ADAMTS5

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ADAM metallopeptidase with thrombospondin type 1 motif, 5
PDB 2rjq EBI.png
PDB rendering based on 2rjq.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ADAMTS5 ; ADAM-TS 11; ADAM-TS 5; ADAM-TS5; ADAMTS-11; ADAMTS-5; ADAMTS11; ADMP-2
External IDs OMIM605007 MGI1346321 HomoloGene5109 ChEMBL: 2285 GeneCards: ADAMTS5 Gene
EC number 3.4.24.-
Orthologs
Species Human Mouse
Entrez 11096 23794
Ensembl ENSG00000154736 ENSMUSG00000022894
UniProt Q9UNA0 Q9R001
RefSeq (mRNA) NM_007038 NM_011782
RefSeq (protein) NP_008969 NP_035912
Location (UCSC) Chr 21:
28.29 – 28.34 Mb
Chr 16:
85.86 – 85.9 Mb
PubMed search [1] [2]

A disintegrin and metalloproteinase with thrombospondin motifs 5 also known as ADAMTS5 is an enzyme that in humans is encoded by the ADAMTS5 gene.[1][2]

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.[3]

Clinical significance[edit]

Genetically modified mice in which the catalytic domain of ADAMTS5 was deleted are resistant to cartilage destruction in an experimental model of osteoarthritis.[4] ADAMTS5 is the major aggrecanase in mouse cartilage in a mouse model of inflammatory arthritis.[5]

References[edit]

  1. ^ 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 (August 1999). "Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family". J. Biol. Chem. 274 (33): 23443–50. doi:10.1074/jbc.274.33.23443. PMID 10438522. 
  2. ^ Hurskainen TL, Hirohata S, Seldin MF, Apte SS (September 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". J. Biol. Chem. 274 (36): 25555–63. doi:10.1074/jbc.274.36.25555. PMID 10464288. 
  3. ^ "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif". 
  4. ^ Glasson SS, Askew R, Sheppard B, Carito B, Blanchet T, Ma HL, Flannery CR, Peluso D, Kanki K, Yang Z, Majumdar MK, Morris EA (March 2005). "Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis". Nature 434 (7033): 644–8. doi:10.1038/nature03369. PMID 15800624. 
  5. ^ Stanton H, Rogerson FM, East CJ, Golub SB, Lawlor KE, Meeker CT, Little CB, Last K, Farmer PJ, Campbell IK, Fourie AM, Fosang AJ (March 2005). "ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro". Nature 434 (7033): 648–52. doi:10.1038/nature03417. PMID 15800625. 

Further reading[edit]

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