Matrix metalloproteinase-16 is an enzyme that in humans is encoded by the MMP16gene.
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.
↑Takino T, Sato H, Shinagawa A, Seiki M (Nov 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.
Mattei MG, Roeckel N, Olsen BR, Apte SS (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. PMID9070935.
Shofuda K, Yasumitsu H, Nishihashi A (1997). "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. doi:10.1074/jbc.272.15.9749. PMID9092507.
Sato H, Tanaka M, Takino T (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. PMID9119382.
Matsumoto S, Katoh M, Saito S (1998). "Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA". Biochim. Biophys. Acta. 1354 (2): 159–70. doi:10.1016/s0167-4781(97)00120-6. PMID9396633.
Terp GE, Christensen IT, Jørgensen FS (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.
Iida J, Pei D, Kang T (2001). "Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen". J. Biol. Chem. 276 (22): 18786–94. doi:10.1074/jbc.M010053200. PMID11278606.
Jung M, Römer A, Keyszer G (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. PMID12661033.
Takino T, Koshikawa N, Miyamori H (2003). "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases". Oncogene. 22 (30): 4617–26. doi:10.1038/sj.onc.1206542. PMID12879005.
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.
Wang SC, Lien HC, Xia W (2004). "Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2". Cancer Cell. 6 (3): 251–61. doi:10.1016/j.ccr.2004.07.012. PMID15380516.