, whey-adapted CM was preferred against the natural 20:80 milk. The intake of the whey-adapted CM induced neuronal activation (assessed through analysis of c-Fos expression in neurons) in brain sites promoting satiation, but importantly, this activation was less pronounced than after ingestion of the natural 20:80 whey:casein CM. Activation of hypothalamic neurons synthesizing anorexigenic neuropeptide oxytocin (OT) was also less robust after the 60:40 CM intake than after the 20:80 CM. Pharmacological blockade of the OT receptor in mice led to an increase in the consumption only of the 20:80 CM, thus, of the milk that induced greater activation of OT neurons. We conclude that the whey-adapted CM is overconsumed compared to the natural 20:80 CM and that this overconsumption is associated with weakened responsiveness of central networks involved in satiety signalling, including OT.
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Tan Q, Akindehin SE, Orsso CE, Waldner RC, DiMarchi RD, Müller TD, Haqq AM. Recent Advances in Incretin-Based Pharmacotherapies for the Treatment of Obesity and Diabetes. Front Endocrinol (Lausanne) 2022; 13:838410. [PMID: 35299971 PMCID: PMC8921987 DOI: 10.3389/fendo.2022.838410] [Citation(s) in RCA: 75] [Impact Index Per Article: 25.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 12/17/2021] [Accepted: 02/07/2022] [Indexed: 01/01/2023] Open
Abstract
The incretin hormone glucagon-like peptide-1 (GLP-1) has received enormous attention during the past three decades as a therapeutic target for the treatment of obesity and type 2 diabetes. Continuous improvement of the pharmacokinetic profile of GLP-1R agonists, starting from native hormone with a half-life of ~2-3 min to the development of twice daily, daily and even once-weekly drugs highlight the pharmaceutical evolution of GLP-1-based medicines. In contrast to GLP-1, the incretin hormone glucose-dependent insulinotropic polypeptide (GIP) received little attention as a pharmacological target, because of conflicting observations that argue activation or inhibition of the GIP receptor (GIPR) provides beneficial effects on systemic metabolism. Interest in GIPR agonism for the treatment of obesity and diabetes was recently propelled by the clinical success of unimolecular dual-agonists targeting the receptors for GIP and GLP-1, with reported significantly improved body weight and glucose control in patients with obesity and type II diabetes. Here we review the biology and pharmacology of GLP-1 and GIP and discuss recent advances in incretin-based pharmacotherapies.
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Affiliation(s)
- Qiming Tan
- Department of Pediatrics, University of Alberta, Edmonton, AB, Canada
| | - Seun E. Akindehin
- Institute for Diabetes and Obesity, Helmholtz Diabetes Center at Helmholtz Zentrum München, Germany and German Center for Diabetes Research (DZD), Munich, Germany
| | - Camila E. Orsso
- Department of Agricultural Food & Nutritional Science, University of Alberta, Edmonton, AB, Canada
| | | | | | - Timo D. Müller
- Institute for Diabetes and Obesity, Helmholtz Diabetes Center at Helmholtz Zentrum München, Germany and German Center for Diabetes Research (DZD), Munich, Germany
- *Correspondence: Timo D. Müller, ; Andrea M. Haqq,
| | - Andrea M. Haqq
- Department of Pediatrics, University of Alberta, Edmonton, AB, Canada
- Department of Agricultural Food & Nutritional Science, University of Alberta, Edmonton, AB, Canada
- *Correspondence: Timo D. Müller, ; Andrea M. Haqq,
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Abstract
Milk proteins are known for their high nutritional quality, based on their essential amino acid composition, and they exhibit a wide range of bioactivities, including satiety, antimicrobial, mineral-binding, and anti-lipidemic properties. Because of their unique water solubility, milk proteins are readily separated into casein and whey fractions, which can be further fractionated into many individual proteins, including alpha-S1- and alpha-S2-caseins, beta-casein, and kappa-casein, and the whey proteins alpha-lactalbumin, lactoferrin, beta-lactoglobulin, and glycomacropeptide. Many of these proteins have unique bioactivities. Further, over the past 30 years, peptides that are encrypted in the primary amino acid sequences of proteins and released along with amino acids during digestion are increasingly recognized as biologically active protein metabolites that may have beneficial effects on human health. This review examines the current state of the science on the contribution of dairy proteins and their unique peptides and amino acids to human health.
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Affiliation(s)
| | - Donald K Layman
- Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA
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31
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Toffolon A, de Rocco‐Ponce M, Vettore M, Iori E, Lante A, Tessari P. Effect of Reversal of Whey-Protein to Casein Ratio of Cow Milk, on Insulin, Incretin, and Amino Acid Responses in Humans. Mol Nutr Food Res 2021; 65:e2100069. [PMID: 34618402 PMCID: PMC9286575 DOI: 10.1002/mnfr.202100069] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/22/2021] [Revised: 05/20/2021] [Indexed: 01/10/2023]
Abstract
SCOPE Milk-proteins, besides lactose, stimulate insulin and incretin secretion. Although whey-proteins (WP) are more efficient than casein (Cas) in hormone secretion, the effects of reversal of the (WP/Cas) ratio in whole-milk are poorly known. METHODS AND RESULTS Healthy volunteers received two different cow-milk drinks, at identical lactose (0.36 g × kg-1 BW) and total-protein (0.18 g × kg1 BW) loads, but at reversed WP/Cas ratio. One is cow-whole milk with a ≈20/80 [WP/Cas] ratio, the other an experimental cow-milk with a ≈70/30 [WP/Cas] ratio ([↑WP↓Cas]-milk). Both milk-types induced the same mild hyperglycemic response. Following [↑WP↓Cas]-milk, the [20'-90'] insulin incremental area (iAUC) (+ ≈44%, p < 0.035), and the [20'-120'] C-peptide iAUC (+ ≈47%, p < 0.015) are greater than those with cow-milk. Similarly, following [↑WP↓Cas]-milk, the GLP-1 [20'-90'] iAUC (+96%, p < 0.025), and the GIP [30'-60'] iAUC (+140%, p < 0.006), were greater than those with cow-milk. Plasma total and branched-chain amino acids are also greater following the [↑WP↓Cas] than cow-milk. CONCLUSIONS Reversal of the (WP/Cas) ratio in cow-milk enhanced the insulin response, an effect possibly mediated by incretins and/or amino acids(s). These data may be useful in designing specific milk formulas with different effects on insulin and incretin response(s).
