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Gene Review

ADAM15  -  ADAM metallopeptidase domain 15

Homo sapiens

Synonyms: ADAM 15, Disintegrin and metalloproteinase domain-containing protein 15, MDC-15, MDC15, Metalloprotease RGD disintegrin protein, ...
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Disease relevance of ADAM15


High impact information on ADAM15

  • The elevated levels of ADAM15 in endothelial cells prompted an evaluation of its role in neovascularization [2].
  • A high level of expression of ADAM15 was found in vascular cells, the endocardium, hypertrophic cells in developing bone, and specific areas of the hippocampus and cerebellum [2].
  • Furthermore, the size of tumors resulting from implanted B16F0 mouse melanoma cells was significantly smaller in adam15(-/-) mice than in wild-type controls [2].
  • However, despite the pronounced expression of ADAM15 in these tissues, no major developmental defects or pathological phenotypes were evident in adam15(-/-) mice [2].
  • In a mouse model for retinopathy of prematurity, adam15(-/-) mice had a major reduction in neovascularization compared to wild-type controls [2].

Biological context of ADAM15


Anatomical context of ADAM15

  • Immunoprecipitation of ADAM15 from Jurkat cells confirmed the association with Lck in vivo, and upon PMA stimulation, the phosphorylation level of ADAM15 was increased [6].
  • Our data suggest that ADAM15 may be a novel component of adherens junctions and thus could play a role in endothelial functions that are mediated by these cell contacts [7].
  • Normal epithelial cells of the lung were negative or slightly positive for ADAM15 (score<2) [5].
  • Whereas transcripts for all metalloproteinases examined were detected in chondrocytes from human osteoarthritic cartilage in monolayer cultures, mRNAs for ADAM-15 and decysin were not present in fresh osteoarthritic human cartilage or explant cultures [9].
  • ADAM 15 was detected in perinatal cortical pyramidal cells; during aging there was also an increase in intracellular staining and the number of stained cells per volume (cell density) [10].

Associations of ADAM15 with chemical compounds

  • Thus, both integrin alpha(9)beta(1) and alpha(v)beta(3) recognize the ADAM15 disintegrin domain [11].
  • This was confirmed in vitro for Hck, Lck, and Grb2, which showed enhanced association with tyrosine-phosphorylated glutathione S-transferase-ADAM15 cytoplasmic domain compared with unphosphorylated protein [6].
  • ADAM 15 might be linked to AD via interaction with integrin and/or src protein tyrosine kinases [10].
  • Tetracycline-regulated ADAM15 overexpression in NIH3T3 cells leads to an inhibition of migration on a fibronectin-coated filter in a Boyden chamber assay and in a scratch wound model [12].
  • Antibodies raised against the cytoplasmic tail of metargidin recognize a glycoprotein of 110 kDa in MDA-MB-468 mammary epithelial carcinoma cells, which can be cell surface-biotinylated, indicating its localization in the plasma membrane [13].

Regulatory relationships of ADAM15

  • Reverse transcription PCR and real-time quantitative PCR analyses indicated that among the ADAMs, ADAM15 mRNA was more frequently expressed in the RA samples and its expression level was significantly 3.8-fold higher in RA than in OA (p < 0.01) [14].

Other interactions of ADAM15

  • ADAM10 and ADAM15 expressions correlated with the cleavage ratio [15].
  • Human ADAM15 is the only ADAM with the RGD motif in the disintegrin domain [11].
  • Using an in vitro assay using recombinant polypeptides expressed in Escherichia coli, we examined the ability of individual domains of human ADAM 12 and ADAM 15 to support tumor cell adhesion [16].
  • These data demonstrate selective, phosphorylation-dependent interactions of ADAM15 with Src family PTKs and Grb2, which highlight the potential for integration of ADAM functions and cellular signaling [6].
  • Expression of ADAMs 8, 9, and 17 were increased, and ADAM15 was decreased by stimulation of THP-1 with PMA, although these ADAMs were not regulated by PPAR gamma or RXR agonists [17].

