MMP16 explained

Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16 gene.^[1]

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 proproteins which are activated when cleaved by extracellular proteinases. This gene produces at least two transcripts, one which encodes a membrane-bound form and another a soluble form of the protein. Both forms of the protein activate MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16.^[2]

Further reading

• Nagase H, Woessner JF . Matrix metalloproteinases. . J. Biol. Chem. . 274 . 31 . 21491–4 . 1999 . 10419448 . 10.1074/jbc.274.31.21491 . free .
• Andersson B, Wentland MA, Ricafrente JY . A "double adaptor" method for improved shotgun library construction. . Anal. Biochem. . 236 . 1 . 107–13 . 1996 . 8619474 . 10.1006/abio.1996.0138 .
• Mattei MG, Roeckel N, Olsen BR, Apte SS . 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 . 1997 . 9070935 . 10.1006/geno.1996.4559 .
• Shofuda K, Yasumitsu H, Nishihashi A . Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain. . J. Biol. Chem. . 272 . 15 . 9749–54 . 1997 . 9092507 . 10.1074/jbc.272.15.9749 . free .
• Yu W, Andersson B, Worley KC . Large-Scale Concatenation cDNA Sequencing . Genome Res. . 7 . 4 . 353–8 . 1997 . 9110174 . 10.1101/gr.7.4.353. 139146 .
• Sato H, Tanaka M, Takino T . 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 . 9119382 . 10.1006/geno.1996.4496 .
• Matsumoto S, Katoh M, Saito S . Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA . Biochim. Biophys. Acta . 1354 . 2 . 159–70 . 1998 . 9396633 . 10.1016/s0167-4781(97)00120-6.
• Terp GE, Christensen IT, Jørgensen FS . Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes . J. Biomol. Struct. Dyn. . 17 . 6 . 933–46 . 2000 . 10949161 . 10.1080/07391102.2000.10506582. 1270176 .
• Iida J, Pei D, Kang T . Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen . J. Biol. Chem. . 276 . 22 . 18786–94 . 2001 . 11278606 . 10.1074/jbc.M010053200 . free .
• Strausberg RL, Feingold EA, Grouse LH . 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 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Jung M, Römer A, Keyszer G . 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 . 12661033 . 10.1002/pros.10194 . 21596144 .
• Takino T, Koshikawa N, Miyamori H . Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases . Oncogene . 22 . 30 . 4617–26 . 2003 . 12879005 . 10.1038/sj.onc.1206542 . 2297/2668 . 10007952 . free .
• Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY . 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 . 14645246 . 10.1074/jbc.M311569200 . free .
• Lang R, Braun M, Sounni NE . Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features . J. Mol. Biol. . 336 . 1 . 213–25 . 2004 . 14741217 . 10.1016/j.jmb.2003.12.022 . 2268/12040 .
• Shofuda T, Shofuda K, Ferri N . Cleavage of focal adhesion kinase in vascular smooth muscle cells overexpressing membrane-type matrix metalloproteinases . Arterioscler. Thromb. Vasc. Biol. . 24 . 5 . 839–44 . 2004 . 15044209 . 10.1161/01.ATV.0000126680.78500.4c . 22959266 . free .
• Wang SC, Lien HC, Xia W . Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2 . Cancer Cell . 6 . 3 . 251–61 . 2004 . 15380516 . 10.1016/j.ccr.2004.07.012 . free .
• Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Kimura K, Wakamatsu A, Suzuki Y . Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes . Genome Res. . 16 . 1 . 55–65 . 2006 . 16344560 . 10.1101/gr.4039406 . 1356129 .

External links

• The MEROPS online database for peptidases and their inhibitors: M10.016

Notes and References

1. 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 . 39 . 23013–20 . Nov 1995 . 7559440 . 10.1074/jbc.270.39.23013 . free .
2. Web site: Entrez Gene: MMP16 matrix metallopeptidase 16 (membrane-inserted).