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Gene Review

ADAMTS8  -  ADAM metallopeptidase with thrombospondin...

Homo sapiens

Synonyms: A disintegrin and metalloproteinase with thrombospondin motifs 8, ADAM-TS 8, ADAM-TS8, ADAMTS-8, FLJ41712, ...
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Disease relevance of ADAMTS8


High impact information on ADAMTS8


Biological context of ADAMTS8


Anatomical context of ADAMTS8


Associations of ADAMTS8 with chemical compounds

  • Meth 8 tumor cells were easily lysed in vitro by rIL-2-activated killer (AK) cells, which mainly consisted of Thy1.2+, Lyt2.2+, L3T4- T cells, and asialo GM1+ natural killer (NK) cells; on the other hand, X5563 tumor cells were only slightly lysed in vitro by AK cells under the same conditions [8].

Enzymatic interactions of ADAMTS8

  • A neoepitope monoclonal antibody (MAb; AGG-C1; anti-NITEGE373) was developed and used to demonstrate the ability of ADAMTS-8 to cleave aggrecan at the aggrecanase-susceptible Glu373-Ala374 peptide bond [6].

Other interactions of ADAMTS8


Analytical, diagnostic and therapeutic context of ADAMTS8

  • This observation has been validated in an independent series of NSCLCs and adjacent normal tissues by comparative multiplex RT-PCR, and METH-2 mRNA expression was dramatically reduced in all 23 tumour samples analysed [3].
  • Immunohistochemistry and Western analysis indicated downregulation of ADAMTS-8 protein in >77% tumours [7].


  1. The quantification of ADAMTS expression in an animal model of cerebral ischemia using real-time PCR. Tian, Y.F., Zhang, P.B., Xiao, X.L., Zhang, J.S., Zhao, J.J., Kang, Q.Y., Chen, X.L., Qiu, F., Liu, Y. Acta anaesthesiologica Scandinavica (2007) [Pubmed]
  2. Expression of METH-1 and METH-2 in pancreatic cancer. Masui, T., Hosotani, R., Tsuji, S., Miyamoto, Y., Yasuda, S., Ida, J., Nakajima, S., Kawaguchi, M., Kobayashi, H., Koizumi, M., Toyoda, E., Tulachan, S., Arii, S., Doi, R., Imamura, M. Clin. Cancer Res. (2001) [Pubmed]
  3. METH-2 silencing and promoter hypermethylation in NSCLC. Dunn, J.R., Panutsopulos, D., Shaw, M.W., Heighway, J., Dormer, R., Salmo, E.N., Watson, S.G., Field, J.K., Liloglou, T. Br. J. Cancer (2004) [Pubmed]
  4. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. Vázquez, F., Hastings, G., Ortega, M.A., Lane, T.F., Oikemus, S., Lombardo, M., Iruela-Arispe, M.L. J. Biol. Chem. (1999) [Pubmed]
  5. ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma. Porter, S., Span, P.N., Sweep, F.C., Tjan-Heijnen, V.C., Pennington, C.J., Pedersen, T.X., Johnsen, M., Lund, L.R., Rømer, J., Edwards, D.R. Int. J. Cancer (2006) [Pubmed]
  6. ADAMTS-8 exhibits aggrecanase activity and is expressed in human articular cartilage. Collins-Racie, L.A., Flannery, C.R., Zeng, W., Corcoran, C., Annis-Freeman, B., Agostino, M.J., Arai, M., DiBlasio-Smith, E., Dorner, A.J., Georgiadis, K.E., Jin, M., Tan, X.Y., Morris, E.A., LaVallie, E.R. Matrix Biol. (2004) [Pubmed]
  7. Expression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumours. Dunn, J.R., Reed, J.E., du Plessis, D.G., Shaw, E.J., Reeves, P., Gee, A.L., Warnke, P., Walker, C. Br. J. Cancer (2006) [Pubmed]
  8. Distinct antitumor mechanisms of recombinant interleukin-2 on recombinant interleukin-2-activated killer-sensitive and -resistant murine tumors. Maekawa, R., Kitagawa, T., Koizumi, K., Sato, K., Homma, M. Journal of biological response modifiers. (1989) [Pubmed]
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