View source for Matrix metallopeptidase 13

{{Infobox_gene}}
'''Collagenase 3''' is an [[enzyme]] that in humans is encoded by the ''MMP13'' [[gene]].<ref name="pmid8207000">{{cite journal |vauthors=Freije JM, Diez-Itza I, Balbin M, Sanchez LM, Blasco R, Tolivia J, Lopez-Otin C | title = Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas | journal = J Biol Chem | volume = 269 | issue = 24 | pages = 16766–73 |date=Jul 1994 | pmid = 8207000 | pmc =  | doi =  }}</ref><ref name="entrez"/> It is a member of the [[matrix metalloproteinase]] (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain {{PDB|1PEX}}. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.<ref name="pmid10949577">{{cite journal  |vauthors=Johansson N, Ahonen M, Kähäri VM |title=Matrix metalloproteinases in tumor invasion. |journal=Cell Mol Life Sci |volume=57 |issue=1 |year= 2000 |pages= 5–15|pmid=10949577 |doi= 10.1007/s000180050495}}</ref>

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{{PBB_Summary
| section_title = 
| summary_text = 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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.<ref name="entrez">{{cite web | title = Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4322| accessdate = }}</ref>
}}

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{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=Leeman MF, Curran S, Murray GI |title=The structure, regulation, and function of human matrix metalloproteinase-13. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=37 |issue= 3 |pages= 149–66 |year= 2003 |pmid= 12139441 |doi=10.1080/10409230290771483  }}
*{{cite journal  |vauthors=Pendás AM, Matilla T, Estivill X, López-Otín C |title=The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family. |journal=Genomics |volume=26 |issue= 3 |pages= 615–8 |year= 1995 |pmid= 7607691 |doi=10.1016/0888-7543(95)80186-P  }}
*{{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=Mitchell PG, Magna HA, Reeves LM, etal |title=Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage. |journal=J. Clin. Invest. |volume=97 |issue= 3 |pages= 761–8 |year= 1996 |pmid= 8609233 |doi=10.1172/JCI118475  | pmc=507114  }}
*{{cite journal   |vauthors=Knäuper V, Will H, López-Otin C, etal |title=Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17124–31 |year= 1996 |pmid= 8663255 |doi=10.1074/jbc.271.29.17124  }}
*{{cite journal   |vauthors=Gomis-Rüth FX, Gohlke U, Betz M, etal |title=The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain. |journal=J. Mol. Biol. |volume=264 |issue= 3 |pages= 556–66 |year= 1997 |pmid= 8969305 |doi= 10.1006/jmbi.1996.0661 }}
*{{cite journal   |vauthors=Knäuper V, Cowell S, Smith B, etal |title=The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 7608–16 |year= 1997 |pmid= 9065415 |doi=10.1074/jbc.272.12.7608  }}
*{{cite journal   |vauthors=Pendás AM, Balbín M, Llano E, etal |title=Structural analysis and promoter characterization of the human collagenase-3 gene (MMP13). |journal=Genomics |volume=40 |issue= 2 |pages= 222–33 |year= 1997 |pmid= 9119388 |doi= 10.1006/geno.1996.4554 }}
*{{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=Willmroth F, Peter HH, Conca W |title=A matrix metalloproteinase gene expressed in human T lymphocytes is identical with collagenase 3 from breast carcinomas. |journal=Immunobiology |volume=198 |issue= 4 |pages= 375–84 |year= 1998 |pmid= 9562863 |doi=  10.1016/s0171-2985(98)80046-6}}
*{{cite journal   |vauthors=Lovejoy B, Welch AR, Carr S, etal |title=Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors. |journal=Nat. Struct. Biol. |volume=6 |issue= 3 |pages= 217–21 |year= 1999 |pmid= 10074939 |doi= 10.1038/6657 }}
*{{cite journal   |vauthors=Barmina OY, Walling HW, Fiacco GJ, etal |title=Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 30087–93 |year= 1999 |pmid= 10514495 |doi=10.1074/jbc.274.42.30087  }}
*{{cite journal   |vauthors=Lauer-Fields JL, Tuzinski KA, Shimokawa K, etal |title=Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. |journal=J. Biol. Chem. |volume=275 |issue= 18 |pages= 13282–90 |year= 2000 |pmid= 10788434 |doi=10.1074/jbc.275.18.13282  }}
*{{cite journal   |vauthors=Hiller O, Lichte A, Oberpichler A, etal |title=Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 33008–13 |year= 2000 |pmid= 10930399 |doi= 10.1074/jbc.M001836200 }}
*{{cite journal   |vauthors=McQuibban GA, Gong JH, Tam EM, etal |title=Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. |journal=Science |volume=289 |issue= 5482 |pages= 1202–6 |year= 2000 |pmid= 10947989 |doi=10.1126/science.289.5482.1202  }}
*{{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=Nakamura H, Fujii Y, Inoki I, etal |title=Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38885–90 |year= 2001 |pmid= 10986281 |doi= 10.1074/jbc.M003875200 }}
}}

{{refend}}

==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.013 M10.013]

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[[Category:Matrix metalloproteinases]]
[[Category:Human proteins]]
[[Category:EC 3.4.24]]


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