Matrix metallopeptidase 13: Difference between revisions

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{{Infobox_gene}}
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'''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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{{GNF_Protein_box
| image = PBB_Protein_MMP13_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cxv.
| PDB = {{PDB2|1cxv}}, {{PDB2|1eub}}, {{PDB2|1fls}}, {{PDB2|1fm1}}, {{PDB2|1pex}}, {{PDB2|1xuc}}, {{PDB2|1xud}}, {{PDB2|1xur}}, {{PDB2|1you}}, {{PDB2|1ztq}}, {{PDB2|2d1n}}, {{PDB2|2e2d}}, {{PDB2|2ow9}}, {{PDB2|456c}}, {{PDB2|830c}}
| Name = Matrix metallopeptidase 13 (collagenase 3)
| HGNCid = 7159
| Symbol = MMP13
| AltSymbols =; CLG3
| OMIM = 600108
| ECnumber =
| Homologene = 20548
| MGIid = 1340026
  | GeneAtlas_image1 = PBB_GE_MMP13_205959_at_tn.png
  | Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008133 |text = collagenase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}  
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4322
    | Hs_Ensembl = ENSG00000137745
    | Hs_RefseqProtein = NP_002418
    | Hs_RefseqmRNA = NM_002427
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 102318937
    | Hs_GenLoc_end = 102331672
    | Hs_Uniprot = P45452
    | Mm_EntrezGene = 17386
    | Mm_Ensembl = ENSMUSG00000050578
    | Mm_RefseqmRNA = NM_008607
    | Mm_RefseqProtein = NP_032633
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 7272545
    | Mm_GenLoc_end = 7283333
    | Mm_Uniprot = Q3U2N6
  }}
}}
'''Matrix metallopeptidase 13 (collagenase 3)''', also known as '''MMP13''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4322| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 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.<ref name="entrez">{{cite web | title = Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4322| accessdate = }}</ref>
| 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==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491-4 |year= 1999 |pmid= 10419448 |doi=  }}
*{{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  | author=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=  }}
*{{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  | author=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= }}
*{{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  | author=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=  }}
*{{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 | author=Freije JM, Díez-Itza I, Balbín M, ''et al.'' |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 |year= 1994 |pmid= 8207000 |doi=  }}
*{{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 | author=Mitchell PG, Magna HA, Reeves LM, ''et al.'' |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=  }}
*{{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 | author=Knäuper V, Will H, López-Otin C, ''et al.'' |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= }}
*{{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 | author=Gomis-Rüth FX, Gohlke U, Betz M, ''et al.'' |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 | author=Knäuper V, Cowell S, Smith B, ''et al.'' |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= }}
*{{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 | author=Pendás AM, Balbín M, Llano E, ''et al.'' |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  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |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=  }}
*{{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 | author=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= }}
*{{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 | author=Lovejoy B, Welch AR, Carr S, ''et al.'' |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 | author=Barmina OY, Walling HW, Fiacco GJ, ''et al.'' |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=  }}
*{{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 | author=Lauer-Fields JL, Tuzinski KA, Shimokawa K, ''et al.'' |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= }}
*{{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 | author=Hiller O, Lichte A, Oberpichler A, ''et al.'' |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  | author=McQuibban GA, Gong JH, Tam EM, ''et al.'' |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=  }}
*{{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  | author=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=  }}
*{{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 }}
*{{cite journal | author=Nakamura H, Fujii Y, Inoki I, ''et al.'' |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}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* 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]]
 
 
{{gene-11-stub}}

Latest revision as of 05:26, 11 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

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]

References

  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. ↑ 2.0 2.1 "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

  • 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

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


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