Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
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.[1]References
- Endostatin binds to the catalytic domain of matrix metalloproteinase-2. Lee, S.J., Jang, J.W., Kim, Y.M., Lee, H.I., Jeon, J.Y., Kwon, Y.G., Lee, S.T. FEBS Lett. (2002) [Pubmed]
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