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(Received for publication, September 8, 1997)
From the Department of Chemistry, Florida State University,
Tallahassee, Florida 32306-4390
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 sites have
been determined. The 58-kDa bands derived from plasminogen by MMP-7 and
MMP-9 both have the N-terminal sequence KVYLSEXKTG, which
corresponds to that of angiostatin. This N terminus is identical to
that of the starting plasminogen itself and corresponds to residues
97-106 of prepro-plasminogen. The 42- and 38-kDa bands generated by
MMP-7 both have the N-terminal sequence VVLLPNVETP, which corresponds
to the amino acid sequence 467-476 of prepro-plasminogen, between
kringle domain 4 and 5. MMP-9 cleaves plasminogen to generate a 42-kDa
fragment with the N-terminal sequence PVVLLPNVE, 1 residue upstream of
the MMP-7 cleavage site. These results indicate that MMP-7 and MMP-9
may regulate new blood vessel formation by cleaving plasminogen and
generating angiostatin molecules.
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