Biology:MMP19

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.

Function

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 protein is expressed in human epidermis and endothelial cells and it has a role in cellular proliferation, migration, angiogenesis and adhesion. Multiple transcript variants encoding distinct isoforms have been identified for this gene.

Further reading

• "Evaluation of some newer matrix metalloproteinases". Ann. N. Y. Acad. Sci. 878 (1): 25–39. 1999. doi:10.1111/j.1749-6632.1999.tb07672.x. PMID 10415718. Bibcode: 1999NYASA.878...25M. 
• "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
• "Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan". Biochem. J. 304 (Pt 2): 347–51. 1995. doi:10.1042/bj3040347. PMID 7998967. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain". Biochem. J. 295 (Pt 1): 273–6. 1993. doi:10.1042/bj2950273. PMID 8216228. 
• "Identification of MMP-18, a putative novel human matrix metalloproteinase". Biochem. Biophys. Res. Commun. 228 (2): 494–8. 1996. doi:10.1006/bbrc.1996.1688. PMID 8920941. 
• "Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution". J. Biol. Chem. 272 (7): 4281–6. 1997. doi:10.1074/jbc.272.7.4281. PMID 9020145. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis". Immunobiology 198 (4): 408–23. 1998. doi:10.1016/s0171-2985(98)80049-1. PMID 9562866. 
• "Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain". FEBS Lett. 430 (3): 186–90. 1998. doi:10.1016/S0014-5793(98)00667-X. PMID 9688535. 
• "Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme". J. Biol. Chem. 275 (20): 14809–16. 2000. doi:10.1074/jbc.275.20.14809. PMID 10809722. 
• "Structure of the human MMP-19 gene". Gene 252 (1–2): 27–37. 2000. doi:10.1016/S0378-1119(00)00236-5. PMID 10903435. 
• "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1–2): 52–6. 2000. doi:10.1016/S0014-5793(00)01819-6. PMID 10922468. 
• "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. 2000. doi:10.1080/07391102.2000.10506582. PMID 10949161. 
• "Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the cell surface". J. Immunol. 168 (3): 1244–51. 2002. doi:10.4049/jimmunol.168.3.1244. PMID 11801661. 
• "ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors". Biochem. Biophys. Res. Commun. 293 (1): 501–8. 2002. doi:10.1016/S0006-291X(02)00254-1. PMID 12054629. 
• "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. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1". Cell Mol Life Sci 61 (14): 1826–33. 2004. doi:10.1007/s00018-004-4105-0. PMID 15241558. 

External links

• The MEROPS online database for peptidases and their inhibitors: M10.021