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Enhanced production of matrix metalloproteinases and activation of matrix metalloproteinase 2 (gelatinase A) in human gastric carcinomas

✍ Scribed by Hidehiro Nomura; Noboru Fujimoto; Motoharu Seiki; Masayoshi Mai; Yasunori Okada

Publisher: John Wiley and Sons
Year: 1996
Tongue: French
Weight: 831 KB
Volume: 69
Category: Article
ISSN: 0020-7136
DOI: 10.1002/(sici)1097-0215(19960220)69:1<9::aid-ijc3>3.0.co;2-8

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✦ Synopsis

We examined the production and tissue localization of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in gastric carcinoma tissues. MMP-I (tissue collagenase), MMP-9 (gelatinase B) and TIMP-2 were immunolocalized in carcinoma cells and MMP-2 (gelatinase A) on tumor cell membranes, whereas no or little immunostaining for MMP-3 (stromelysin-I) and TIMP-I was seen in carcinoma cells. Stro-ma1 cells in carcinoma tissue were also positively stained for these MMPs and TIMPs. MMP-2 immunostaining was observed exclusively on advanced gastric carcinoma cells and correlated with vascular invasion by tumor cells. Sandwich enzyme immunoassays revealed enhanced production of MMP-I, MMP-2, MMP-3. MMP-9 and TIMP-I by carcinoma tissues. Gelatinolytic activities were significantly higher in carcinoma samples than in normal controls. Using gelatin zymography, active forms of MMP-2 and MMP-9 were more frequently detected in carcinoma tissue, and the activation rate of the zymogen of MMP-2 (proMMP-2). but not that of proMMP-9, correlated well with degree of local invasion and lymphatic permeation. Our data indicate an enhanced production of 4 MMPs in gastric carcinoma tissue and sunnest that activation of pro-MMP-2 may be a key step for spreadEg of

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