Membrane-Type-2 Matrix Metalloproteinase Can Initiate the Processing of Progelatinase A and is Regulated by the Tissue Inhibitors of Metalloproteinases
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1997.t01-1-00653.x/fullpdf
Reference23 articles.
1. Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases.
2. Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes
3. Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2
4. Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex
5. The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
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