Ricci V, Giannouli M, Romano M, Zarrilli R. Helicobacter pylori gamma-glutamyl transpeptidase and its pathogenic role. World J Gastroenterol 2014; 20(3): 630-638 [PMID: 24574736 DOI: 10.3748/wjg.v20.i3.630]
Corresponding Author of This Article
Raffaele Zarrilli, MD, PhD, Department of Public Health, Hygiene Section, University of Naples “Federico II”, 80131 Naples, Italy. rafzarri@unina.it
Research Domain of This Article
Microbiology
Article-Type of This Article
Topic Highlight
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Author contributions: All authors contributed to this manuscrip.
Supported by Italian Ministry for University and Research (Progetto di Ricerca di Interesse Nazionale No. 2009A37C8C_002, to Ricci V); Fondazione Cariplo Grant (No. 2011-0485 to Ricci V); Second University of Naples (CIRANAD to Romano M); and University of Naples “Federico II” (Fondo d’Ateneo per la Ricerca; to Zarrilli R)
Correspondence to: Raffaele Zarrilli, MD, PhD, Department of Public Health, Hygiene Section, University of Naples “Federico II”, 80131 Naples, Italy. rafzarri@unina.it
Telephone: +39-81-7463026 Fax: +39-81-7463352
Received: October 2, 2013 Revised: October 30, 2013 Accepted: November 28, 2013 Published online: January 21, 2014
Abstract
Helicobacter pylori (H. pylori) gamma-glutamyl transpeptidase (GGT) is a bacterial virulence factor that converts glutamine into glutamate and ammonia, and converts glutathione into glutamate and cysteinylglycine. H. pylori GGT causes glutamine and glutathione consumption in the host cells, ammonia production and reactive oxygen species generation. These products induce cell-cycle arrest, apoptosis, and necrosis in gastric epithelial cells. H. pylori GGT may also inhibit apoptosis and induce gastric epithelial cell proliferation through the induction of cyclooxygenase-2, epidermal growth factor-related peptides, inducible nitric oxide synthase and interleukin-8. H. pylori GGT induces immune tolerance through the inhibition of T cell-mediated immunity and dendritic cell differentiation. The effect of GGT on H. pylori colonization and gastric persistence are also discussed.
Core tip: In this review, we focus on the biochemical features and physiological role of Helicobacter pylori (H. pylori) gamma-glutamyl transpeptidase and analyze the mechanisms through which gamma-glutamyl transpeptidase affects H. pylori gastric colonization, persistence, immune tolerance and damage to the gastric mucosa.
