ADAMTS5

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ADAMTS5
PDB 2rjq EBI.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADAMTS5, ADAM-TS 11, ADAM-TS 5, ADAM-TS5, ADAMTS-11, ADAMTS-5, ADAMTS11, ADMP-2, ADAM metallopeptidase with thrombospondin type 1 motif 5
External IDsOMIM: 605007 MGI: 1346321 HomoloGene: 5109 GeneCards: ADAMTS5
Gene location (Human)
Chromosome 21 (human)
Chr.Chromosome 21 (human)[1]
Chromosome 21 (human)
Genomic location for ADAMTS5
Genomic location for ADAMTS5
Band21q21.3Start26,917,922 bp[1]
End26,967,088 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_007038

NM_011782

RefSeq (protein)

NP_008969

NP_035912

Location (UCSC)Chr 21: 26.92 – 26.97 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

A disintegrin and metalloproteinase with thrombospondin motifs 5 also known as ADAMTS5 is an enzyme that in humans is encoded by the ADAMTS5 gene.[4][5]

Function[edit]

ADAMTS5 is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage.[6] ADAMTS5 may also have a role in the pathogenesis of human osteoarthritis.[7]

Animal studies[edit]

Genetically modified mice in which the catalytic domain of ADAMTS5 was deleted are resistant to cartilage destruction in an experimental model of osteoarthritis.[8] ADAMTS5 is the major aggrecanase in mouse cartilage in a mouse model of inflammatory arthritis.[9]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000154736 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Abbaszade I, Liu RQ, Yang F, Rosenfeld SA, Ross OH, Link JR, Ellis DM, Tortorella MD, Pratta MA, Hollis JM, Wynn R, Duke JL, George HJ, Hillman MC, Murphy K, Wiswall BH, Copeland RA, Decicco CP, Bruckner R, Nagase H, Itoh Y, Newton RC, Magolda RL, Trzaskos JM, Burn TC (Aug 1999). "Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family". The Journal of Biological Chemistry. 274 (33): 23443–50. doi:10.1074/jbc.274.33.23443. PMID 10438522.
  5. ^ Hurskainen TL, Hirohata S, Seldin MF, Apte SS (Sep 1999). "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family". The Journal of Biological Chemistry. 274 (36): 25555–63. doi:10.1074/jbc.274.36.25555. PMID 10464288.
  6. ^ "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif".
  7. ^ Verma P, Dalal K (Dec 2011). "ADAMTS-4 and ADAMTS-5: key enzymes in osteoarthritis". Journal of Cellular Biochemistry. 112 (12): 3507–14. doi:10.1002/jcb.23298. PMID 21815191. S2CID 30611107.
  8. ^ Glasson SS, Askew R, Sheppard B, Carito B, Blanchet T, Ma HL, Flannery CR, Peluso D, Kanki K, Yang Z, Majumdar MK, Morris EA (Mar 2005). "Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis". Nature. 434 (7033): 644–8. Bibcode:2005Natur.434..644G. doi:10.1038/nature03369. PMID 15800624. S2CID 4339874.
  9. ^ Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, Little CB, Last K, Farmer PJ, Campbell IK, Fourie AM, Fosang AJ (Mar 2005). "ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro". Nature. 434 (7033): 648–52. Bibcode:2005Natur.434..648S. doi:10.1038/nature03417. PMID 15800625. S2CID 4366441.

Further reading[edit]

External links[edit]