ADAMTS5 (21q21.3) , Aggrekanaasi-2 ( HyalektanaasI)

https://www.ncbi.nlm.nih.gov/gene/11096

DMP-2; ADAM-TS5; ADAMTS-5; ADAMTS11; ADAM-TS 5; ADAMTS-11; ADAM-TS 11

Summary

This gene encodes 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 encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme contains two C-terminal TS motifs and functions as an aggrecanase that cleaves aggrecan, a major proteoglycan of cartilage, and may mediate cartilage destruction in osteoarthritis. [provided by RefSeq, Feb 2016]

Expression

Broad expression in ovary (RPKM 9.8), endometrium (RPKM 9.6) and 17 other tissues See more

Preferred Names

A disintegrin and metalloproteinase with thrombospondin motifs 5

Names

a disintegrin and metalloproteinase with thrombospondin motifs 11

a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2)

aggrecanase-2

Protein 
 https://www.ncbi.nlm.nih.gov/protein/NP_008969.2

Related articles in PubMed

1. Targeted next-generation sequencing identified ADAMTS5 as novel genetic substrate in patients with bicuspid aortic valve. Lin X, et al. Int J Cardiol, 2018 Feb 1. PMID 29162281
2. Epigenetic silencing of ADAMTS5 is associated with increased invasiveness and poor survival in patients with colorectal cancer. Li J, et al. J Cancer Res Clin Oncol, 2018 Feb. PMID 29143120
3. ADAMTS5 Deficiency in Calcified Aortic Valves Is Associated With Elevated Pro-Osteogenic Activity in Valvular Interstitial Cells. Li F, et al. Arterioscler Thromb Vasc Biol, 2017 Jul. PMID 28546218, Free PMC Article
4. Role of ADAMTS5 in Unexplained Fetal Growth Restriction (FGR). Ozler S, et al. Fetal Pediatr Pathol, 2016. PMID 27159841
5. Overexpression of ADAMTS5 can regulate the migration and invasion of non-small cell lung cancer. Gu J, et al. Tumour Biol, 2016 Jul. PMID 26738863

See all (95) citations in PubMed

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. Data suggest that 3prime untranslated region of ADAMTS5 mRNA contains 'seedmatched-sequence' for hsa-miR-140-3p (microRNA-140-3p); in chondrocytes from articular cartilage of patients with knee osteoarthritis, interleukin-1beta up-regulates expression of ADAMTS5 and down-regulates expression of hsa-miR-140-3p. (ADAMTS5 = ADAM metallopeptidase with thrombospondin type 1 motif 5 A)
2. A novel genetic variant in ADAMTS5 is associated with bicuspid aortic valve disease.
3. expression by synovial cells induced by hemoglobin at low doses, suggesting a possible role for hemoglobin in cartilage damage after intra-articular hemorrhagehttps://www.ncbi.nlm.nih.gov/pubmed/29137610
4. The SNPs rs1337185 in COL11A1 and rs162509 in ADAMTS5 are associated with susceptibility to lumbar disc degeneration. The C allele of rs1337185 is risky for patients who are affected by lumbar pathologies such as disc herniation, stenosis and spondylolisthesis. The G allele of rs16250 represents a risk factor for the development of disc herniation.
5. ADAMTS5 is hypermethylated and inhibits cancer cells invasion and migration in colorectal cancer, and correlates with OS and DFS.
6. Development of a monoclonal anti-ADAMTS-5 antibody that specifically blocks the interaction with LRP1.
7. MMP-13 may play a role on physiological turnover of cartilage extracellular matrix and that LRP1 is a key modulator of extracellular levels of MMP-13 and its internalization is independent of the levels of ADAMTS-4, -5 and TIMP-3.
8. The IL1B/AP-1/miR-30a/ADAMTS-5 axis regulates cartilage matrix degradation in osteoarthritis.
9. The findings suggest that miR-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5.
10. Results provide direct evidence indicating that Fibulin-2 is a novel substrate of ADAMTS-5 and that this proteolysis could alter the cellular microenvironment affecting the balance between protumor and antitumor effects associated to both Fibulin-2 and the ADAMTSs metalloproteases.

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