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Affiliation(s)
- Alessandro Toffolon
- Diabetes and Metabolism DivisionDepartment of Medicine (DIMED)University of PadovaPadova35128Italy
| | - Maurizio de Rocco‐Ponce
- Diabetes and Metabolism DivisionDepartment of Medicine (DIMED)University of PadovaPadova35128Italy
| | - Monica Vettore
- Diabetes and Metabolism DivisionDepartment of Medicine (DIMED)University of PadovaPadova35128Italy
| | - Elisabetta Iori
- Diabetes and Metabolism DivisionDepartment of Medicine (DIMED)University of PadovaPadova35128Italy
| | - Anna Lante
- Department of AgronomyFood Natural ResourcesAnimals & Environment (DAFNAE)University of PadovaPadova35123Italy
| | - Paolo Tessari
- Diabetes and Metabolism DivisionDepartment of Medicine (DIMED)University of PadovaPadova35128Italy
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Aird TP, Farquharson AJ, Bermingham KM, O'Sulllivan A, Drew JE, Carson BP. Divergent serum metabolomic, skeletal muscle signaling, transcriptomic, and performance adaptations to fasted versus whey protein-fed sprint interval training. Am J Physiol Endocrinol Metab 2021; 321:E802-E820. [PMID: 34747202 PMCID: PMC8906818 DOI: 10.1152/ajpendo.00265.2021] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 07/22/2021] [Revised: 10/04/2021] [Accepted: 10/15/2021] [Indexed: 12/01/2022]
Abstract
Sprint interval training (SIT) is a time-efficient alternative to endurance exercise, conferring beneficial skeletal muscle metabolic adaptations. Current literature has investigated the nutritional regulation of acute and chronic exercise-induced metabolic adaptations in muscle following endurance exercise, principally comparing the impact of training in fasted and carbohydrate-fed (CHO) conditions. Alternative strategies such as exercising in low CHO, protein-fed conditions remain poorly characterized, specifically pertaining to adaptations associated with SIT. Thus, this study aimed to compare the metabolic and performance adaptations to acute and short-term SIT in the fasted state with preexercise hydrolyzed (WPH) or concentrated (WPC) whey protein supplementation. In healthy males, preexercise protein ingestion did not alter exercise-induced increases in PGC-1α, PDK4, SIRT1, and PPAR-δ mRNA expression following acute SIT. However, supplementation of WPH beneficially altered acute exercise-induced CD36 mRNA expression. Preexercise protein ingestion attenuated acute exercise-induced increases in muscle pan-acetylation and PARP1 protein content compared with fasted SIT. Acute serum metabolomic differences confirmed greater preexercise amino acid delivery in protein-fed compared with fasted conditions. Following 3 wk of SIT, training-induced increases in mitochondrial enzymatic activity and exercise performance were similar across nutritional groups. Interestingly, resting muscle acetylation status was downregulated in WPH conditions following training. Such findings suggest preexercise WPC and WPH ingestion positively influences metabolic adaptations to SIT compared with fasted training, resulting in either similar or enhanced performance adaptations. Future studies investigating nutritional modulation of metabolic adaptations to exercise are warranted to build upon these novel findings.NEW & NOTEWORTHY These are the first data to show the influence of preexercise protein on serum and skeletal muscle metabolic adaptations to acute and short-term sprint interval training (SIT). Preexercise whey protein concentrate (WPC) or hydrolysate (WPH) feeding acutely affected the serum metabolome, which differentially influenced acute and chronic changes in mitochondrial gene expression, intracellular signaling (acetylation and PARylation) resulting in either similar or enhanced performance outcomes when compared with fasted training.
