| First Author | Lee SJ | Year | 2002 |
| Journal | FEBS Lett | Volume | 519 |
| Issue | 1-3 | Pages | 147-52 |
| PubMed ID | 12023034 | Mgi Jnum | J:76743 |
| Mgi Id | MGI:2180231 | Doi | 10.1016/s0014-5793(02)02742-4 |
| Citation | Lee SJ, et al. (2002) Endostatin binds to the catalytic domain of matrix metalloproteinase-2. FEBS Lett 519(1-3):147-52 |
| abstractText | 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. |
