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  • Title: Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
    Author: Lee SJ, Jang JW, Kim YM, Lee HI, Jeon JY, Kwon YG, Lee ST.
    Journal: FEBS Lett; 2002 May 22; 519(1-3):147-52. PubMed ID: 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.
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