MMP15

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.[6]

References
  1. GRCh38: Ensembl release 89: ENSG00000102996 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. Sato H, Tanaka M, Takino T, Inoue M, Seiki M (February 1997). "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. doi:10.1006/geno.1996.4496. PMID 9119382.
  5. Mattei MG, Roeckel N, Olsen BR, Apte SS (February 1997). "Genes of the membrane-type matrix metalloproteinase (MT-MMP) gene family, MMP14, MMP15, and MMP16, localize to human chromosomes 14, 16, and 8, respectively". Genomics. 40 (1): 168–9. doi:10.1006/geno.1996.4559. PMID 9070935.
  6. "Entrez Gene: MMP15".

Further reading
  • Terp GE, Christensen IT, Jørgensen FS (June 2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. doi:10.1080/07391102.2000.10506582. PMID 10949161.
  • Morrison CJ, Overall CM (2006). "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. doi:10.1074/jbc.M603331200. PMID 16825197.
  • Takino T, Sato H, Shinagawa A, Seiki M (1995). "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. doi:10.1074/jbc.270.39.23013. PMID 7559440.
  • Will H, Hinzmann B (1995). "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment". Eur. J. Biochem. 231 (3): 602–8. doi:10.1111/j.1432-1033.1995.tb20738.x. PMID 7649159.
  • Lu YG, Zhou HY, Ding LC, et al. (2006). "[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. PMID 17029196.
  • Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY (2004). "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. doi:10.1074/jbc.M311569200. PMID 14645246.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • d'Ortho MP, Will H, Atkinson S, et al. (1997). "Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases". Eur. J. Biochem. 250 (3): 751–7. doi:10.1111/j.1432-1033.1997.00751.x. PMID 9461298.
  • Buisson-Legendre N, Smith S, March L, Jackson C (2004). "Elevation of activated protein C in synovial joints in rheumatoid arthritis and its correlation with matrix metalloproteinase 2". Arthritis Rheum. 50 (7): 2151–6. doi:10.1002/art.20313. PMID 15248212.
  • Hotary K, Li XY, Allen E, et al. (2006). "A cancer cell metalloprotease triad regulates the basement membrane transmigration program". Genes Dev. 20 (19): 2673–86. doi:10.1101/gad.1451806. PMC 1578694. PMID 16983145.
  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
  • Jung M, Römer A, Keyszer G, et al. (2003). "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. doi:10.1002/pros.10194. PMID 12661033.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Hitchon CA, Danning CL, Illei GG, et al. (2002). "Gelatinase expression and activity in the synovium and skin of patients with erosive psoriatic arthritis". J. Rheumatol. 29 (1): 107–17. PMID 11824946.
  • Sato H, Tanaka M, Takino T, et al. (1997). "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. doi:10.1006/geno.1996.4496. PMID 9119382.
  • The MEROPS online database for peptidases and their inhibitors: M10.015

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