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Gene Review

ADAM9  -  ADAM metallopeptidase domain 9

Homo sapiens

Synonyms: ADAM 9, CORD9, Cellular disintegrin-related protein, Disintegrin and metalloproteinase domain-containing protein 9, KIAA0021, ...
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Disease relevance of ADAM9


High impact information on ADAM9


Chemical compound and disease context of ADAM9

  • Microarray analysis detected elevated ADAM9 during the transition of human LNCaP prostate cancer cells from an androgen-dependent to an androgen-independent and metastatic state [2].
  • CONCLUSIONS: Our results show that especially for primary tumors containing stromal elements, the assessment of mRNA expression levels of ADAM-9 and ADAM-11 could be useful to identify patients with recurrent breast cancer who are likely to benefit or fail from tamoxifen therapy [8].
  • However, we observed downregulation of ADAM-9 mRNA expression upon culture of melanoma cells within 3-dimensional lattices composed of fibrillar type I collagen, whereas culture within gels consisting of the polysaccharide alginate did not alter transcript levels [9].

Biological context of ADAM9


Anatomical context of ADAM9


Associations of ADAM9 with chemical compounds

  • New protein synthesis is necessary for the expression of ADAM9 mRNA and genistein suppresses induction of ADAM9 mRNA [11].
  • The induction of ADAM9 by stress can be inhibited by both actinomycin D and cycloheximide through increased gene transcription and protein synthesis [2].
  • Induction of ADAM9 protein in LNCaP or C4-2 cells can be completely abrogated by the administration of an antioxidant, ebselen, or genetic transfer of a hydrogen peroxide degradative enzyme, catalase, suggesting that reactive oxygen species (ROS) are a common mediator [2].
  • Peptides mimicking the predicted cysteine-switch region of MDC9 or TACE inhibit both enzymes in the low micromolar range, providing experimental evidence for regulation of metalloprotease disintegrins via a cysteine-switch mechanism [14].
  • Renal tubular epithelial cells in all nephron segments express a distinct member of the metalloprotease-disintegrin family, ADAM9 (a disintegrin and metalloprotease 9), in a punctate basolateral distribution co-localized to the beta1 integrin chain [Mahimkar, Baricos, Visaya, Pollock and Lovett (2000) J. Am. Soc. Nephrol. 11, 595-603] [15].

