Alternative titles; symbols
HGNC Approved Gene Symbol: MMP15
Cytogenetic location: 16q21 Genomic coordinates (GRCh38): 16:58,025,754-58,046,901 (from NCBI)
Matrix metalloproteinases (MMPs) are zinc-binding endopeptidases that degrade various components of the extracellular matrix. They have been implicated in normal and pathologic processes including tissue remodeling, wound healing, angiogenesis, and tumor invasion. MMPs have different substrate specificities and are encoded by different genes.
Will and Hinzmann (1995) isolated a cDNA encoding a novel MMP (MMP15) from a human lung cDNA library. The MMP15 cDNA encodes a 669-amino acid protein that has the typical structural features of an MMP. In addition, it contains a predicted transmembrane segment at the C terminus. MMP15 shares 73.9% sequence similarity with MMP14 (600754), a membrane-localized MMP that also contains a C-terminal transmembrane segment. Takino et al. (1995) proposed that the membrane-type MMPs (see also MMP16 602262 and MMP17 602285) are a subclass in the MMP family since the other members lack a C-terminal transmembrane domain and are secreted as soluble forms. Will and Hinzmann (1995) showed by immunoblotting that MMP15-specific antibodies detect a 72-kD protein in lung cell surface membranes, suggesting that MMP15 is membrane-bound. They demonstrated by Northern blotting that MMP15 is widely expressed as a 3.6-kb transcript, with highest levels in liver, placenta, testis, colon, and intestine.
Mattei et al. (1997) mapped the MMP15 gene to chromosome 16q13-q21 by isotopic in situ hybridization. Sato et al. (1997) used fluorescence in situ hybridization to localize the MMP15 gene to 16q12.2-q21.
Mattei, M.-G., Roeckel, N., Olsen, B. R., Apte, S. S. 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: 168-169, 1997. [PubMed: 9070935] [Full Text: https://doi.org/10.1006/geno.1996.4559]
Sato, H., Tanaka, M., Takino, T., Inoue, M., Seiki, M. 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: 412-413, 1997. [PubMed: 9119382] [Full Text: https://doi.org/10.1006/geno.1996.4496]
Takino, T., Sato, H., Shinagawa, A., Seiki, M. 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: 23013-23020, 1995. [PubMed: 7559440] [Full Text: https://doi.org/10.1074/jbc.270.39.23013]
Will, H., Hinzmann, B. cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Europ. J. Biochem. 231: 602-608, 1995. [PubMed: 7649159] [Full Text: https://doi.org/10.1111/j.1432-1033.1995.tb20738.x]