Open AccessMembrane‐Type‐2 Matrix Metalloproteinase Can Initiate the Processing of Progelatinase A and is Regulated by the Tissue Inhibitors of Metalloproteinases
Author(s) -
Butler Georgina S.,
Will Horst,
Atkinson Susan J.,
Murphy Gillian
Publication year - 1997
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1997.t01-1-00653.x
Subject(s) - matrix metalloproteinase , metalloproteinase , matrix (chemical analysis) , chemistry , activator (genetics) , tissue inhibitor of metalloproteinase , cell , microbiology and biotechnology , biochemistry , biology , gene , chromatography
Membrane‐type‐1 matrix metalloproteinase has been identified as an activator of the matrix metalloproteinase progelatinase A at cell surfaces. We report here that a soluble active form of membrane‐type‐2 matrix metalloproteinase can also process progelatinase A in a comparable fashion to the type‐1 at rates which are dependent on the concentration of the proenzyme. Activation is inhibited by tissue inhibitors of metalloproteinases TIMP‐2 and TIMP‐3, but only partially by TIMP‐1. These results suggest that cellular activation of progelatinase A may be initiated by different members of the membrane‐type matrix metalloproteinase family depending on tissue distribution.