Physical interactions of ADAM9


Regulatory relationships of ADAM9


Other interactions of ADAM9


Analytical, diagnostic and therapeutic context of ADAM9


  1. The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer. Carl-McGrath, S., Lendeckel, U., Ebert, M., Roessner, A., Röcken, C. Int. J. Oncol. (2005) [Pubmed]
  2. Oxidative Stress Induces ADAM9 Protein Expression in Human Prostate Cancer Cells. Sung, S.Y., Kubo, H., Shigemura, K., Arnold, R.S., Logani, S., Wang, R., Konaka, H., Nakagawa, M., Mousses, S., Amin, M., Anderson, C., Johnstone, P., Petros, J.A., Marshall, F.F., Zhau, H.E., Chung, L.W. Cancer Res. (2006) [Pubmed]
  3. Overexpression of ADAM9 in non-small cell lung cancer correlates with brain metastasis. Shintani, Y., Higashiyama, S., Ohta, M., Hirabayashi, H., Yamamoto, S., Yoshimasu, T., Matsuda, H., Matsuura, N. Cancer Res. (2004) [Pubmed]
  4. ADAM9 expression is a significant and independent prognostic marker of PSA relapse in prostate cancer. Fritzsche, F.R., Jung, M., Tölle, A., Wild, P., Hartmann, A., Wassermann, K., Rabien, A., Lein, M., Dietel, M., Pilarsky, C., Calvano, D., Grützmann, R., Jung, K., Kristiansen, G. Eur. Urol. (2008) [Pubmed]
  5. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. Weskamp, G., Krätzschmar, J., Reid, M.S., Blobel, C.P. J. Cell Biol. (1996) [Pubmed]
  6. Mitogenic activity and signaling mechanism of 2-(14,15- epoxyeicosatrienoyl)glycerol, a novel cytochrome p450 arachidonate metabolite. Chen, J., Chen, J.K., Falck, J.R., Anjaiah, S., Capdevila, J.H., Harris, R.C. Mol. Cell. Biol. (2007) [Pubmed]
  7. ADAM-9 (MDC-9/meltrin-gamma), a member of the a disintegrin and metalloproteinase family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the alpha(v)beta5 integrin. Karadag, A., Zhou, M., Croucher, P.I. Blood (2006) [Pubmed]
  8. How ADAM-9 and ADAM-11 differentially from estrogen receptor predict response to tamoxifen treatment in patients with recurrent breast cancer: a retrospective study. Sieuwerts, A.M., Meijer-van Gelder, M.E., Timmermans, M., Trapman, A.M., Garcia, R.R., Arnold, M., Goedheer, A.J., Portengen, H., Klijn, J.G., Foekens, J.A. Clin. Cancer Res. (2005) [Pubmed]
  9. Adam-9 expression and regulation in human skin melanoma and melanoma cell lines. Zigrino, P., Mauch, C., Fox, J.W., Nischt, R. Int. J. Cancer (2005) [Pubmed]
  10. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. Cissé, M.A., Sunyach, C., Lefranc-Jullien, S., Postina, R., Vincent, B., Checler, F. J. Biol. Chem. (2005) [Pubmed]
  11. Involvement of ADAM9 in multinucleated giant cell formation of blood monocytes. Namba, K., Nishio, M., Mori, K., Miyamoto, N., Tsurudome, M., Ito, M., Kawano, M., Uchida, A., Ito, Y. Cell. Immunol. (2001) [Pubmed]
  12. ADAM12 in human liver cancers: TGF-beta-regulated expression in stellate cells is associated with matrix remodeling. Le Pabic, H., Bonnier, D., Wewer, U.M., Coutand, A., Musso, O., Baffet, G., Clément, B., Théret, N. Hepatology (2003) [Pubmed]
  13. A secreted form of human ADAM9 has an alpha-secretase activity for APP. Hotoda, N., Koike, H., Sasagawa, N., Ishiura, S. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  14. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. Roghani, M., Becherer, J.D., Moss, M.L., Atherton, R.E., Erdjument-Bromage, H., Arribas, J., Blackburn, R.K., Weskamp, G., Tempst, P., Blobel, C.P. J. Biol. Chem. (1999) [Pubmed]
  15. The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrins. Mahimkar, R.M., Visaya, O., Pollock, A.S., Lovett, D.H. Biochem. J. (2005) [Pubmed]
  16. Overexpression of ADAM9 enhances growth factor-mediated recycling of E-cadherin in human colon cancer cell line HT29 cells. Hirao, T., Nanba, D., Tanaka, M., Ishiguro, H., Kinugasa, Y., Doki, Y., Yano, M., Matsuura, N., Monden, M., Higashiyama, S. Exp. Cell Res. (2006) [Pubmed]
  17. Expression of ADAM-9 mRNA and protein in human breast cancer. O'Shea, C., McKie, N., Buggy, Y., Duggan, C., Hill, A.D., McDermott, E., O'Higgins, N., Duffy, M.J. Int. J. Cancer (2003) [Pubmed]
  18. Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta. Nelson, K.K., Schlöndorff, J., Blobel, C.P. Biochem. J. (1999) [Pubmed]
  19. The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs. Amour, A., Knight, C.G., English, W.R., Webster, A., Slocombe, P.M., Knäuper, V., Docherty, A.J., Becherer, J.D., Blobel, C.P., Murphy, G. FEBS Lett. (2002) [Pubmed]
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