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Affiliation(s)
- Tom P Aird
- Physical Education and Sports Sciences, University of Limerick, Limerick, Ireland
- Physical Activity for Health, Health Research Institute, University of Limerick, Limerick, Ireland
| | | | - Kate M Bermingham
- School of Agriculture and Food Science, University College Dublin, Dublin, Ireland
| | - Aifric O'Sulllivan
- School of Agriculture and Food Science, University College Dublin, Dublin, Ireland
| | - Janice E Drew
- The Rowett Institute, University of Aberdeen, Aberdeen, United Kingdom
| | - Brian P Carson
- Physical Education and Sports Sciences, University of Limerick, Limerick, Ireland
- Physical Activity for Health, Health Research Institute, University of Limerick, Limerick, Ireland
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Dridi C, Millette M, Aguilar B, Manus J, Salmieri S, Lacroix M. Effect of Physical and Enzymatic Pre-Treatment on the Nutritional and Functional Properties of Fermented Beverages Enriched with Cricket Proteins. Foods 2021; 10:2259. [PMID: 34681307 PMCID: PMC8534633 DOI: 10.3390/foods10102259] [Citation(s) in RCA: 5] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/03/2021] [Revised: 09/08/2021] [Accepted: 09/10/2021] [Indexed: 01/26/2023] Open
Abstract
The aim of this study was to evaluate the effects of γ-irradiation (IR), ultrasound (US), and combined treatments of ultrasound followed by γ-irradiation (US-IR), ultrasound followed by enzymatic hydrolysis with and without centrifugation (US-E and US-EWC, respectively), and ultrasound followed by γ-irradiation and enzymatic hydrolysis (US-IRE), on the digestibility and the nutritional value of fermented beverages containing probiotics. Results showed that US (20 min), IR (3 kGy) and US-IR (tUS = 20 min, dose = 3 kGy) treatments raised protein solubility from 11.5 to 21.5, 24.3 and 29.9%, respectively. According to our results, these treatments were accompanied by the increased amount of total sulfhydryl groups, surface hydrophobicity and changes to the secondary structure of the proteins measured by Fourier-transform infrared spectroscopy (FTIR). Fermented probiotic beverages, non-enriched (C) and enriched with untreated (Cr) or treated cricket protein with combined treatments were also evaluated for their in vitro protein digestibility. Results showed that the soluble fraction of US-IRE fermented beverage had the highest digestibility (94%) as compared to the whole fermented tested beverages. The peptides profile demonstrated that US-IRE had a low proportion of high molecular weight (MW) peptides (0.7%) and the highest proportion of low MW peptides by over 80% as compared to the other treatments.
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Affiliation(s)
- Chaima Dridi
- INRS Armand-Frappier Health Biotechnology Research Centre, Research Laboratories in Sciences, Applied to Food (RESALA), Canadian Irradiation Centre (CIC), Institute of Nutrition and Functional Foods (INAF), 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada; (C.D.); (J.M.); (S.S.)
| | - Mathieu Millette
- Bio-K Plus International Inc., a Kerry Company, Preclinical Research Division, 495 Armand-Frappier Blvd, Laval, QC H7V 4B3, Canada;
| | - Blanca Aguilar
- Research Laboratory of Industrial Microbiology, Centro Universitario de Ciencias Exactas e Ingenierías, Universidad de Guadalajara, 1421, Blvd, Marcelino Garcia Barragan, Col. Olímpica, Guadalajara 44430, Jalisco, Mexico;
| | - Johanne Manus
- INRS Armand-Frappier Health Biotechnology Research Centre, Research Laboratories in Sciences, Applied to Food (RESALA), Canadian Irradiation Centre (CIC), Institute of Nutrition and Functional Foods (INAF), 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada; (C.D.); (J.M.); (S.S.)
| | - Stephane Salmieri
- INRS Armand-Frappier Health Biotechnology Research Centre, Research Laboratories in Sciences, Applied to Food (RESALA), Canadian Irradiation Centre (CIC), Institute of Nutrition and Functional Foods (INAF), 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada; (C.D.); (J.M.); (S.S.)
| | - Monique Lacroix
- INRS Armand-Frappier Health Biotechnology Research Centre, Research Laboratories in Sciences, Applied to Food (RESALA), Canadian Irradiation Centre (CIC), Institute of Nutrition and Functional Foods (INAF), 531 Boulevard des Prairies, Laval, QC H7V 1B7, Canada; (C.D.); (J.M.); (S.S.)
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Krill Protein Hydrolysate Provides High Absorption Rate for All Essential Amino Acids-A Randomized Control Cross-Over Trial. Nutrients 2021; 13:nu13093187. [PMID: 34579064 PMCID: PMC8465607 DOI: 10.3390/nu13093187] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/11/2021] [Revised: 09/07/2021] [Accepted: 09/10/2021] [Indexed: 02/04/2023] Open
Abstract
BACKGROUND adequate protein intake is essential to humans and, since the global demand for protein-containing foods is increasing, identifying new high-quality protein sources is needed. In this study, we investigated the acute postprandial bioavailability of amino acids (AAs) from a krill protein hydrolysate compared to a soy and a whey protein isolate. METHODS the study was a randomized, placebo-controlled crossover trial including ten healthy young males. On four non-consecutive days, volunteers consumed water or one of three protein-matched supplements: whey protein isolate, soy protein isolate or krill protein hydrolysate. Blood samples were collected prior to and until 180 min after consumption. Serum postprandial AA concentrations were determined using 1H NMR spectroscopy. Hunger and satiety were assessed using visual analogue scales (VAS). RESULTS whey and krill resulted in significantly higher AA concentrations compared to soy between 20-60 min and 20-40 min after consumption, respectively. Area under the curve (AUC) analyses revealed that whey resulted in the highest postprandial serum concentrations of essential AAs (EAAs) and branched chain AAs (BCAAs), followed by krill and soy, respectively. CONCLUSIONS krill protein hydrolysate increases postprandial serum EAA and BCAA concentrations in a superior manner to soy protein isolate and thus might represent a promising future protein source in human nutrition.
