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Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface.

Abstract:

The cell-surface activation of pro-matrix metalloproteinase 2 (pro-MMP-2) is considered to be critical for cell migration and invasion. Treatment of human uterine cervical fibroblasts with concanavalin A activates pro-MMP-2 on the cell surface by converting it to the 65-kDa form with a minor form of 45 kDa. However, the 65-kDa MMP-2 was inactivated by tissue inhibitor of metalloproteinases (TIMP)-2 that was bound to the plasma membrane upon concanavalin A treatment. TIMP-2 binds to the plasma...

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Publisher copy:
10.1074/jbc.273.38.24360

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Tanzawa, K More by this author
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Journal:
The Journal of biological chemistry
Volume:
273
Issue:
38
Pages:
24360-24367
Publication date:
1998-09-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:971a3754-50c8-4ed0-a0af-b2396d13a6c4
Source identifiers:
411391
Local pid:
pubs:411391

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