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.
^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". Genomics39 (3): 412–3. doi:10.1006/geno.1996.4496. PMID9119382.
^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". Genomics40 (1): 168–9. doi:10.1006/geno.1996.4559. PMID9070935.
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. PMID10949161.
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. PMID16825197.
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. PMID7559440.
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 Zhi23 (5): 505–10. PMID17029196.CS1 maint: Explicit use of et al. (link)
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. PMID14645246.
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. PMID9461298.CS1 maint: Explicit use of et al. (link)
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. PMID15248212.
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.". Prostate55 (2): 89–98. doi:10.1002/pros.10194. PMID12661033.CS1 maint: Explicit use of et al. (link)
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. PMID11824946.CS1 maint: Explicit use of et al. (link)
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.". Genomics39 (3): 412–3. doi:10.1006/geno.1996.4496. PMID9119382.CS1 maint: Explicit use of et al. (link)