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Watkins JD, Koumanov F, Gonzalez JT. Protein- and Calcium-Mediated GLP-1 Secretion: A Narrative Review. Adv Nutr 2021; 12:2540-2552. [PMID: 34192748 PMCID: PMC8634310 DOI: 10.1093/advances/nmab078] [Citation(s) in RCA: 10] [Impact Index Per Article: 2.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/03/2021] [Revised: 03/31/2021] [Accepted: 05/25/2021] [Indexed: 02/06/2023] Open
Abstract
Glucagon-like peptide 1 (GLP-1) is an incretin hormone produced in the intestine that is secreted in response to nutrient exposure. GLP-1 potentiates glucose-dependent insulin secretion from the pancreatic β cells and promotes satiety. These important actions on glucose metabolism and appetite have led to widespread interest in GLP-1 receptor agonism. Typically, this involves pharmacological GLP-1 mimetics or targeted inhibition of dipeptidyl peptidase-IV, the enzyme responsible for GLP-1 degradation. However, nutritional strategies provide a widely available, cost-effective alternative to pharmacological strategies for enhancing hormone release. Recent advances in nutritional research have implicated the combined ingestion of protein and calcium with enhanced endogenous GLP-1 release, which is likely due to activation of receptors with high affinity and/or sensitivity for amino acids and calcium. Specifically targeting these receptors could enhance gut hormone secretion, thus providing a new therapeutic option. This narrative review provides an overview of the latest research on protein- and calcium-mediated GLP-1 release with an emphasis on human data, and a perspective on potential mechanisms that link potent GLP-1 release to the co-ingestion of protein and calcium. In light of these recent findings, potential future research directions are also presented.
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Affiliation(s)
- Jonathan D Watkins
- Centre for Nutrition, Exercise and Metabolism, Department for Health, University of Bath, Bath, United Kingdom
| | - Françoise Koumanov
- Centre for Nutrition, Exercise and Metabolism, Department for Health, University of Bath, Bath, United Kingdom
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Brierley DI, de Lartigue G. Reappraising the role of the vagus nerve in GLP-1-mediated regulation of eating. Br J Pharmacol 2021; 179:584-599. [PMID: 34185884 PMCID: PMC8714868 DOI: 10.1111/bph.15603] [Citation(s) in RCA: 33] [Impact Index Per Article: 8.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/22/2021] [Revised: 06/03/2021] [Accepted: 06/16/2021] [Indexed: 12/19/2022] Open
Abstract
Here, we provide a focused review of the evidence for the roles of the vagus nerve in mediating the regulatory effects of peripherally and centrally produced GLP-1 on eating behaviour and energy balance. We particularly focus on recent studies which have used selective genetic, viral, and transcriptomic approaches to provide important insights into the anatomical and functional organisation of GLP-1-mediated gut-brain signalling pathways. A number of these studies have challenged canonical ideas of how GLP-1 acts in the periphery and the brain to regulate eating behaviour, with important implications for the development of pharmacological treatments for obesity.
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Affiliation(s)
- Daniel I Brierley
- Centre for Cardiovascular and Metabolic Neuroscience, Department of Neuroscience, Physiology and Pharmacology, University College London, London, UK
| | - Guillaume de Lartigue
- Center for Integrative Cardiovascular and Metabolic Disease, University of Florida, Gainesville, Florida, USA
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Amino Acid Absorption Profiles in Growing Pigs Fed Different Protein Sources. Animals (Basel) 2021; 11:ani11061740. [PMID: 34200892 PMCID: PMC8246322 DOI: 10.3390/ani11061740] [Citation(s) in RCA: 5] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/19/2021] [Revised: 06/02/2021] [Accepted: 06/09/2021] [Indexed: 11/30/2022] Open
Abstract
Simple Summary The speed by which amino acids are absorbed into the blood after intake of different protein sources may affect their metabolism and utilization. A better understanding of the absorption pattern can be used to optimize the formulation of diets for pigs and to reduce the nitrogen excretion to the environment. We studied the amino acid appearance in blood of growing pigs after a meal, as influenced by protein source (wheat, soybean meal, enzyme-treated soybean meal, hydrothermally-treated rapeseed meal, casein, or hydrolyzed casein). The amino acid concentration in plasma was influenced by both time after feeding and the protein source. Overall, the highest concentrations were found at 60 min after feeding for all diets, and soybean meal had a prolonged AA absorption compared to especially casein and hydrolyzed casein. We conclude that the AA absorption profiles did not indicate clear differences among protein sources, allowing categorizing in fast and slow proteins sources, but the results show differences in the duration of AA absorption. Abstract The aim of the present study was to determine postprandial amino acid (AA) appearance in the blood of growing pigs as influenced by protein source. Seven growing pigs (average body weight 18 kg), in a 7 × 5 Youden square design, were fitted with a jugular vein catheter and fed seven diets containing wheat, soybean meal, enzyme-treated soybean meal, hydrothermally-treated rapeseed meal, casein, hydrolyzed casein, and a crystalline AA blend with the same AA profile as casein. The latter was not eaten by the pigs, therefore being excluded. Blood samples were collected at −30, 30, 60, 90, 120, 180, and 360 min after a meal and analyzed for free AA. Overall, plasma AA concentrations were highest 60 min after feeding. There were no differences in plasma AA concentration between casein and hydrolyzed casein, but soybean meal resulted in lower AA plasma concentrations compared with enzyme-treated soybean meal at 60 and 120 min after feeding. There were no differences between hydrothermally-treated rapeseed meal and soybean meal. In conclusion, the ingredients could not clearly be categorized as being slow or fast protein with regard to protein digestion and absorption of AA, but soybean meal resulted in a prolonged appearance of plasma AA compared to casein and hydrolyzed casein.
