Significance of cell-surface expression of matrix metalloproteinases and their inhibitors on gastric epithelium and infiltrating mucosal lymphocytes in progression of helicobacter pylori-associated gastritis

References

• Curran S, Murray GI. Matrix metalloproteinases: molecular aspects of their roles in tumor invasion and metastasis. Eur J Cancer 2000;36:1621–30.
   PubMed Web of Science ®Google Scholar
• Seiki M, Yana I. Role of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis. Cancer Sci 2003;94:569–74.
   PubMed Web of Science ®Google Scholar
• Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, et al. A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 1994;370:2747–53.
   Google Scholar
• Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J Biol Chem 1996;271:30375–80.
   PubMed Web of Science ®Google Scholar
• Liu YE, Wang M, Greene J, Su J, Ullrich S, Li H, et al. Preparation and characterization of recombinant tissue inhibitor of metalloproteinase 4 (TIMP-4). J Biol Chem 1997;272:20479–83.
   PubMed Web of Science ®Google Scholar
• Blaser MJ. Hypotheses on the pathogenesis and natural history of Helicobacter pylori-induced inflammation. Gastroenterology 1992;102:720–7.
   PubMed Web of Science ®Google Scholar
• Wagner S, Beil W, Westermann J, Logan RPH, Bock CT, Trautwein C, et al. Regulation of gastric epithelial cell growth by Helicobacter pylori: evidence for a major role of apoptosis. Gastroenterology 1997;113:1836–47.
   PubMed Web of Science ®Google Scholar
• Mori N, Sato H, Hayashibara T, Senba M, Geleziunas R, Wada A, et al. Helicobacter pylori induces matrix metalloproteinase-9 through activation of nuclear factor κB. Gastroenterology 2003; 124:988–92.
   Google Scholar
• Bebb JR, Letley DP, Thomas RJ, Aviles F, Collins HM, Watson SA, et al. Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner. Gut 2003;52: 1408–13.
   Google Scholar
• Crawford HC, Krishna US, Israel DA, Matrisian LM, Washington MK, Peek RM, Jr. Helicobacter pylori strain-selective induction of matrix metalloproteinase-7 in vitro and within gastric mucosa. Gastroenterology 2003;125: 1125–36.
   Google Scholar
• Koyama S. Apoptotic depletion of infiltrating mucosal lymphocytes associated with Fas ligand expression by Helicobacter pylori-infected gastric mucosal epithelium: human glandularstomach as a site of immune privilege. Dig Dis Sci 2000;45:773–80.
   PubMedGoogle Scholar
• Koyama S. Flow cytometric measurement of tumor necrosis factor-related apoptosis inducing ligand and its receptors in gastric epithelium and infiltrating mucosal lymphocytes in Helicobacter pylori-associated gastritis. J Gastroenterol Hepatol 2003;18:763–70.
   PubMedGoogle Scholar
• Pender SLF, Tickle SP, Docherty AJP, Howie D, Wathen NC, MacDonald TT. A major role for matrix metalloproteinases in T cell injury in the gut. J Immunol 1997;158:1582–90.
   PubMed Web of Science ®Google Scholar
• Salmela MT, MacDonald TT, Black D, Irvine B, Zhuma T, Saarialho-Kere U, et al. Upregulation of matrix metalloproteinases in a model of T cell mediated tissue injury in the gut: analysis by gene array and in situ hybridisation. Gut 2002;51: 540–7.
   Google Scholar
• Koyama S, Maruyama T, Adachi S, Nozue M. Expression of costimulatory molecules, B7–1 and B7–2 on human gastric carcinoma. J Cancer Res Clin Oncol 1998;124:383–8.
   PubMedGoogle Scholar
• Koyama S, Maruyama T, Adachi S. Expression of epidermal growth factor receptor and CD44 splicing variants sharing exons 6 and 9 on gastric and esophageal carcinomas: a two-color flow-cytometric analysis. J Cancer Res Clin Oncol 1999;125: 47–54.
   Google Scholar
• Koyama S, Koike N, Adachi S. Fas receptor counterattack against tumor-infiltrating lymphocytes in vivo as a mechanism of immune escape by gastric carcinoma. J Cancer Res Clin Oncol 2001;127:20–6.
   Google Scholar
• Koyama S, Koike N, Adachi S. Expression of TNF-related apoptosis inducing ligand (TRAIL) and its receptors in gastric carcinoma and tumor-infiltrating lymphocytes: a possible mechanism of immune evasion of the tumor. J Cancer Res Clin Oncol 2002;128:73–9.
