The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ADAMTS3  -  ADAM metallopeptidase with thrombospondin...

Homo sapiens

Synonyms: A disintegrin and metalloproteinase with thrombospondin motifs 3, ADAM-TS 3, ADAM-TS3, ADAMTS-3, ADAMTS-4, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ADAMTS3

  • We investigated such a role for ADAMTS-3 in Swarm rat chondrosarcoma RCS-LTC cells, which fail to process the procollagen II N-propeptide [1].
  • OBJECTIVES: To determine by genetic association analysis whether the 4q functional candidate genes IGFBP7, ADAMTS3, and IL8 might encode for susceptibility to osteoarthritis (OA) [2].
  • CONCLUSIONS: Macrophages infiltrating granulation and adjacent disc tissues express ADAMTS-4, suggesting its involvement in herniated disc regression [3].
  • The active forms of ADAMTS-4 were increased in synovial fluid samples from patients with active Lyme arthritis and were elevated in the joints of mice infected with B burgdorferi [4].
  • In mice with nutritionally induced obesity (high fat diet) as well as in lean controls, aggrecan mRNA expression was downregulated whereas ADAMTS-4 and ADAMTS-5 were upregulated with time [5].

High impact information on ADAMTS3

  • ADAMTS3 induced procollagen I processing in dermatosparactic fibroblasts, suggesting a role in procollagen I processing during musculoskeletal development [6].
  • In the present study, the topological substrate specificity of ADAMTS-4 (aggrecanase-1) was examined using triple-helical or single-stranded poly(Pro) II helical peptides [7].
  • In turn, non-catalytic ADAMTS-4 domains were critical for hydrolysis of triple-helical and poly(Pro) II helical substrates [7].
  • These results suggest that cleavage at preferred sites in the chondroitin sulfate-rich region is mediated by ADAMTS-4 or an aggrecanase other than ADAMTS-5 [8].
  • RESULTS: ADAMTS-4, but not ADAMTS-5, was induced in human chondrocytes infected with B burgdorferi [4].

Biological context of ADAMTS3

  • Stable transfection of RCS-LTC cells with bovine ADAMTS-2 or human ADAMTS-3 partially rescued the processing defect, suggesting that ADAMTS-3 has procollagen II N-propeptidase activity [1].
  • An ADAMTS3 single nucleotide polymorphism was associated in the probands (p = 0.015) and an ADAMTS3 insertion/deletion approached significance (p = 0.059) [2].
  • CONCLUSIONS: The analysis implies that the chromosome 4q female hip OA susceptibility is not coded for by polymorphism within the functional candidates IGFBP7, ADAMTS3, or IL8 [2].
  • Non-degenerate discs showed low numbers of cells expressing the degradative enzymes MMP 1 and ADAMTS 4, suggesting a role for these enzymes in normal homeostasis [9].
  • Thus, in long bone growth, aggrecan turnover seems to be dependent on ADAMTS-4 activity [10].

Anatomical context of ADAMTS3


Associations of ADAMTS3 with chemical compounds

  • We conclude that ADAMTS-4 activation in this cell system involves the coordinated activity of both glycosylphosphatidyl inositol-anchored MT4-MMP and the proteoglycan form of syndecan-1 on the cell surface [15].
  • ADAMTS-4 and MMPs cleave aggrecan more efficiently within the chondroitin sulfate (CS)-rich region than the interglobular domain (IGD) [16].

