Journal of Microbiology and Biotechnology

  • 제23권4호
  • /
  • Pages.467-472
  • /
  • 2013
  • /
  • 1017-7825(pISSN)
  • /
  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지
DOI QR코드

DOI QR Code

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)
  • 투고 : 2012.10.15
  • 심사 : 2012.12.12
  • 발행 : 2013.04.28
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

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.

키워드

참고문헌

  1. Anderson, M. E. and A. Meister. 1986. Inhibition of γ-glutamyl transpeptidase and induction of glutathionuria by γ-glutamyl amino acids. Proc. Natl. Acad. Sci. USA 83: 5029-5032. https://doi.org/10.1073/pnas.83.14.5029
  2. Atherton, J. C. 2006. The pathogenesis of Helicobacter pyloriinduced gastro-duodenal diseases. Annu. Rev. Pathol. 1: 63-96. https://doi.org/10.1146/annurev.pathol.1.110304.100125
  3. Berg, J. M., J. L. Tymoczko, and L. Stryer. 2007. The biosynthesis of amino acids, pp. 679-708. Biochemistry, 6th Ed. Freeman and Company, New York.
  4. Blaser, M. J. 1999. Where does Helicobacter pylori come from and why is it going away? J. Am. Med. Assoc. 282: 2260-2262. https://doi.org/10.1001/jama.282.23.2260
  5. Bumann, D., S. Aksu, M. Wendland, K. Janek, U. Zimny- Arndt, N. Sabarth, et al. 2002. Proteome analysis of secreted proteins of the gastric pathogen Helicobacter pylori. Infect. Immun. 70: 3396-3403. https://doi.org/10.1128/IAI.70.7.3396-3403.2002
  6. Chevalier, C., J. M. Thiberge, R. L. Ferrero, and A. Labigne. 1999. Essential role of Helicobacter pylori γ-glutamyltranspeptidase for the colonization of the gastric mucosa of mice. Mol. Microbiol. 31: 1359-1372. https://doi.org/10.1046/j.1365-2958.1999.01271.x
  7. Choi, K. M., W. J. Lim, J. K. Park, and S. Y. Hwang. 2001. Presumptive mechanisms of peptic ulceration by Helicobacter pylori VacA involving mucoprotease and CagA. Mol. Cells 11: 312-320.
  8. Choi, K. M., J. K. Park, and S. Y. Hwang. 2003. Pathogenetic impact of vacuolar degeneration by accelerated transport of Helicobacter pylori VacA. J. Microbiol. Biotechnol. 13: 666-672.
  9. Chu, S., S. Tanaka, J. D. Kaunitz, and M. H. Montrose. 1999. Dynamic regulation of gastric surface pH by luminal pH. J. Clin. Invest. 103: 605-612. https://doi.org/10.1172/JCI5217
  10. Courtay, C., T. Oster, F. Michelet, A. Visvikis, M. Diederich, M. Wellman, and G. Siest. 1992. Gamma-glutamyltransferase: Nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous $\gamma$-glutamyltransferase polypeptide in human tissues. Biochem. Pharm. 43: 2527-2533. https://doi.org/10.1016/0006-2952(92)90140-E
  11. Cover, T. L. and M. J. Blaser. 1992. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J. Biol. Chem. 267: 10570-10575.
  12. Doig, P., B. L. de Jonge, R. A. Alm, E. D. Brown, M. Uria- Nickelsen, B. Noonan, et al. 1999. Helicobacter pylori physiology predicted from genomic comparison of two strains. Microbiol. Mol. Biol. Rev. 63: 675-707.
  13. Ellman, G. L. 1959. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82: 70-77. https://doi.org/10.1016/0003-9861(59)90090-6
  14. Gong, M. and B. Ho. 2004. Prominent role of $\gamma$-glutamyltranspeptidase on the growth of Helicobacter pylori. World J. Gastroenterol. 10: 2994-2996.
  15. Grunwald, S., R. Krause, M. Bruch, T. Henle, and M. Brandsch. 2006. Transepithelial flux of early and advanced glycation compounds across Caco-2 cell monolayers and their interaction with intestinal amino acid and peptide transport systems. Br. J. Nutr. 95: 1221-1228. https://doi.org/10.1079/BJN20061793
  16. Hu, L. T. and H. L. Mobley. 1990. Purification and N-terminal analysis of urease from Helicobacter pylori. Infect. Immun. 58: 992-998.
  17. Hwang, S. Y., W. D. Kingsbury, N. M. Hall, D. R. Jakas, G. L. Dunn, and C. Gilvarg. 1986. Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine. Anal. Biochem. 154: 552-558. https://doi.org/10.1016/0003-2697(86)90028-X
  18. Ki, M. R., S. K. Yun, K. M. Choi, and S. Y. Hwang. 2011. Identification and characterization of the acid phosphatase HppA in Helicobacter pylori. J. Microbiol. Biotechnol. 21: 483-493. https://doi.org/10.4014/jmb.1101.01017
