Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9)
BC Patterson, QXA Sang - Journal of Biological Chemistry, 1997 - ASBMB
Angiostatin is one of the most potent inhibitors of angiogenesis. Reports have shown that
metalloelastase, pancreas elastase, plasmin reductase, and plasmin convert plasminogen
to angiostatin. However, the cleavage sites of plasminogen by those enzymes have not
been determined. Here we demonstrate that two members of the human matrix
metalloproteinase (MMP) family, matrilysin (MMP-7) and gelatinase B/type IV collagenase
(MMP-9), hydrolyze human plasminogen to generate angiostatin fragments. The cleavage …
metalloelastase, pancreas elastase, plasmin reductase, and plasmin convert plasminogen
to angiostatin. However, the cleavage sites of plasminogen by those enzymes have not
been determined. Here we demonstrate that two members of the human matrix
metalloproteinase (MMP) family, matrilysin (MMP-7) and gelatinase B/type IV collagenase
(MMP-9), hydrolyze human plasminogen to generate angiostatin fragments. The cleavage …
