• Acute kidney injury associated with nephrotic syndrome
• Complete remission
• Edema
• Monogenic variants
• Steroid-resistant nephrotic syndrome

• Humans
• Nephrotic Syndrome/genetics
• Nephrotic Syndrome/drug therapy
• Child
• Male
• Child, Preschool
• Female
• Adolescent
• Infant
• Drug Resistance/genetics
• Proteinuria/genetics
• Steroids/therapeutic use
• Mutation
• Genetic Testing/methods
• Retrospective Studies

• Kobe University

• FcRn
• IgG
• albumin
• autoimmune
• hypoalbuminemia
• monoclonal antibody
• serum protein

Thrombosis is a major comorbidity of obesity and type-2 diabetes mellitus (T2DM). Despite the development of numerous effective treatments and preventative strategies to address thrombotic disease in such individuals, the incidence of thrombotic complications remains high. This suggests that not all the pathophysiological mechanisms underlying these events have been identified or targeted. Non-esterified fatty acids (NEFAs) are increasingly regarded as a nexus between obesity, insulin resistance, and vascular disease. Notably, plasma NEFA levels are consistently elevated in obesity and T2DM and may impact hemostasis in several ways. A potentially unrecognized route of NEFA-mediated thrombotic activity is their ability to disturb Zn²⁺ speciation in the plasma. Zn²⁺ is a potent regulator of coagulation and its availability in the plasma is monitored carefully through buffering by human serum albumin (HSA). The binding of long-chain NEFAs such as palmitate and stearate, however, trigger a conformational change in HSA that reduces its ability to bind Zn²⁺, thus increasing the ion’s availability to bind and activate coagulation proteins. NEFA-mediated perturbation of HSA-Zn²⁺ binding is thus predicted to contribute to the prothrombotic milieu in obesity and T2DM, representing a novel targetable disease mechanism in these disorders.

• diabetes
• human serum albumin
• insulin resistance
• non-esterified fatty acids
• obesity
• thrombosis
• zinc

• Animals
• Diabetes Mellitus, Type 2/blood
• Diabetes Mellitus, Type 2/epidemiology
• Diabetes Mellitus, Type 2/metabolism
• Fatty Acids, Nonesterified/blood
• Fatty Acids, Nonesterified/metabolism
• Humans
• Obesity/blood
• Obesity/epidemiology
• Obesity/metabolism
• Thrombosis/blood
• Thrombosis/epidemiology
• Thrombosis/metabolism
• Zinc/blood
• Zinc/metabolism

• FS/20/3/34956 British Heart Foundation
• FS/19/69/34639 British Heart Foundation

• FS/15/42/31556 British Heart Foundation
• PG/15/9/31270 British Heart Foundation
• Commonwealth Scholarship Commission

Albumin, the most abundant plasma protein, not only controls osmotic blood pressure, but also serves as a carrier for various small molecules, including pharmaceuticals. Its impact on pharmacological properties of many drugs has been extensively studied over decades. Here, we focus on its interaction with the following mobilizing agents: Granulocyte-colony stimulating factor (G-CSF) and AMD3100, where such analyses are lacking. These compounds are widely used for hematopoietic stem cell mobilization of healthy donors or patients. Using albumin-deficient (Alb−/−) mice, we studied the contribution of albumin to mobilization outcomes. Mobilization with the bicyclam CXCR4 antagonist AMD3100 was attenuated in Alb−/− mice compared to wild-type littermates. By contrast, mobilization with recombinant human G-CSF (rhG-CSF), administered twice daily over a five-day course, was significantly increased in Alb−/− mice. In terms of a mechanism, we show that rhG-CSF bioavailability in the bone marrow is significantly improved in Alb−/− mice, compared to wild-type (WT) littermates, where rhG-CSF levels dramatically drop within a few hours of the injection. These observations likely explain the favorable mobilization outcomes with split-dose versus single-dose administration of rhG-CSF to healthy donors.

