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Glutamine-Induced Production and Secretion of Helicobacter pylori ${\gamma}$-Glutamyltranspeptidase at Low pH and Its Putative Role in Glutathione Transport

  • Ki, Mi Ran (Department of Biotechnology and Bioinformatics, College of Science and Technology, Korea University) ;
  • Yun, Na Rae (Department of Biotechnology and Bioinformatics, College of Science and Technology, Korea University) ;
  • Hwang, Se Young (Department of Biotechnology and Bioinformatics, College of Science and Technology, Korea University)
  • Received : 2012.10.15
  • Accepted : 2012.12.12
  • Published : 2013.04.28

Abstract

Helicobacter pylori increased the ${\gamma}$-glutamyltranspeptidase (GGT) production under low-pH (maximal at pH 4) and appropriate $pCO_2$ conditions, while the production of GGT mRNA correlated with increased total enzyme activity. At pH 4, the bacterium augmented enzyme production in the presence of glutamine (~10 mM) in the medium, which predominantly occurred after a 6-min time-lag. Monovalent salts such as NaCl or $NH_4Cl$ facilitated enzymatic activation in acidic solutions of approximately pH 4.5. In addition, glutathione's ${\gamma}$-glutamyl moiety cysteinylglycine appeared to be taken up readily by the intact H. pylori, but not by the one pretreated with a potent GGT inhibitor, acivicin, suggesting that the GGT may partake in glutathione uptake by the cell.

Keywords

References

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