  19. Ki, M. R., S. K. Yun, K. M. Choi, and S. Y. Hwang. 2003. Potential and significance of ammonium production from Helicobacter pylori. J. Microbiol. Biotechnol. 13: 673-679.
  20. Kingsbury, W. D., J. C. Boehm, D. Perry, and C. Gilvarg. 1984. Portage of various compounds into bacteria by attachment to glycine residues in peptides. Proc. Natl. Acad. Sci. USA 81: 4573-4576. https://doi.org/10.1073/pnas.81.14.4573
  21. Leduc, D., J. Gallaud, K. Stingl, and H. de Reuse. 2010. Coupled amino acid deamidase-transport systems essential for Helicobacter pylori colonization. Infect. Immun. 78: 2782- 2792. https://doi.org/10.1128/IAI.00149-10
  22. Leduc, D., J. Gallaud, K. Stingl, and H. de Reuse. 2010. Coupled amino acid deamidase-transport systems essential for Helicobacter pylori colonization. Infect. Immun. 78: 2782-2792. https://doi.org/10.1128/IAI.00149-10
  23. Marcus, E. A., A. P. Moshfegh, G. Sachs, and D. R. Scott. 2005. The periplasmic alpha-carbonic anhydrase activity of Helicobacter pylori is essential for acid acclimation. J. Bacteriol. 187: 729-738. https://doi.org/10.1128/JB.187.2.729-738.2005
  24. Marshall, B. J. and J. R. Warren. 1984. Unidentified curved bacilli in the stomach of patients with gastritis and peptic ulceration. Lancet 1: 1311-1315.
  25. McGovern, K. J., T. G. Blanchard, J. A. Gutierrez, S. J. Czinn, S. Krakowka, and P. Youngman. 2001. $\gamma$-Glutamyltransferase is a Helicobacter pylori virulence factor but is not essential for colonization. Infect. Immun. 69: 4168-4173.
  26. Mount, D. B. and M. F. Romero. 2004. The SLC26 gene family of multifunctional anion exchangers. Pflugers Arch. 447: 710-721. https://doi.org/10.1007/s00424-003-1090-3
  27. Orlowski, M. and A. Meister. 1963. $\gamma$-Glutamyl-p-nitroanilide: A new convenient substrate for determination and study of Land D-$\gamma$-glutamyltranspeptidase activities. Biochim. Biophys. Acta 73: 679-681. https://doi.org/10.1016/0926-6569(63)90197-4
  28. Reitzer, L. J. 1996. Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and Dalanine, pp. 302-320. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanic, M. Schaechter, and H. E. Umbarger (eds.). E. coli and Salmonella Typhimurium: Cellular and Molecular Biology. American Society for Microbiology, Washington, DC.
  29. Rektorschek, M., D. Weeks, G. Sachs, and K. Melchers. 1998. Influence of pH on metabolism and urease activity of Helicobacter pylori. Gastroenterology 115: 628-641. https://doi.org/10.1016/S0016-5085(98)70142-8
  30. Rokkas, T., D. Pistiolas, P. Sechopoulos, I. Robotis, and G. Margantinis. 2007. The long-term impact of Helicobacter pylori eradication on gastric histology: A systematic review and metaanalysis. Helicobacter 12: 32-38. https://doi.org/10.1111/j.1523-5378.2007.00563.x
  31. Schneider, M., I. W. Marison, and U. von Stockar. 1996. The importance of ammonia in mammalian cell culture. J. Biotechnol. 46: 161-185. https://doi.org/10.1016/0168-1656(95)00196-4
  32. Schulz, J. B., J. Lindenau, J. Seyfried, and J. Dichgans. 2000. Glutathione, oxidative stress and neurodegeneration. Eur. J. Biochem. 267: 4904-4911. https://doi.org/10.1046/j.1432-1327.2000.01595.x
  33. Shibayama, K., J. Wachino, Y. Arakawa, M. Saidijam, N. G. Rutherford, and P. J. Henderson. 2007. Metabolism of glutamine and glutathione via $\gamma$-glutamyltranspeptidase and glutamate transport in Helicobacter pylori: Possible significance in the pathophysiology of the organism. Mol. Microbiol. 64: 396-406. https://doi.org/10.1111/j.1365-2958.2007.05661.x
  34. Wachino, J., K. Shibayama, S. Suzuki, K. Yamane, S. Mori, and Y. Arakawa. 2010. Profile of expression of Helicobacter pylori $\gamma$-glutamyltranspeptidase. Helicobacter 15: 184-192. https://doi.org/10.1111/j.1523-5378.2010.00755.x

피인용 문헌

  1. The histone‐like protein HU has a role in gene expression during the acid adaptation response in Helicobacter pylori vol.22, pp.4, 2013, https://doi.org/10.1111/hel.12381