| First Author | Wang Z | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 34 | Pages | 26411-5 |
| PubMed ID | 10827175 | Mgi Jnum | J:64001 |
| Mgi Id | MGI:1888586 | Doi | 10.1074/jbc.M001270200 |
| Citation | Wang Z, et al. (2000) TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem 275(34):26411-5 |
| abstractText | Matrix metalloproteinases (MMPs) are synthesized as latent proenzymes. A proteolytic cleavage event involving processing of the cysteine-rich N-terminal propeptide is required for their full activation. Previous in vitro studies indicated that activation of proMMP-2 can occur through formation of a trimolecular complex between MMP-14, TIMP-2, and proMMP-2 at the cell surface. Using TIMP-2-deficient mice and cells derived from them, TIMP-2 was shown to be required for efficient proMMP-2 activation both in vivo and in vitro. The requirement for TIMP-2 was not cell-autonomous as exogenously added TIMP-2 could restore activation of proMMP-2 to TIMP-2-deficient cells. Mutant mice were overtly normal, viable, and fertile on the C57BL/6 background, indicating that both TIMP-2 and activated proMMP-2 are dispensable for normal development. |
