Matrix metallopeptidase 13

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Matrix metallopeptidase 13 (collagenase 3)
Protein MMP13 PDB 1cxv.png
PDB rendering based on 1cxv.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols MMP13 ; CLG3; MANDP1; MMP-13
External IDs OMIM600108 MGI1340026 HomoloGene20548 IUPHAR: 1637 ChEMBL: 280 GeneCards: MMP13 Gene
EC number 3.4.24.-
RNA expression pattern
PBB GE MMP13 205959 at tn.png
More reference expression data
Species Human Mouse
Entrez 4322 17386
Ensembl ENSG00000137745 ENSMUSG00000050578
UniProt P45452 P33435
RefSeq (mRNA) NM_002427 NM_008607
RefSeq (protein) NP_002418 NP_032633
Location (UCSC) Chr 11:
102.81 – 102.83 Mb
Chr 9:
7.27 – 7.28 Mb
PubMed search [1] [2]

Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene.[1][2] 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.[3]

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.[2]


  1. ^ Freije JM, Diez-Itza I, Balbin M, Sanchez LM, Blasco R, Tolivia J, Lopez-Otin C (Jul 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. 
  2. ^ a b "Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)". 
  3. ^ Johansson N, Ahonen M, Kähäri VM. (2000). "Matrix metalloproteinases in tumor invasion.". Cell Mol Life Sci. 57 (1): 5–15. doi:10.1007/s000180050495. PMID 10949577. 

Further reading[edit]

  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. 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. doi:10.1080/10409230290771483. PMID 12139441. 
  • 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. doi:10.1016/0888-7543(95)80186-P. PMID 7607691. 
  • 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. 
  • 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. doi:10.1172/JCI118475. PMC 507114. PMID 8609233. 
  • 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. doi:10.1074/jbc.271.29.17124. PMID 8663255. 
  • 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. 
  • 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. doi:10.1074/jbc.272.12.7608. PMID 9065415. 
  • 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. 
  • 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. 
  • 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. doi:10.1016/s0171-2985(98)80046-6. PMID 9562863. 
  • 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. 
  • 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. doi:10.1074/jbc.274.42.30087. PMID 10514495. 
  • 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. doi:10.1074/jbc.275.18.13282. PMID 10788434. 
  • 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. 
  • 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. doi:10.1126/science.289.5482.1202. PMID 10947989. 
  • 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. 
  • 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. 

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: M10.013