• AMD3100
• Plerixafor
• granulocyte-colony stimulating factor
• hematopoietic stem cell mobilization
• hematopoietic stem cell transplantation
• pharmacodynamics
• serum albumin deficiency

• Hypoalbuminemia
• hypocalcemia
• sequence analysis, DNA
• vitamin D deficiency

• Adult
• Humans
• Hypoalbuminemia/congenital
• Hypoalbuminemia/diagnosis
• Hypoalbuminemia/genetics
• Hypoalbuminemia/metabolism
• Male
• Polymorphism, Single Nucleotide
• Republic of Korea
• Sequence Analysis, DNA
• Serum Albumin, Human/genetics

Congenital analbuminemia (CAA) is an inherited, autosomal recessive disorder with an incidence of 1:1,000,000 live birth. Affected individuals have a strongly decreased concentration, or complete absence, of serum albumin. The trait is usually detected by serum protein electrophoresis and immunochemistry techniques. However, due to the existence of other conditions in which the albumin concentrations are very low or null, analysis of the albumin (ALB) gene is necessary for the molecular diagnosis. CAA can lead to serious consequences in the prenatal period, because it can cause miscarriages and preterm birth, which often is due to oligohydramnios and placental abnormalities. Neonatally and in early childhood the trait is a risk factor that can lead to death, mainly from fluid retention and infections in the lower respiratory tract. By contrast, CAA is better tolerated in adulthood. Clinically, in addition to the low level of albumin, the patients almost always have hyperlipidemia, but they usually also have mild oedema, reduced blood pressure and fatigue. The fairly mild symptoms in adulthood are due to compensatory increment of other plasma proteins. The condition is rare; clinically, only about 90 cases have been detected worldwide. Among these, 53 have been studied by sequence analysis of the ALB gene, allowing the identification of 27 different loss of function (LoF) pathogenic variants. These include a variant in the start codon, frame-shift/insertions, frame-shift/deletions, nonsense variants, and variants affecting splicing. Most are unique, peculiar for each affected family, but one, a frame-shift deletion called Kayseri, has been found to cause about one third of the known cases allowing to presume a founder effect. This review provides an overview of the literature about CAA, about supportive and additional physiological and pharmacological information obtained from albumin-deficient mouse and rat models and a complete and up-to-date dataset of the pathogenic variants identified in the ALB gene.

• DNA-sequencing
• analbuminemia
• autosomal recessive
• compensatory mechanisms
• frequency
• hyperlipidemia
• pathogenic variations
• preterm birth

Congenital analbuminemia (CAA) is a very rare disorder. Our data describes the clinical features and laboratory results of a new case established by mutation analysis of the albumin gene in a 39-year-old woman presenting with hypercholesterolemia. Our findings contribute to shed light on the molecular genetics of the disorder and confirm that safe and well tolerated hypocholesterolemic treatment with atorvastatin may be administered in dislipidemic patient with CAA in order to reduce their cardiovascular risk.

Our patient presented with a history of hypercholesterolemia and referred asthenia and heaviness in both legs. She was born from healthy and non-consanguineous parents and her development was normal. She had not familiarity for early cardiovascular disease, and did not report personal history of hypertension, chronic kidney or liver diseases. Clinical laboratories results showed critically reduced value of albumin whereas other serum proteins were elevated. Main causes of hypoalbuminemia (proteinuria, inflammatory state and insufficient hepatic synthesis) were ruled out by normal procedures and laboratory tests. So the hypothesis of a CAA was tested through mutation analysis of the albumin gene that revealed a homozygous CA deletion in exon 12, at nucleotide positions c1614-1615. This finding brought to the diagnosis of CAA. Currently the patient receives Atorvastatin 20 mg od and undergoes clinical and laboratory follow-up every six months. She never needed albumin infusions.

Our experience shows how treatment with atorvastatin may be safely administered and well tolerated in patients affected by CAA.

• Congenital analbuminemia
• Hypercholesterolemia
• Hypoalbuminemia
• Rare disease
• Case report

• amiloride
• diuretics
• epithelial sodium channel
• nephrotic syndrome
• oedema

• Animals
• Dermatan Sulfate/metabolism
• Glycosaminoglycans/metabolism
• Heparin/metabolism
• Heparitin Sulfate/metabolism
• Humans
• Kininogens/metabolism
• Proteins/metabolism
• Zinc/metabolism

• FS/15/42/31556 British Heart Foundation
• PG/15/9/31270 British Heart Foundation

• Cardiovascular risk
• Hemodialysis
• Mortality risk
• suPAR

• Aged
• Creatinine/blood
• Female
• Humans
• Kidney Failure, Chronic/blood
• Kidney Failure, Chronic/diagnosis
• Kidney Failure, Chronic/mortality
• Kidney Failure, Chronic/therapy
• Kidney Function Tests/methods
• Male
• Middle Aged
• Natriuretic Peptide, Brain/blood
• Peptide Fragments/blood
• Poland/epidemiology
• Predictive Value of Tests
• Prognosis
• Receptors, Urokinase Plasminogen Activator/blood
• Renal Dialysis/methods
• Risk Assessment
• Risk Factors

