Matrix metallopeptidase 13

Matrix metallopeptidase 13 (collagenase 3)
File:PBB Protein MMP13 image.jpg PDB rendering based on 1cxv.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1cxv​, 1eub​, 1fls​, 1fm1​, 1pex​, 1xuc​, 1xud​, 1xur​, 1you​, 1ztq​, 2d1n​, 2e2d​, 2ow9​, 456c​, 830c​
Identifiers
Symbols	MMP13 ; CLG3
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20548
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MMP13 205959 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Matrix metallopeptidase 13 (collagenase 3), also known as MMP13, is a human gene.

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. 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.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
• Leeman MF, Curran S, Murray GI (2003). "The structure, regulation, and function of human matrix metalloproteinase-13". Crit. Rev. Biochem. Mol. Biol. 37 (3): 149–66. PMID 12139441.CS1 maint: Multiple names: authors list (link)
• Pendás AM, Matilla T, Estivill X, López-Otín C (1995). "The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family". Genomics. 26 (3): 615–8. PMID 7607691.CS1 maint: Multiple names: authors list (link)
• 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. PMID 8125298.
• Freije JM, Díez-Itza I, Balbín M; et al. (1994). "Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas". J. Biol. Chem. 269 (24): 16766–73. PMID 8207000.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mitchell PG, Magna HA, Reeves LM; et al. (1996). "Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage". J. Clin. Invest. 97 (3): 761–8. PMID 8609233.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Knäuper V, Will H, López-Otin C; et al. (1996). "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". J. Biol. Chem. 271 (29): 17124–31. PMID 8663255.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gomis-Rüth FX, Gohlke U, Betz M; et al. (1997). "The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain". J. Mol. Biol. 264 (3): 556–66. doi:10.1006/jmbi.1996.0661. PMID 8969305.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Knäuper V, Cowell S, Smith B; et al. (1997). "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". J. Biol. Chem. 272 (12): 7608–16. PMID 9065415.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pendás AM, Balbín M, Llano E; et al. (1997). "Structural analysis and promoter characterization of the human collagenase-3 gene (MMP13)". Genomics. 40 (2): 222–33. doi:10.1006/geno.1996.4554. PMID 9119388.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Willmroth F, Peter HH, Conca W (1998). "A matrix metalloproteinase gene expressed in human T lymphocytes is identical with collagenase 3 from breast carcinomas". Immunobiology. 198 (4): 375–84. PMID 9562863.CS1 maint: Multiple names: authors list (link)
• Lovejoy B, Welch AR, Carr S; et al. (1999). "Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors". Nat. Struct. Biol. 6 (3): 217–21. doi:10.1038/6657. PMID 10074939.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Barmina OY, Walling HW, Fiacco GJ; et al. (1999). "Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization". J. Biol. Chem. 274 (42): 30087–93. PMID 10514495.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lauer-Fields JL, Tuzinski KA, Shimokawa K; et al. (2000). "Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases". J. Biol. Chem. 275 (18): 13282–90. PMID 10788434.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hiller O, Lichte A, Oberpichler A; et al. (2000). "Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII". J. Biol. Chem. 275 (42): 33008–13. doi:10.1074/jbc.M001836200. PMID 10930399.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McQuibban GA, Gong JH, Tam EM; et al. (2000). "Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3". Science. 289 (5482): 1202–6. PMID 10947989.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 10949161.CS1 maint: Multiple names: authors list (link)
• Nakamura H, Fujii Y, Inoki I; et al. (2001). "Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites". J. Biol. Chem. 275 (49): 38885–90. doi:10.1074/jbc.M003875200. PMID 10986281.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)