Analytical, diagnostic and therapeutic context of ADAMTS3


  1. Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. Fernandes, R.J., Hirohata, S., Engle, J.M., Colige, A., Cohn, D.H., Eyre, D.R., Apte, S.S. J. Biol. Chem. (2001) [Pubmed]
  2. Genetic association analysis of the IGFBP7, ADAMTS3, and IL8 genes as the potential osteoarthritis susceptibility that maps to chromosome 4q. Kawahara, C., Forster, T., Chapman, K., Carr, A., Loughlin, J. Ann. Rheum. Dis. (2005) [Pubmed]
  3. Expression of ADAMTS-4 (aggrecanase-1) and possible involvement in regression of lumbar disc herniation. Hatano, E., Fujita, T., Ueda, Y., Okuda, T., Katsuda, S., Okada, Y., Matsumoto, T. Spine (2006) [Pubmed]
  4. Role of aggrecanase 1 in Lyme arthritis. Behera, A.K., Hildebrand, E., Szafranski, J., Hung, H.H., Grodzinsky, A.J., Lafyatis, R., Koch, A.E., Kalish, R., Perides, G., Steere, A.C., Hu, L.T. Arthritis Rheum. (2006) [Pubmed]
  5. Expression of aggrecan(ases) during murine preadipocyte differentiation and adipose tissue development. Voros, G., Sandy, J.D., Collen, D., Lijnen, H.R. Biochim. Biophys. Acta (2006) [Pubmed]
  6. Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases: insights on collagen biosynthesis and dermatosparaxis. Le Goff, C., Somerville, R.P., Kesteloot, F., Powell, K., Birk, D.E., Colige, A.C., Apte, S.S. Development (2006) [Pubmed]
  7. Substrate Conformation Modulates Aggrecanase (ADAMTS-4) Affinity and Sequence Specificity: SUGGESTION OF A COMMON TOPOLOGICAL SPECIFICITY FOR FUNCTIONALLY DIVERSE PROTEASES. Lauer-Fields, J.L., Minond, D., Sritharan, T., Kashiwagi, M., Nagase, H., Fields, G.B. J. Biol. Chem. (2007) [Pubmed]
  8. ADAMTS-5 Deficiency Does Not Block Aggrecanolysis at Preferred Cleavage Sites in the Chondroitin Sulfate-rich Region of Aggrecan. East, C.J., Stanton, H., Golub, S.B., Rogerson, F.M., Fosang, A.J. J. Biol. Chem. (2007) [Pubmed]
  9. Localization of degradative enzymes and their inhibitors in the degenerate human intervertebral disc. Le Maitre, C.L., Freemont, A.J., Hoyland, J.A. J. Pathol. (2004) [Pubmed]
  10. Use of anti-neoepitope antibodies for the analysis of degradative events in cartilage and the molecular basis for neoepitope specificity. Mort, J.S., Flannery, C.R., Makkerh, J., Krupa, J.C., Lee, E.R. Biochem. Soc. Symp. (2003) [Pubmed]
  11. Dysregulated expression of adamalysin-thrombospondin genes in human breast carcinoma. Porter, S., Scott, S.D., Sassoon, E.M., Williams, M.R., Jones, J.L., Girling, A.C., Ball, R.Y., Edwards, D.R. Clin. Cancer Res. (2004) [Pubmed]
  12. Expression of ADAMTS-1, -4, -5 and TIMP-3 in normal and multiple sclerosis CNS white matter. Haddock, G., Cross, A.K., Plumb, J., Surr, J., Buttle, D.J., Bunning, R.A., Woodroofe, M.N. Mult. Scler. (2006) [Pubmed]
  13. Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments. Struglics, A., Larsson, S., Pratta, M.A., Kumar, S., Lark, M.W., Lohmander, L.S. Osteoarthr. Cartil. (2006) [Pubmed]
  14. Aggrecanase-mediated cartilage degradation. Arner, E.C. Current opinion in pharmacology. (2002) [Pubmed]
  15. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. Gao, G., Plaas, A., Thompson, V.P., Jin, S., Zuo, F., Sandy, J.D. J. Biol. Chem. (2004) [Pubmed]
  16. Effects of covalently attached chondroitin sulfate on aggrecan cleavage by ADAMTS-4 and MMP-13. Miwa, H.E., Gerken, T.A., Hering, T.M. Matrix Biol. (2006) [Pubmed]
WikiGenes - Universities