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J Biol Chem. 2000 Aug 25;275(34):26411-5.

TIMP-2 is required for efficient activation of proMMP-2 in vivo.

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  • 1Roswell Park Cancer Institute, Department of Molecular and Cellular Biology, Buffalo, New York 16263, USA.

Abstract

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.

PMID:
10827175
[PubMed - indexed for MEDLINE]
PMCID:
PMC2683068
Free PMC Article
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