Authors:
G Murphy, F Willenbrock, RV Ward, MI Cockett, D Eaton, AJ Docherty
Journal name: 
Biochem J
Citation info: 
283 ( Pt 3):637-641
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.
DOI: 
http://doi.org/10.1042/bj2830637
E-pub date: 
30 Apr 1992
Users with this publication listed: 
Gillian Murphy