ADAMTS5

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Template:Short description An Error has occurred retrieving Wikidata item for infobox 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

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] ADAMTS5 may also have a role in the pathogenesis of human osteoarthritis.[4]

Animal studies

Genetically modified mice in which the catalytic domain of ADAMTS5 was deleted are resistant to cartilage destruction in an experimental model of osteoarthritis.[5] ADAMTS5 is the major aggrecanase in mouse cartilage in a mouse model of inflammatory arthritis.[6]

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.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.
  2. ^ Page Module:Citation/CS1/styles.css has no content.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.
  3. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif".
  4. ^ Page Module:Citation/CS1/styles.css has no content.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.
  5. ^ Page Module:Citation/CS1/styles.css has no content.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.
  6. ^ Page Module:Citation/CS1/styles.css has no content.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

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