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Impact of food-derived bioactive peptides on gut function and health. Food Res Int 2021; 147:110485. [PMID: 34399481 DOI: 10.1016/j.foodres.2021.110485] [Citation(s) in RCA: 32] [Impact Index Per Article: 8.0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/03/2021] [Revised: 05/10/2021] [Accepted: 05/23/2021] [Indexed: 12/14/2022]
Abstract
The gastrointestinal tract (GIT) is the largest interface between our body and the environment. It is an organ system extending from the mouth to the anus and functions for food intake, digestion, transport and absorption of nutrients, meanwhile providing protection from environmental factors, like toxins, antigens, and pathogens. Diet is one of the leading factors modulating the function of the GIT. Bioactive peptides presenting naturally in food or derived from food proteins during digestion or processing have been revealed multifunctional in diverse biological processes, including maintaining gut health and function. This review summarizes the available evidence regarding the effects of food-derived bioactive peptides on gut function and health. Findings and insights from studies based on in vitro and animal models are discussed. The gastrointestinal mucosa maintains a delicate balance between immune tolerance to nutrients and harmful components, which is crucial for the digestive system's normal functions. Dietary bioactive peptides positively impact gastrointestinal homeostasis by modulating the barrier function, immune responses, and gut microbiota. However, there is limited clinical evidence on the safety and efficacy of bioactive peptides, much less on the applications of dietary peptides for the treatment or prevention of diseases related to the GIT. Further study is warranted to establish the applications of bioactive peptides in regulating gut health and function.
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Effect of age, stress and protein supply on plasma amino acids during continuous enteral nutrition; a pragmatic study in rats. Clin Nutr 2021; 40:3931-3939. [PMID: 34139466 DOI: 10.1016/j.clnu.2021.04.045] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/27/2020] [Revised: 03/18/2021] [Accepted: 04/28/2021] [Indexed: 11/20/2022]
Abstract
BACKGROUND & AIMS As life expectancy increases, an increasing older population may require surgery with perioperative nutritional management. While little is known about the combined effect of age and stress on amino acid metabolism during enteral nutrition, we hypothesized that blood amino acid bioavailability may be influenced not only by the characteristics of the ingested protein but also by intestinal ageing and splanchnic sequestration of amino acids. Plasma amino acid kinetics were thus evaluated in aged and adult rats receiving continuous enteral nutrition before and after standardized surgical stress. METHODS Sixteen 5-month-old and sixteen 21-month-old male rats were used. After a gastrostomy, the insertion of a jugular vein catheter and a one-week recovery, the animals were enterally fed with commercially available formulas containing whole milk proteins or a whey hydrolysate for 24 h before (healthy state) and 18 h after a standardized laparotomy (surgical stress). Data were analyzed by 3-factor ANOVA. RESULTS In all rats, enteral nutrition was associated with a marked increase in plasma alanine, threonine, lysine and proline (+50 to +150 μmol/L; p < 0.001), and a decrease in glycine (≈-80 μmol/L; p < 0.01). For most amino acids, their availability depended first on the amino acid composition of each protein and second on surgical stress. Aging was only associated with higher tyrosine and threonine availability (p < 0.001). There was only limited statistical interaction between age and surgical stress. CONCLUSION In rats, plasma amino acid availability during continuous enteral nutrition is determined by the nature of the protein source and the occurrence of stress. The effects of aging on plasma amino acid availability seem very limited. Commonly used formulas therefore appear to be as suitable for elderly patients as for adult patients.
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Morgan PT, Breen L. The role of protein hydrolysates for exercise-induced skeletal muscle recovery and adaptation: a current perspective. Nutr Metab (Lond) 2021; 18:44. [PMID: 33882976 PMCID: PMC8061049 DOI: 10.1186/s12986-021-00574-z] [Citation(s) in RCA: 21] [Impact Index Per Article: 5.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/17/2020] [Accepted: 04/14/2021] [Indexed: 12/20/2022] Open
Abstract
The protein supplement industry is expanding rapidly and estimated to have a multi-billion market worth. Recent research has centred on understanding how the manufacturing processes of protein supplements may impact muscle recovery and remodeling. The hydrolysed forms of protein undergo a further heating extraction process during production which may contribute to amino acids (AA) appearing in circulation at a slightly quicker rate, or greater amplitude, than the intact form. Whilst the relative significance of the rate of aminoacidemia to muscle protein synthesis is debated, it has been suggested that protein hydrolysates, potentially through the more rapid delivery and higher proportion of di-, tri- and smaller oligo-peptides into circulation, are superior to intact non-hydrolysed proteins and free AAs in promoting skeletal muscle protein remodeling and recovery. However, despite these claims, there is currently insufficient evidence to support superior muscle anabolic properties compared with intact non-hydrolysed proteins and/or free AA controls. Further research is warranted with appropriate protein controls, particularly in populations consuming insufficient amounts of protein, to support and/or refute an important muscle anabolic role of protein hydrolysates. The primary purpose of this review is to provide the reader with a current perspective on the potential anabolic effects of protein hydrolysates in individuals wishing to optimise recovery from, and maximise adaptation to, exercise training.