• Body fluids
• Body water
• Congestive heart failure
• Extracellular volume
• Hepatic cirrhosis
• Hypertonicity
• Hypotonicity
• Nephrotic syndrome
• Sepsis

• R01 HL105649 NHLBI NIH HHS
• U01 HL071556 NHLBI NIH HHS
• F32 DK009924 NIDDK NIH HHS
• R01 HL109015 NHLBI NIH HHS
• U01 DK099914 NIDDK NIH HHS
• R01 DK073665 NIDDK NIH HHS

• Adult
• Aged
• Cohort Studies
• Female
• Humans
• Kidney Failure, Chronic/blood
• Kidney Failure, Chronic/complications
• Kidney Failure, Chronic/mortality
• Male
• Middle Aged
• Prospective Studies
• Serum Albumin/metabolism
• Survival Analysis

• Baxter Healthcare Corporation
• Amgen
• Medicinska Forskningsrådet
• Martin Rind Foundation SE
• Njurfonden
• Westmans Foundation Sweden

• Congenital Abnormalities/diagnosis
• Delivery, Obstetric
• Female
• Humans
• Mutation
• Polyhydramnios/diagnosis
• Polyhydramnios/diagnostic imaging
• Polyhydramnios/drug therapy
• Pregnancy
• Pregnancy Complications/diagnosis
• Serum Albumin/administration & dosage
• Serum Albumin/deficiency
• Serum Albumin/genetics
• Young Adult

• DNA mutational analysis
• congenital analbuminemia
• frame-shift
• single base deletion

• Alport syndrome
• albumin
• collagen type IV

• ALT, alanine aminotransferase
• AST, aspartate aminotransferase
• FcRn, neonatal Fc receptor
• HDL, high-density lipoprotein
• HSA, human serum albumin
• IgG, immunoglobulin G
• LDH, low-density-lipoprotein
• MSA, mouse serum albumin
• TALEN
• TALEN, transcription activator-like effector nuclease
• albumin
• albumin-conjugates
• analbuminemia
• hFcRn, human FcRn
• human serum albumin
• hypoalbuminemia
• mouse model
• neonatal Fc receptor
• pharmacokinetics
• transgenic

• Epithelial sodium channel
• Nephrotic syndrome
• Potassium sparing diuretics
• Proteinuria
• Serine proteases

• Epithelial Sodium Channels/metabolism
• Humans
• Hypertension/etiology
• Hypertension/metabolism
• Kidney/metabolism
• Nephrotic Syndrome/complications
• Nephrotic Syndrome/metabolism
• Proteinuria
• Sodium/metabolism
• Water-Electrolyte Imbalance/complications
• Water-Electrolyte Imbalance/drug therapy
• Water-Electrolyte Imbalance/metabolism

• P30 DK079307 NIDDK NIH HHS
• R01 DK051391 NIDDK NIH HHS
• R37 DK051391 NIDDK NIH HHS
• T32 DK061296 NIDDK NIH HHS

• albumin
• albuminoids
• hibernation
• positive selection
• vitamin D
• vitamin D-binding protein

Congenital analbuminemia is a rare autosomal recessive disorder manifested by the presence of a very low amount of circulating serum albumin. It is an allelic heterogeneous defect, caused by variety of mutations within the albumin gene in homozygous or compound heterozygous state. Herein we report the clinical and molecular characterization of a new case of congenital analbuminemia diagnosed in a female newborn of consanguineous (first degree cousins) parents from Ankara, Turkey, who presented with a low albumin concentration (< 8 g/L) and severe clinical symptoms.

The albumin gene of the index case was screened by single-strand conformation polymorphism, heteroduplex analysis, and direct DNA sequencing. The effect of the splicing mutation was evaluated by examining the cDNA obtained by reverse transcriptase - polymerase chain reaction (RT-PCR) from the albumin mRNA extracted from proband’s leukocytes.

