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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

Overview
Journal Biochem J
Specialty Biochemistry
Date 1992 May 1
PMID 1317162
Citations 50
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Abstract

Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.

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