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Affiliation(s)
- Paul T Morgan
- School of Sport, Exercise and Rehabilitation Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
| | - Leigh Breen
- School of Sport, Exercise and Rehabilitation Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK
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Tatsumi M, Kumagai S, Abe T, Murakami S, Takeda H, Shichinohe T, Watanabe Y, Katayama S, Hirai S, Honda A, Takekuma Y, Sugawara M. Sarcopenia in a patient with most serious complications after highly invasive surgeries treated with nutrition, rehabilitation, and pharmacotherapy: a case report. J Pharm Health Care Sci 2021; 7:16. [PMID: 33820554 PMCID: PMC8022529 DOI: 10.1186/s40780-021-00197-9] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/06/2020] [Accepted: 02/24/2021] [Indexed: 01/07/2023] Open
Abstract
BACKGROUND Several studies have reported the implementation of nutrition therapy and rehabilitation for acute and critical illnesses. However, rehabilitation nutrition for elderly sarcopenia patients with extremely severe postoperative complications during hospitalization has not yet been established. CASE PRESENTATION We report the case of a 70-year-old man with sarcopenia that developed as a postoperative complication of the surgical resection of perihilar cholangiocarcinoma and left the patient bedridden from prolonged malnutrition and muscle weakness. The patient's general condition improved after a nearly 6-month intervention by our Nutrition Support Team (NST) that combined nutrition, exercise, and pharmacotherapy. CONCLUSIONS The appropriate timing and order of pharmacotherapy, nutrient administration, exercise therapy, and team collaboration may enable elderly patients with severe (secondary) sarcopenia and postoperative complications to regain self-sustained walking.
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Affiliation(s)
- Michiyo Tatsumi
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Satomi Kumagai
- Department of Nutrition, Hokkaido University Hospital, Sapporo, Hokkaido, Japan
| | - Takahiro Abe
- Department of Rehabilitation, Hokkaido University Hospital, Sapporo, Hokkaido, Japan
| | - Soichi Murakami
- Department of Gastroenterological Surgery II, Hokkaido University Hospital, Sapporo, Hokkaido, Japan
| | - Hiroshi Takeda
- Pathophysiology and Therapeutics, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido, Japan
| | - Toshiaki Shichinohe
- Department of Gastroenterological Surgery II, Hokkaido University Hospital, Sapporo, Hokkaido, Japan
| | - Yuko Watanabe
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Shinsuke Katayama
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Shiaki Hirai
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Aiko Honda
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Yoh Takekuma
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan
| | - Mitsuru Sugawara
- Department of Pharmacy, Hokkaido University Hospital, Kita 14, Nishi 5, Kita-Ku, Sapporo, Hokkaido, 060-8648, Japan.
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Petzel EA, Acharya S, Bailey EA, Brake DW. Effects of polymerization of casein and sources of lysine on amino acid bioavailability among calves fed liquid-based diets. J Dairy Sci 2021; 104:6779-6791. [PMID: 33741162 DOI: 10.3168/jds.2020-19461] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/12/2020] [Accepted: 02/03/2021] [Indexed: 11/19/2022]
Abstract
Two experiments were conducted to evaluate the bioavailability of AA between polymerized and less polymerized or unpolymerized sources of AA. In the first experiment, 6 bull calves (53.8 ± 0.6 kg of body weight) were bottle-fed milk replacer that contained 0, 60, or 120 additional grams of AA from casein or acid hydrolyzed casein every 12 h. Plasma essential AA increased linearly with increasing intake of casein from either source. Branched-chain amino acids accounted for 74% of increases in essential AA, regardless of source of AA. Concentrations of nonessential AA increased linearly with increased intake of AA from acid hydrolyzed casein but only tended to increase in response to casein. Also, the rate of increase in total plasma AA concentration in response to acid hydrolyzed casein (4.3 µM increase per g of supplemental AA) tended to be 145% greater than casein (3.0 µM per g of supplemental AA). In a separate experiment, 6 additional bull calves (52.1 ± 0.9 kg of body weight) were bottle-fed milk replacer that contained 0, 4.8, or 9.6 additional grams of Lys from ε-polylysine or Lys-HCl each 12 h to measure Lys bioavailability between a polymerized and unpolymerized source of Lys. Plasma Lys concentrations increased linearly in response to greater Lys intake from Lys-HCl (slope = 13.51 µM/g Lys,), but plasma Lys concentrations did not change in response to increased intake of Lys from ε-polylysine. Plasma concentrations of Thr, Met, Glu, and Gln decreased linearly with increasing ε-polylysine intake, whereas concentrations of His, Val, Leu, and Ile increased linearly with increasing ε-polylysine intake. Data from these experiments suggest that the form of AA provided to calves should be considered when formulating diets to meet AA requirements.
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Affiliation(s)
- E A Petzel
- Division of Animal Sciences, University of Missouri, Columbia 65211
| | - S Acharya
- Division of Animal Sciences, University of Missouri, Columbia 65211
| | - E A Bailey
- Division of Animal Sciences, University of Missouri, Columbia 65211
| | - D W Brake
- Division of Animal Sciences, University of Missouri, Columbia 65211.