   Google Scholar
• Koyama S. Differential expression of intracellular apoptotic signaling molecules in tumor and tumor-infiltrating lymphocytes during the development of invasion and/or metastasis of gastric carcinoma. Dig Dis Sci 2003;48:2290–300.
   PubMed Web of Science ®Google Scholar
• Satoh K, Kimura K, Taniguchi Y, Kihara K, Taskimoto T, Saifuku K, et al. Biopsy sites suitable for the diagnosis of Helicobacter pylori infection and assessment of the extent of atrophic gastritis. Am J Gastroenterol 1998;93:569–73.
   PubMed Web of Science ®Google Scholar
• Dixon MF, Genta RM, Yardley JH, Correa P. Classification and grading of gastritis. The updated Sydney System. Am J Surg Pathol 1996;20:1161–81.
   PubMed Web of Science ®Google Scholar
• Fujimoto N, Mouri N, Iwata K, Ohuchi E, Okada Y, Hayakawa T. A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 2 (72-kDa gelatinase/type IV collagenase) using monoclonal antibodies. Clin Chim Acta 1993;221:91–103.
   PubMed Web of Science ®Google Scholar
• Ohuchi E, Azumano I, Yoshida S, Iwata K, Okada Y. A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 7 (matrilysin) using monoclonal antibodies. Clin Chim Acta 1996;244: 181–98.
   Google Scholar
• Fujimoto N, Zhang J, Iwata K, Shinya T, Okada Y, Hayakawa T. A one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinase-2 using monoclonal antibodies. Clin Chim Acta 1993;220:31–45.
   PubMed Web of Science ®Google Scholar
• Nomura H, Fujimoto N, Seiki M, Mai M, Okada Y. Enhanced production of matrix metalloproteinases and activation of matrix metalloproteinase-2 (gelatinase A) in human gastric carcinomas. Int J Cancer (Pred Oncol) 1996;69: 9–16.
   Google Scholar
• Honda M, Mori M, Ueo H, Sugimachi K, Akiyoshi T. Matrix metalloproteinase-7 expression in gastric carcinoma. Gut 1996; 39:444–8.
   Google Scholar
• Murray GI, Duncan ME, Melvin WT, Fothergill JE. Matrix metalloproteinases and their inhibitors in gastric cancer. Gut 1998;43:791–7.
   PubMed Web of Science ®Google Scholar
• Yamashita K, Azumano I, Mai M, Okada Y. Expression and tissue localization of matrix metalloproteinase 7 (matrilysin) in human gastric carcinomas. Implications for vessel invasion and metastasis. Int J Cancer (Pred Oncol) 1998;79:187–94.
   Google Scholar
• Liu XP, Kawauchi S, Oga A, Tsushima K, Tsushima M, Furuya T, et al. Prognostic significance of matrix metalloproteinase-7 (MMP-7) expression at the invasive front in gastric carcinoma. Jpn J Cancer Res 2002;95:291–5.
   Google Scholar
• Strongin AY, Collier I, Bannikov G, Marmer BL, Grants GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteinase. J Biol Chem 1995;270:5331–8.
   Google Scholar
• Kinoshita T, Sato H, Okada A, Ohuchi E, Imai K, Okada Y, et al. TIMP-2 promotes activation of progelatinase A by membranetype 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 1998;273:16088–103.
   Google Scholar
• Itoh Y, Ito A, Iwata K, Tanzawa K, Mori Y, Nagase H. Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface. J Biol Chem 1998;273:24360–7.
   PubMed Web of Science ®Google Scholar
• Shoufuda K, Moriyama K, Nishihashi A, Higashi S, Mizushima H, Yasumitsu H, et al. Role of tissue inhibitor of metalloproteinnases-2 (MMP-2) in regulation of pro-gelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells. J Biochem 1998;124:462–70.
   PubMedGoogle Scholar
• Wang Z, Juttermann, Soloway PD. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem 2000; 275:26411–5.
   PubMed Web of Science ®Google Scholar
• Itoh Y, Takamura A, Ito N, Maru Y, Sato H, Suenaga N, et al. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 2001;20:4782–93.
   PubMed Web of Science ®Google Scholar
• Baragi VM, Fliszar CJ, Conroy MC, Ye Q-Z, Shipley JM, Welgus HG. Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit compromised binding affinities as compared to fill-length stromelysin. J Biol Chem 1994;269:12692–7.
   Google Scholar