DNA sequencing revealed that the proband is homozygous, and both parents are heterozygous, for a novel G>A transition at position c.1652+1, the first base of intron 12, which inactivates the strongly conserved GT dinucleotide at the 5′ splice site consensus sequence of this intron. The splicing defect results in the complete skipping of the preceding exon (exon 12) and in a frame-shift within exon 13 with a premature stop codon after the translation of three mutant amino acid residues.

Our results confirm the clinical diagnosis of congenital analbuminemia in the proband and the inheritance of the trait and contribute to shed light on the molecular genetics of analbuminemia.

• DNA and cDNA sequence analysis
• albumin gene
• congenital analbuminemia
• human serum albumin
• splicing mutation

• Amino Acids/metabolism
• Analysis of Variance
• Finland
• Genome-Wide Association Study
• Genotype
• Humans
• Inheritance Patterns/genetics
• Lipid Metabolism/genetics
• Magnetic Resonance Spectroscopy
• Metabolome
• Phenotype
• Polymorphism, Single Nucleotide/genetics
• Quantitative Trait Loci/genetics
• Serum/metabolism

• R01 HL087679 NHLBI NIH HHS
• R01 AA009203 NIAAA NIH HHS
• 1RL1MH083268 NIMH NIH HHS
• 5R01HL087679 NHLBI NIH HHS
• 89061/Z/09/Z Wellcome Trust
• AA-12502 NIAAA NIH HHS
• 098051 Wellcome Trust
• AA-15416 NIAAA NIH HHS
• GR069224 Wellcome Trust
• K02 AA018755 NIAAA NIH HHS
• 090532 Wellcome Trust
• G0500539 Medical Research Council
• R01 AA012502 NIAAA NIH HHS
• Wellcome Trust
• R01 AA015416 NIAAA NIH HHS
• AA-08315 NIAAA NIH HHS
• RL1 MH083268 NIMH NIH HHS
• 089062/Z/09/Z Wellcome Trust
• G0600705 Medical Research Council
• R37 AA012502 NIAAA NIH HHS

Analbuminemia is a rare autosomal recessive disorder manifested by the absence, or severe reduction, of circulating serum albumin (ALB). We report here a new case diagnosed in a 45 years old man of Southwestern Asian origin, living in Switzerland, on the basis of his low ALB concentration (0.9 g/L) in the absence of renal or gastrointestinal protein loss, or liver dysfunction. The clinical diagnosis was confirmed by a mutational analysis of the albumin (ALB) gene, carried out by single-strand conformational polymorphism (SSCP), heteroduplex analysis (HA), and DNA sequencing. This screening of the ALB gene revealed that the proband is homozygous for two mutations: the insertion of a T in a stretch of eight Ts spanning positions c.1289 + 23–c.1289 + 30 of intron 10 and a c.802 G > T transversion in exon 7. Whereas the presence of an additional T in the poly-T tract has no direct deleterious effect, the latter nonsense mutation changes the codon GAA for Glu244 to the stop codon TAA, resulting in a premature termination of the polypeptide chain. The putative protein product would have a length of only 243 amino acid residues instead of the normal 585 found in the mature serum albumin, but no evidence for the presence in serum of such a truncated polypeptide chain could be obtained by two dimensional electrophoresis and western blotting analysis.

• DNA sequence
• analbuminemia
• heteroduplex analysis
• human serum albumin
• single-strand conformation polymorphism

• Asian People/genetics
• Codon, Nonsense
• Exons
• Heteroduplex Analysis
• Humans
• Male
• Middle Aged
• Pathology, Molecular/methods
• Polymorphism, Single-Stranded Conformational
• Sequence Analysis, DNA
• Serum Albumin/deficiency
• Serum Albumin/genetics
• Switzerland

Proteins localized within the same subcellular compartment tend to be functionally associated. This study shows that subcellular localization and network distance between disease-associated proteins provide complementary information explaining patterns of disease comorbidity.

A positive correlation was found between subcellular localization of disease-associated protein pairs and measures of comorbidity.

It was shown that the emergence of phenotypically similar diseases are triggered as a result of molecular connections between disease-causing genes (Oti and Brunner, 2007; Zaghloul and Katsanis, 2010). From a genetics, perspective diseases are associated with certain genes (Goh et al, 2007; Feldman et al, 2008), whereas from a proteomics perspective phenotypically similar diseases are connected via biological modules such as protein–protein interactions (PPIs) or molecular pathways (Lage et al, 2007; Jiang et al, 2008; Wu et al, 2008; Linghu et al, 2009; Suthram et al, 2010). These molecular connections between diseases were observed on the population level as well: diseases connected through molecular connections such as shared genes, PPIs, and metabolic pathways tend to show elevated comorbidity (Rzhetsky et al, 2007; Lee et al, 2008; Zhernakova et al, 2009; Park et al, 2009a, 2009b). While these findings constitute a step toward improving our understanding of the mechanism of disease progression, there are still many more molecule-level connections between disease pairs that need to be explored in order to establish a firmer comorbidity association.