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Adjustment of Whey:Casein Ratio from 20:80 to 60:40 in Milk Formulation Affects Food Intake and Brainstem and Hypothalamic Neuronal Activation and Gene Expression in Laboratory Mice. Foods 2021; 10:foods10030658. [PMID: 33808819 PMCID: PMC8003661 DOI: 10.3390/foods10030658] [Citation(s) in RCA: 7] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/03/2021] [Revised: 03/12/2021] [Accepted: 03/16/2021] [Indexed: 02/06/2023] Open
Abstract
Adjustment of protein content in milk formulations modifies protein and energy levels, ensures amino acid intake and affects satiety. The shift from the natural whey:casein ratio of ~20:80 in animal milk is oftentimes done to reflect the 60:40 ratio of human milk. Studies show that 20:80 versus 60:40 whey:casein milks differently affect glucose metabolism and hormone release; these data parallel animal model findings. It is unknown whether the adjustment from the 20:80 to 60:40 ratio affects appetite and brain processes related to food intake. In this set of studies, we focused on the impact of the 20:80 vs. 60:40 whey:casein content in milk on food intake and feeding-related brain processes in the adult organism. By utilising laboratory mice, we found that the 20:80 whey:casein milk formulation was consumed less avidly and was less preferred than the 60:40 formulation in short-term choice and no-choice feeding paradigms. The relative PCR analyses in the hypothalamus and brain stem revealed that the 20:80 whey:casein milk intake upregulated genes involved in early termination of feeding and in an interplay between reward and satiety, such as melanocortin 3 receptor (MC3R), oxytocin (OXT), proopiomelanocortin (POMC) and glucagon-like peptide-1 receptor (GLP1R). The 20:80 versus 60:40 whey:casein formulation intake differently affected brain neuronal activation (assessed through c-Fos, an immediate-early gene product) in the nucleus of the solitary tract, area postrema, ventromedial hypothalamic nucleus and supraoptic nucleus. We conclude that the shift from the 20:80 to 60:40 whey:casein ratio in milk affects short-term feeding and relevant brain processes.
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Shrestha A, Samuelsson LM, Sharma P, Day L, Cameron-Smith D, Milan AM. Comparing Response of Sheep and Cow Milk on Acute Digestive Comfort and Lactose Malabsorption: A Randomized Controlled Trial in Female Dairy Avoiders. Front Nutr 2021; 8:603816. [PMID: 33659266 PMCID: PMC7917135 DOI: 10.3389/fnut.2021.603816] [Citation(s) in RCA: 6] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 09/08/2020] [Accepted: 01/22/2021] [Indexed: 11/13/2022] Open
Abstract
Background: Sheep milk (SM) is a possible alternate dairy source for those who experience digestive symptoms with cow milk (CM). While both the milks contain lactose, one of the causes for self-reported intolerance to CM, the composition of SM and CM also differs across proteins and fats, which have been shown to impact digestive processes. Objective: To compare the acute digestive comfort and lactose malabsorption of SM to CM in female dairy avoiders. Method: In a double-blinded, randomized cross over trial, 30 dairy-avoiding females (aged 20-30 years) drank 650 mL of SM or CM (each reconstituted from spray dried powder) following an overnight fast, on two separate occasions at least 1 week apart. Blood samples were collected for glucose and insulin assessment, and single nucleotide polymorphisms of the lactase (LCT) gene (C/T13910 and G/A22018). Breath H2 and visual analog scale (VAS) digestive symptom scores were recorded at fasting and regular intervals over 4 h after ingestion. Results: Eighty percentage of study participants were lactase non-persistent (LNP; CC13910 and GG22018 genotype). Digestive symptoms, including abdominal cramps, distension, rumbling, bloating, belching, diarrhea, flatulence, vomiting, and nausea, were similar in response to SM and CM ingestion (milk × time, P > 0.05). Breath H2 was greater after CM than SM (72 ± 10 vs. 43 ± 6 ppm at 240 min, P < 0.001), which may be due to greater lactose content in CM (33 vs. 25 g). Accordingly, when corrected for the lactose content breath H2 did not differ between the two milks. The response remained similar when analyzed in the LNP subset alone (n = 20). Conclusions: Despite a higher energy and nutrient content, SM did not increase adverse digestive symptoms after ingestion, relative to CM, although there was a reduced breath H2 response, which could be attributed to the lower lactose content in SM. The tolerability of SM should be explored in populations without lactose intolerance for whom underlying trigger for intolerance is unknown.
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Affiliation(s)
- Aahana Shrestha
- The Liggins Institute, The University of Auckland, Auckland, New Zealand.,Riddet Institute, Palmerston North, New Zealand
| | | | - Pankaja Sharma
- The Liggins Institute, The University of Auckland, Auckland, New Zealand.,Riddet Institute, Palmerston North, New Zealand
| | - Li Day
- AgResearch Ltd., Te Ohu Rangahau Kai, Palmerston North, New Zealand
| | - David Cameron-Smith
- The Liggins Institute, The University of Auckland, Auckland, New Zealand.,Riddet Institute, Palmerston North, New Zealand.,Singapore Institute for Clinical Sciences, Agency for Science, Technology, and Research, Singapore, Singapore
| | - Amber M Milan
- The Liggins Institute, The University of Auckland, Auckland, New Zealand.,AgResearch Ltd., Te Ohu Rangahau Kai, Palmerston North, New Zealand
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Abstract
Glucagon-like peptide-1 (GLP-1) is an enterohormone with a key role in several processes controlling body homeostasis, including glucose homeostasis and food intake regulation. It is secreted by the intestinal cells in response to nutrients, such as glucose, fat and amino acids. In the present review, we analyse the effect of protein on GLP-1 secretion and clearance. We review the literature on the GLP-1 secretory effects of protein and protein hydrolysates, and the mechanisms through which they exert these effects. We also review the studies on protein from different sources that has inhibitory effects on dipeptidyl peptidase-4 (DPP4), the enzyme responsible for GLP-1 inactivation, with particular emphasis on specific sources and treatments, and the gaps there still are in knowledge. There is evidence that the protein source and the hydrolytic processing applied to them can influence the effects on GLP-1 signalling. The gastrointestinal digestion of proteins, for example, significantly changes their effectiveness at modulating this enterohormone secretion in both in vivo and in vitro studies. Nevertheless, little information is available regarding human studies and more research is required to understand their potential as regulators of glucose homeostasis.
