Alternative titles; symbols
HGNC Approved Gene Symbol: MMP16
Cytogenetic location: 8q21.3 Genomic coordinates (GRCh38): 8:88,032,011-88,327,483 (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.
Takino et al. (1995) isolated a novel MMP cDNA (MMP16) from a human placenta cDNA library. The MMP16 protein consists of 604 amino acids and has a characteristic MMP domain structure. Additionally, MMP16 has a C-terminal extension containing a potential transmembrane domain, similar to MMP14 (600754), MMP15 (602261), and MMP17 (602285). Takino et al. (1995) proposed that the membrane-type MMPs are a subclass in the MMP family since the other members lack a C-terminal transmembrane domain and are secreted as soluble forms. Takino et al. (1995) showed that MMP16-specific monoclonal antibodies detect a nonsecreted, 64-kD protein in transfected cells. They used immunofluorescence to show that fusion proteins containing the transmembrane domain of MMP16 are localized on the cell surface, suggesting that MMP16 is membrane-bound. They showed by Northern blotting that MMP16 is expressed as a 12-kb transcript in brain, placenta, heart, and some carcinoma cell lines, but is not detectably expressed in lung, kidney, liver, spleen, and muscle.
Takino et al. (1995) demonstrated that, like MMP14, MMP16 induces the activation of pro-gelatinase A.
Mattei et al. (1997) mapped the MMP16 gene to chromosome 8q21.3-q22.1 by isotopic in situ hybridization. Sato et al. (1997) used fluorescence in situ hybridization to localize the MMP16 gene to 8q21.
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]