Subcellular localization provides spatial information of proteins in the cell; proteins target subcellular localizations to interact with appropriate partners and form functional complexes in signaling pathways and metabolic processes (Au et al, 2007). Abnormal protein localizations are known to lead to the loss of functional effects in diseases (Luheshi et al, 2008; Laurila and Vihinen, 2009). For example, mis-localizations of nuclear/cytoplasmic transport have been detected in many types of carcinoma cells (Kau et al, 2004). A proper identification of protein subcellular localization can hence be useful in discovering disease-associated proteins (Giallourakis et al, 2005; Calvo and Mootha, 2010). With this understanding, we postulate that disease-associated proteins connected by subcellular localizations could also explain the phenotypic similarities between diseases. Furthermore, such connections may also couple to disease progressions that contribute to multiple disease manifestation, that is, comorbidity.

Protein subcellular localization has been extensively studied through various methods to determine a variety of protein functions. To the best of our knowledge, the connection between diseases and subcellular localizations are yet to be studied systematically. To resolve this we constructed, for the first time, a human Disease-associated Protein and subcellular Localization (DPL) matrix (top panel in Box 1). Our DPL matrix provides the ‘cellular localization map of diseases' that represents the spatial index of diseases in the cell. We found that each disease shows unique characteristics of subcellular localization profile in the DPL matrix. We were interested in determining whether subsets of 1284 human diseases exhibit distinct enrichment profiles across subcellular localizations. We calculated pairwise correlations and performed a hierarchical clustering of the enrichments of the 1284 diseases across 10 different subcellular localizations.

Our DPL matrix revealed that 778 diseases (∼62%, P=1.40 × 10⁻³) are enriched in a single localization and 273 diseases (∼21%, P=3.45 × 10⁻³) are enriched in dual localizations. In the DPL matrix, certain disease-associated proteins are likely to be found in membrane-bounded organelles such as mitochondria, lysosome, and peroxisome, indicating that the mutations of proteins localized to these compartments are connected to the pathophysiological conditions of those organelles. Meanwhile, certain disease-associated proteins in the DPL matrix are enriched in dual localizations, such as extracellular/plasma membrane or endoplasmic reticulum/Golgi. Although these two pairs of subcellular localizations appear to be distinct compartments at first, they are functionally related compartments in close proximity during protein translocation process in the cell, and thus are likely to share interacting protein partners (Gandhi et al, 2006).

Comorbidity represents the co-occurrence of multiple diseases in the same individual (Lee et al, 2008; Hidalgo et al, 2009; Park et al, 2009a). Many comorbid disease pairs have been shown to share common genes in the human disease network. For example, Diabetes and Alzheimer's disease share a risk factor in angiotensin I converting enzyme, and frequently occur together in an individual. In such instances, comorbidity can be partially attributed to the disease connections on the molecular level. To explore the impact of protein subcellular localization on comorbidity, we hypothesized that certain disease pairs could also be connected via subcellular localization by the molecular connections between the disease-associated proteins (bottom panel in Box 1).

We found a positive correlation between subcellular localization similarity and relative risk (Figure 3B, Pearson's correlation coefficient between relative risk and subcellular localization similarity=0.81, P=2.96 × 10⁻⁵). The subcellular localization similarity represents the correlation of subcellular localization profiles between disease pairs. To our surprise, when we compared the relative risk of disease pairs linked via various molecular connections, we found that disease pairs connected by subcellular localization showed a near three-fold higher comorbidity tendency (with link distances equal to 2 or 3) when compared with random pairs (Figure 3E).

We then assessed quantitatively the impact of network distances and subcellular localizations on the comorbidity tendency of disease pairs. We expected the proteins associated with comorbid disease pairs to be located closely in the protein interaction network via fewer links compared with random disease pairs. Indeed, a higher comorbidity tendency was found when two disease-associated proteins were positioned within a shorter distance (gray plots in Figure 3F). Moreover, when subcellular localization information was combined with small network distances, the comorbidity tendency increased dramatically (orange plots in Figure 3F). It suggests that subcellular localization and close network distances, two conceptually distinct molecular connections, contributed synergistically to the comorbidity tendency.

