Abstract
Matrix metalloproteinase-3 (MP-3 or stromelysin-1) specifically hydrolyzes the Glu59-Asn60, Pro447-Val448, and Pro544-Ser545 peptide bonds in plasminogen, yielding a 55 kDa NH2-terminal angiostatin-like domain (comprising kringles 1-4), a 14 kDa domain comprising kringle 5, and a 30 kDa domain comprising the serine proteinases domain. The conversion is completely abolished in the presence of the MMP inhibitors EDTA or 1,10-phenanthroline. Biospecific interactions analysis indicates that binding of proMMP-3 and MMP-3 to plasminogen occurs with comparable affinity (KA of 4.7 x 10(6) and 4.1 x 10(6) M-1, respectively) and is mediated via the miniplasminogen moiety (kringle 5 plus the proteinase domain) and via the catalytic domain of MMP-3. Thus, proteolytic cleavage of plasminogen by MMP-3 generates angiostatin-like fragments.
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