MMP14
Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.[1]
Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.
However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted.
"This protein activates MMP2 protein, and this activity may be involved in tumor invasion."[2]
Interactions
MMP14 has been shown to interact with TIMP2.[3]
See also
References
- ↑ Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M (Jul 1994). "A matrix metalloproteinase expressed on the surface of invasive tumour cells". Nature 370 (6484): 61–5. doi:10.1038/370061a0. PMID 8015608.
- ↑ "Entrez Gene: MMP14 matrix metallopeptidase 14 (membrane-inserted)".
- ↑ Zucker S, Drews M, Conner C, Foda HD, DeClerck YA, Langley KE, Bahou WF, Docherty AJ, Cao J (Jan 1998). "Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)". J. Biol. Chem. 273 (2): 1216–22. doi:10.1074/jbc.273.2.1216. PMID 9422789.
Further reading
External links
- The MEROPS online database for peptidases and their inhibitors: M10.014
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| | 1bqq: CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX |
| 1buv: CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX |
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