Disease progression is not restricted to the mutation of disease-causing genes, but also affected by molecular connections in ‘disease modules,' resulting in comorbidity (Fraser, 2006; Lee et al, 2008). In this study, for the first time we applied subcellular localization information to elucidate the molecular connections between comorbid diseases. We believe that, based on our finding, our approach helps to define the boundaries of ‘disease modules.' Taken together, integration of diverse molecular connections should improve the molecular level understanding of hitherto unexplained comorbid disease pairs and help us in expanding the scope of our knowledge of the mechanism of human disease progression.

Proteins targeting the same subcellular localization tend to participate in mutual protein–protein interactions (PPIs) and are often functionally associated. Here, we investigated the relationship between disease-associated proteins and their subcellular localizations, based on the assumption that protein pairs associated with phenotypically similar diseases are more likely to be connected via subcellular localization. The spatial constraints from subcellular localization significantly strengthened the disease associations of the proteins connected by subcellular localizations. In particular, certain disease types were more prevalent in specific subcellular localizations. We analyzed the enrichment of disease phenotypes within subcellular localizations, and found that there exists a significant correlation between disease classes and subcellular localizations. Furthermore, we found that two diseases displayed high comorbidity when disease-associated proteins were connected via subcellular localization. We newly explained 7584 disease pairs by using the context of protein subcellular localization, which had not been identified using shared genes or PPIs only. Our result establishes a direct correlation between protein subcellular localization and disease association, and helps to understand the mechanism of human disease progression.

There is accumulating evidence that oxidative stress plays an important role in the pathophysiology of chronic obstructive pulmonary disease (COPD). One current hypothesis is that the increased oxidant burden in these patients is not adequately counterbalanced by the lung antioxidant systems.

To determine the levels of oxidised human serum albumin (HSA) in COPD lung explants and the effect of oxidation on HSA degradation using an ex vivo lung explant model.

Parenchymal lung tissue was obtained from 38 patients (15F/23M) undergoing lung resection and stratified by smoking history and disease using the GOLD guidelines and the lower limit of normal for FEV₁/FVC ratio. Lung tissue was homogenised and analysed by ELISA for total levels of HSA and carbonylated HSA. To determine oxidised HSA degradation lung tissue explants were incubated with either 200 μg/ml HSA or oxidised HSA and supernatants collected at 1, 2, 4, 6, and 24 h and analysed for HSA using ELISA and immunoblot.

When stratified by disease, lung tissue from GOLD II (median = 38.2 μg/ml) and GOLD I (median = 48.4 μg/ml) patients had lower levels of HSA compared to patients with normal lung function (median = 71.9 μg/ml, P < 0.05). In addition the number of carbonyl residues, which is a measure of oxidation was elevated in GOLD I and II tissue compared to individuals with normal lung function (P < 0.05). When analysing smoking status current smokers had lower levels of HSA (median = 43.3 μg/ml, P < 0.05) compared to ex smokers (median = 71.9 μg/ml) and non-smokers (median = 71.2 μg/ml) and significantly greater number of carbonyl residues per HSA molecule (P < 0.05). When incubated with either HSA or oxidised HSA lung tissue explants rapidly degraded the oxidised HSA but not unmodified HSA (P < 0.05).

We report on a reliable methodology for measuring levels of oxidised HSA in human lung tissue and cell culture supernatant. We propose that differences in the levels of oxidised HSA within lung tissue from COPD patients and current smokers provides further evidence for an oxidant/antioxidant imbalance and has important biological implications for the disease.

• Female
• Humans
• Infant
• Mutation
• RNA Splicing
• Serum Albumin/deficiency
• Serum Albumin/genetics

• Adult
• Blood Protein Disorders/congenital
• Blood Protein Disorders/genetics
• Heterozygote
• Humans
• Male
• Mutation
• Polymorphism, Restriction Fragment Length
• Polymorphism, Single-Stranded Conformational
• Serum Albumin/deficiency
• Serum Albumin/genetics

• Adult
• Albumins/deficiency
• Albumins/genetics
• Child, Preschool
• Codon, Nonsense
• Female
• Humans
• Male
• Morocco