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Raoufi N, Ye A, Han J. New insights into in vivo gastroduodenal digestion of oil-in-water emulsions: gastric stability and in vitro digestion modeling. Crit Rev Food Sci Nutr 2021; 62:3723-3737. [PMID: 33432823 DOI: 10.1080/10408398.2020.1868396] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 02/08/2023]
Abstract
In this paper, effect of emulsion stability on gastroduodenal emptying/secretion was reviewed and differentiated. Moreover, novel perspectives on physiology of gastric lumen, duodenum, and gall bladder were achieved using mathematical models, being useful for designing artificial digestive systems. In this regard, numerical data for dynamic gastric emptying/secretion were offered for gastric-stable and gastric-unstable emulsion intakes. It was shown that alterations in human gastric and duodenal volume follow, respectively, linear and sinusoidal curves, with high correlation coefficients (r2 > 0.93). For both emulsions, about 30-40 mL ingesta discharged rapidly from stomach upon ingestion; However, further gastric emptying was regulated for the rest of digestion period, so that 0.1 mL/min oil was passing through duodenum. Intragastric evacuation of both emulsions started with a lag phase during which stomach stored secretions incrementally by slow gastric discharge. Lag phase ended with fat layering, when emptying considerably enhanced. This reduction was gradual for stable emulsion while unstable emulsion experienced a rapid emptying before slow declining trend. Along with initial gastric emptying, 87% of gallbladder content discharged into duodenum, prolonged up to the gradual reduction phase of stomach. Supplementary investigations are needed to quantify gastroduodenal secretions, particularly pepsin and pancreas in response to emulsion ingesta.
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Affiliation(s)
- Nassim Raoufi
- Department of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, PR China
| | - Aiqian Ye
- Riddet Institute, Massey University, Palmerston North, New Zealand
| | - Jianzhong Han
- Department of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, PR China
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Mennah-Govela YA, Bornhorst GM. Breakdown mechanisms of whey protein gels during dynamic in vitro gastric digestion. Food Funct 2021; 12:2112-2125. [DOI: 10.1039/d0fo03325a] [Citation(s) in RCA: 5] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/10/2023]
Abstract
Particle geometry influenced the breakdown mechanisms impacting the pH, pepsin activity, and protein hydrolysis of whey protein gels during dynamic in vitro gastric digestion.
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Affiliation(s)
- Yamile A. Mennah-Govela
- Dept. of Biological and Agricultural Engineering
- 1308 Bainer Hall
- University of California
- Davis
- Davis
| | - Gail M. Bornhorst
- Dept. of Biological and Agricultural Engineering
- 1308 Bainer Hall
- University of California
- Davis
- Davis
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Mennah-Govela YA, Bornhorst GM. Food buffering capacity: quantification methods and its importance in digestion and health. Food Funct 2021; 12:543-563. [DOI: 10.1039/d0fo02415e] [Citation(s) in RCA: 17] [Impact Index Per Article: 4.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/21/2022]
Abstract
Understanding the influence of food properties on buffering capacity will have an impact on gastric secretions and breakdown during digestion.
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Affiliation(s)
- Yamile A. Mennah-Govela
- Department. of Biological and Agricultural Engineering
- 1308 Bainer Hall
- University of California
- Davis
- Davis
| | - Gail M. Bornhorst
- Department. of Biological and Agricultural Engineering
- 1308 Bainer Hall
- University of California
- Davis
- Davis
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Hira T, Sekishita M, Hara H. Blood Sampling From Rat Ileal Mesenteric Vein Revealed a Major Role of Dietary Protein in Meal-Induced GLP-1 Response. Front Endocrinol (Lausanne) 2021; 12:689685. [PMID: 34149624 PMCID: PMC8206781 DOI: 10.3389/fendo.2021.689685] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 04/01/2021] [Accepted: 05/17/2021] [Indexed: 11/29/2022] Open
Abstract
The present study was conducted to examine region-dependent glucagon-like peptide-1 (GLP-1) responses to "meal ingestion" under physiological (conscious and unrestrained) conditions using rats with a catheter inserted into either the portal vein (PV) or the ileal mesenteric vein (ILMV). After recovery from the cannulation surgery, blood samples were collected from either PV or ILMV catheter before and after the voluntary ingestion of test diets. After an AIN-93G standard diet ingestion, GLP-1 concentration was higher in ILMV than in PV, and postprandial responses of peptide-YY (PYY) had similar trend, while that of glucose dependent-insulinotropic polypeptide showed an opposite trend to GLP-1/PYY responses. In a separated experiment, a protein-enriched diet containing casein at 25% wt/wt transiently increased GLP-1 concentration only in ILMV; however, a protein-free diet did not increase GLP-1 concentrations in PV or ILMV. These results indicate that postprandial GLP-1 is immediately released from the distal intestine under physiological conditions, and that dietary protein has a critical role in the enhancement of postprandial GLP-1 response.
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Affiliation(s)
- Tohru Hira
- Research Faculty of Agriculture, Hokkaido University, Sapporo, Japan
- Graduate School of Agriculture, Hokkaido University, Sapporo, Japan
- *Correspondence: Tohru Hira,
| | - Madoka Sekishita
- Graduate School of Agriculture, Hokkaido University, Sapporo, Japan
| | - Hiroshi Hara
- Faculty of Human Life Science, Fuji Women’s University, Ishikari, Japan
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