Biology:MMP15

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.

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 proenzymes 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; members of this subfamily can be anchored to the extracellular membrane by either a transmembrane domain or glycophosphatidylinositol linkage, suggesting that these proteins are expressed at the cell surface rather than secreted in a soluble form.

Further reading

• "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. June 2000. doi:10.1080/07391102.2000.10506582. PMID 10949161. 
• "TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains.". J. Biol. Chem. 281 (36): 26528–39. 2006. doi:10.1074/jbc.M603331200. PMID 16825197. 
• "Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family.". J. Biol. Chem. 270 (39): 23013–20. 1995. doi:10.1074/jbc.270.39.23013. PMID 7559440. 
• "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment.". Eur. J. Biochem. 231 (3): 602–8. 1995. doi:10.1111/j.1432-1033.1995.tb20738.x. PMID 7649159. 
• "[Analysis of differential expression genes related to different metastasis potential of adenoid cystic carcinoma using restriction fragments differential display PCR]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi 23 (5): 505–10. 2006. PMID 17029196. 
• "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells.". J. Biol. Chem. 279 (6): 4260–8. 2004. doi:10.1074/jbc.M311569200. PMID 14645246. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases.". Eur. J. Biochem. 250 (3): 751–7. 1997. doi:10.1111/j.1432-1033.1997.00751.x. PMID 9461298. 
• "Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2.". Arthritis Rheum. 50 (7): 2151–6. 2004. doi:10.1002/art.20313. PMID 15248212. 
• "A cancer cell metalloprotease triad regulates the basement membrane transmigration program.". Genes Dev. 20 (19): 2673–86. 2006. doi:10.1101/gad.1451806. PMID 16983145. 
• "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
• "mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue.". Prostate 55 (2): 89–98. 2003. doi:10.1002/pros.10194. PMID 12661033. 
• "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Gelatinase expression and activity in the synovium and skin of patients with erosive psoriatic arthritis.". J. Rheumatol. 29 (1): 107–17. 2002. PMID 11824946. 
• "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization.". Genomics 39 (3): 412–3. 1997. doi:10.1006/geno.1996.4496. PMID 9119382. 

External links

• The MEROPS online database for peptidases and their inhibitors: M10.015

This article incorporates text from the United States National Library of Medicine, which is in the public domain.