MMP19

MMP19
Identifiers
Aliases	MMP19 , MMP18, RASI-1, CODA, matrix metallopeptidase 19
External IDs	OMIM: 601807; MGI: 1927899; HomoloGene: 1820; GeneCards: MMP19; OMA:MMP19 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12q13.2 Start 55,835,433 bp [1] End 55,842,966 bp [1]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [2] Band 10 D3|10 77.16 cM Start 128,626,779 bp [2] End 128,636,693 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left uterine tube gallbladder olfactory bulb upper lobe of left lung spleen ascending aorta stromal cell of endometrium Descending thoracic aorta smooth muscle tissue right ovary Top expressed in liver stroma of bone marrow blood left lobe of liver adrenal gland uterus aortic valve ascending aorta muscle of thigh umbilical cord More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding metal ion binding peptidase activity hydrolase activity metallopeptidase activity metalloendopeptidase activity serine-type endopeptidase activity Cellular component extracellular region extracellular matrix extracellular space Biological process cell differentiation ovulation from ovarian follicle extracellular matrix disassembly luteolysis proteolysis multicellular organism development angiogenesis ovarian follicle development response to hormone response to cAMP collagen catabolic process extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4327 58223 Ensembl ENSG00000123342 ENSMUSG00000025355 UniProt Q99542 Q9JHI0 RefSeq (mRNA) NM_001032360 NM_001272101 NM_002429 NM_022790 NM_022792 NM_001164197 NM_021412 RefSeq (protein) NP_001259030 NP_002420 NP_001157669 NP_067387 Location (UCSC) Chr 12: 55.84 – 55.84 Mb Chr 10: 128.63 – 128.64 Mb PubMed search [3] [4]
Wikidata
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Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene. ^{[5] [6]}

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. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000123342 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025355 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Kolb C, Mauch S, Peter HH, Krawinkel U, Sedlacek R (Oct 1997). "The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient". Immunol Lett. 57 (1–3): 83–8. doi:10.1016/S0165-2478(97)00057-6. PMID   9232430.
6. "Entrez Gene: MMP19 matrix metallopeptidase 19".

Further reading

• Murphy G, Knäuper V, Cowell S, et al. (1999). "Evaluation of some newer matrix metalloproteinases". Ann. N. Y. Acad. Sci. 878 (1): 25–39. Bibcode:1999NYASA.878...25M. doi:10.1111/j.1749-6632.1999.tb07672.x. PMID   10415718. S2CID   38505267.
• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi: 10.1074/jbc.274.31.21491 . PMID   10419448.
• Fosang AJ, Last K, Neame PJ, et al. (1995). "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. doi:10.1042/bj3040347. PMC   1137499 . PMID   7998967.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Fosang AJ, Last K, Knäuper V, et al. (1993). "Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain". Biochem. J. 295 (Pt 1): 273–6. doi:10.1042/bj2950273. PMC   1134849 . PMID   8216228.
• Cossins J, Dudgeon TJ, Catlin G, et al. (1996). "Identification of MMP-18, a putative novel human matrix metalloproteinase". Biochem. Biophys. Res. Commun. 228 (2): 494–8. Bibcode:1996BBRC..228..494C. doi:10.1006/bbrc.1996.1688. PMID   8920941.
• Pendás AM, Knäuper V, Puente XS, et al. (1997). "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. doi: 10.1074/jbc.272.7.4281 . PMID   9020145.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Sedlacek R, Mauch S, Kolb B, et al. (1998). "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. doi:10.1016/s0171-2985(98)80049-1. PMID   9562866.
• Fosang AJ, Last K, Fujii Y, et al. (1998). "Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain". FEBS Lett. 430 (3): 186–90. Bibcode:1998FEBSL.430..186F. doi: 10.1016/S0014-5793(98)00667-X . PMID   9688535. S2CID   21861810.
• Stracke JO, Hutton M, Stewart M, et al. (2000). "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. doi: 10.1074/jbc.275.20.14809 . PMID   10809722.
• Mueller MS, Mauch S, Sedlacek R (2000). "Structure of the human MMP-19 gene". Gene. 252 (1–2): 27–37. doi:10.1016/S0378-1119(00)00236-5. PMID   10903435.
• Stracke JO, Fosang AJ, Last K, et al. (2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1–2): 52–6. Bibcode:2000FEBSL.478...52S. doi:10.1016/S0014-5793(00)01819-6. PMID   10922468. S2CID   37366875.
• 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. PMID   10949161. S2CID   1270176.
• Mauch S, Kolb C, Kolb B, et al. (2002). "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. doi: 10.4049/jimmunol.168.3.1244 . PMID   11801661.
• Rodríguez-Manzaneque JC, Westling J, Thai SN, et al. (2002). "ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors". Biochem. Biophys. Res. Commun. 293 (1): 501–8. Bibcode:2002BBRC..293..501C. doi:10.1016/S0006-291X(02)00254-1. PMID   12054629.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Titz B, Dietrich S, Sadowski T, Beck C, Petersen A, Sedlacek R (2004). "Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1". Cell Mol Life Sci. 61 (14): 1826–33. doi:10.1007/s00018-004-4105-0. PMC   11138908 . PMID   15241558. S2CID   6853562.

External links

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