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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]].<ref name="pmid9232430">{{cite journal |vauthors=Kolb C, Mauch S, Peter HH, Krawinkel U, Sedlacek R | title = The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient | journal = Immunol Lett | volume = 57 | issue = 1–3 | pages = 83–8 |date=Oct 1997 | pmid = 9232430 | pmc = | doi =10.1016/S0165-2478(97)00057-6 }}</ref><ref name="entrez"/> | |||
== Function == | |||
Proteins of the matrix metalloproteinase ([[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 (skin)|epidermis]] and [[endothelium|endothelial]] cells and it has a role in cellular [[cell growth|proliferation]], [[cell migration|migration]], [[angiogenesis]] and [[cell adhesion|adhesion]]. Multiple transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MMP19 matrix metallopeptidase 19| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4327| accessdate = }}</ref> | |||
== References == | |||
{{reflist}} | |||
== Further reading == | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{cite journal |vauthors=Murphy G, Knäuper V, Cowell S, etal |title=Evaluation of some newer matrix metalloproteinases |journal=Ann. N. Y. Acad. Sci. |volume=878 |issue= |pages= 25–39 |year= 1999 |pmid= 10415718 |doi=10.1111/j.1749-6632.1999.tb07672.x }} | |||
*{{cite journal |vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491 }} | |||
*{{cite journal |vauthors=Fosang AJ, Last K, Neame PJ, etal |title=Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan |journal=Biochem. J. |volume=304 |issue= Pt 2|pages= 347–51 |year= 1995 |pmid= 7998967 |doi= | pmc=1137499 }} | |||
*{{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }} | |||
*{{cite journal |vauthors=Fosang AJ, Last K, Knäuper V, etal |title=Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain |journal=Biochem. J. |volume=295 |issue= Pt 1|pages= 273–6 |year= 1993 |pmid= 8216228 |doi= | pmc=1134849 }} | |||
*{{cite journal |vauthors=Cossins J, Dudgeon TJ, Catlin G, etal |title=Identification of MMP-18, a putative novel human matrix metalloproteinase |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 2 |pages= 494–8 |year= 1996 |pmid= 8920941 |doi= 10.1006/bbrc.1996.1688 }} | |||
*{{cite journal |vauthors=Pendás AM, Knäuper V, Puente XS, etal |title=Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4281–6 |year= 1997 |pmid= 9020145 |doi=10.1074/jbc.272.7.4281 }} | |||
*{{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }} | |||
*{{cite journal |vauthors=Sedlacek R, Mauch S, Kolb B, etal |title=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 |journal=Immunobiology |volume=198 |issue= 4 |pages= 408–23 |year= 1998 |pmid= 9562866 |doi= 10.1016/s0171-2985(98)80049-1}} | |||
*{{cite journal |vauthors=Fosang AJ, Last K, Fujii Y, etal |title=Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain |journal=FEBS Lett. |volume=430 |issue= 3 |pages= 186–90 |year= 1998 |pmid= 9688535 |doi=10.1016/S0014-5793(98)00667-X }} | |||
*{{cite journal |vauthors=Stracke JO, Hutton M, Stewart M, etal |title=Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 14809–16 |year= 2000 |pmid= 10809722 |doi=10.1074/jbc.275.20.14809 }} | |||
*{{cite journal |vauthors=Mueller MS, Mauch S, Sedlacek R |title=Structure of the human MMP-19 gene |journal=Gene |volume=252 |issue= 1–2 |pages= 27–37 |year= 2000 |pmid= 10903435 |doi=10.1016/S0378-1119(00)00236-5 }} | |||
*{{cite journal |vauthors=Stracke JO, Fosang AJ, Last K, etal |title=Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP) |journal=FEBS Lett. |volume=478 |issue= 1–2 |pages= 52–6 |year= 2000 |pmid= 10922468 |doi=10.1016/S0014-5793(00)01819-6 }} | |||
*{{cite journal |vauthors=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi= 10.1080/07391102.2000.10506582}} | |||
*{{cite journal |vauthors=Mauch S, Kolb C, Kolb B, etal |title=Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the cell surface |journal=J. Immunol. |volume=168 |issue= 3 |pages= 1244–51 |year= 2002 |pmid= 11801661 |doi= 10.4049/jimmunol.168.3.1244}} | |||
*{{cite journal |vauthors=Rodríguez-Manzaneque JC, Westling J, Thai SN, etal |title=ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 501–8 |year= 2002 |pmid= 12054629 |doi= 10.1016/S0006-291X(02)00254-1 }} | |||
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | |||
}} | |||
*{{cite journal |vauthors=Titz B, Dietrich S, Sadowski T, Beck C, Petersen A, Sedlacek R |title=Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1|journal=Cell Mol Life Sci|volume=61 |issue= 14 |pages= 1826–33|year= 2004 |pmid= 15241558 |doi= 10.1007/s00018-004-4105-0}} | |||
{{refend}} | |||
==External links== | |||
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.021 M10.021] | |||
{{Metalloendopeptidases}} | |||
{{Enzymes}} | |||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
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Latest revision as of 05:26, 11 November 2017
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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.[1][2]
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.[2]
References
- ↑ 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.
- ↑ 2.0 2.1 "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: 25–39. doi:10.1111/j.1749-6632.1999.tb07672.x. PMID 10415718.
- 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. 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. 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. 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. doi:10.1016/S0014-5793(98)00667-X. PMID 9688535.
- 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. doi:10.1016/S0014-5793(00)01819-6. PMID 10922468.
- 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.
- 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. 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. 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. PMID 15241558.
External links
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