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FEBS Lett ; 519(1-3): 147-52, 2002 May 22.
Article in English | MEDLINE | ID: mdl-12023034

ABSTRACT

We previously reported that endostatin inhibits endothelial and tumor cellular invasion by blocking activation and catalytic activity of matrix metalloproteinase (MMP)-2. Here we have examined the domain of proMMP-2 responsible for the binding of endostatin using surface plasmon resonance. ProMMP-2 and proMMP-2deltaHP lacking the hinge and hemopexin-like (HP) domains bound little to the immobilized endostatin. The active MMP-2 and MMP-2deltaHP, but not the HP domain of MMP-2, bound to endostatin at similar levels. In addition, preincubation of MMP-2 and MMP-2deltaHP with the MMP inhibitor actinonin, which binds to the active site of MMP-2, abolished their bindings to endostatin. These results indicate that endostatin binds to neither the latent proMMP-2 nor the HP domain but to the catalytic domain of MMP-2.


Subject(s)
Collagen/metabolism , Matrix Metalloproteinase 2/metabolism , Peptide Fragments/metabolism , Animals , Catalytic Domain/physiology , Cell Line , Collagen/genetics , Endostatins , Enzyme Inhibitors/pharmacology , Enzyme Precursors/antagonists & inhibitors , Enzyme Precursors/genetics , Enzyme Precursors/metabolism , Gelatinases/antagonists & inhibitors , Gelatinases/genetics , Gelatinases/metabolism , Humans , Hydroxamic Acids/pharmacology , Matrix Metalloproteinase Inhibitors , Metalloendopeptidases/antagonists & inhibitors , Metalloendopeptidases/genetics , Metalloendopeptidases/metabolism , Mice , Peptide Fragments/genetics , Protein Binding/physiology , Protein Structure, Tertiary/physiology , Sequence Deletion , Spodoptera , Surface Plasmon Resonance , Tissue Inhibitor of Metalloproteinase-2/genetics , Tissue Inhibitor of Metalloproteinase-2/metabolism
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