Analytical, diagnostic and therapeutic context of ADAM15


  1. Distinct ADAM metalloproteinases regulate G protein-coupled receptor-induced cell proliferation and survival. Schäfer, B., Marg, B., Gschwind, A., Ullrich, A. J. Biol. Chem. (2004) [Pubmed]
  2. Potential role for ADAM15 in pathological neovascularization in mice. Horiuchi, K., Weskamp, G., Lum, L., Hammes, H.P., Cai, H., Brodie, T.A., Ludwig, T., Chiusaroli, R., Baron, R., Preissner, K.T., Manova, K., Blobel, C.P. Mol. Cell. Biol. (2003) [Pubmed]
  3. Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells. Ortiz, R.M., Kärkkäinen, I., Huovila, A.P. Genes Chromosomes Cancer (2004) [Pubmed]
  4. ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian cancer cell adhesion and motility in an RGD-dependent fashion. Beck, V., Herold, H., Benge, A., Luber, B., Hutzler, P., Tschesche, H., Kessler, H., Schmitt, M., Geppert, H.G., Reuning, U. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  5. Expression of ADAM15 in lung carcinomas. Schütz, A., Härtig, W., Wobus, M., Grosche, J., Wittekind, C.h., Aust, G. Virchows Arch. (2005) [Pubmed]
  6. Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. Poghosyan, Z., Robbins, S.M., Houslay, M.D., Webster, A., Murphy, G., Edwards, D.R. J. Biol. Chem. (2002) [Pubmed]
  7. ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin. Ham, C., Levkau, B., Raines, E.W., Herren, B. Exp. Cell Res. (2002) [Pubmed]
  8. Assignment of the ADAM15 gene to human chromosome band 1q21.3 by in situ hybridization. Kärkkäinen, I., Karhu, R., Huovila, A.P. Cytogenet. Cell Genet. (2000) [Pubmed]
  9. Effects of culture conditions and exposure to catabolic stimulators (IL-1 and retinoic acid) on the expression of matrix metalloproteinases (MMPs) and disintegrin metalloproteinases (ADAMs) by articular cartilage chondrocytes. Flannery, C.R., Little, C.B., Caterson, B., Hughes, C.E. Matrix Biol. (1999) [Pubmed]
  10. Comparative localization of ADAMs 10 and 15 in human cerebral cortex normal aging, Alzheimer disease and Down syndrome. Bernstein, H.G., Bukowska, A., Krell, D., Bogerts, B., Ansorge, S., Lendeckel, U. J. Neurocytol. (2003) [Pubmed]
  11. Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. Eto, K., Huet, C., Tarui, T., Kupriyanov, S., Liu, H.Z., Puzon-McLaughlin, W., Zhang, X.P., Sheppard, D., Engvall, E., Takada, Y. J. Biol. Chem. (2002) [Pubmed]
  12. ADAM15 overexpression in NIH3T3 cells enhances cell-cell interactions. Herren, B., Garton, K.J., Coats, S., Bowen-Pope, D.F., Ross, R., Raines, E.W. Exp. Cell Res. (2001) [Pubmed]
  13. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. Krätzschmar, J., Lum, L., Blobel, C.P. J. Biol. Chem. (1996) [Pubmed]
  14. Expression of ADAM15 in rheumatoid synovium: up-regulation by vascular endothelial growth factor and possible implications for angiogenesis. Komiya, K., Enomoto, H., Inoki, I., Okazaki, S., Fujita, Y., Ikeda, E., Ohuchi, E., Matsumoto, H., Toyama, Y., Okada, Y. Arthritis Res. Ther. (2005) [Pubmed]
  15. Altered expression of disintegrin metalloproteinases and their inhibitor in human dilated cardiomyopathy. Fedak, P.W., Moravec, C.S., McCarthy, P.M., Altamentova, S.M., Wong, A.P., Skrtic, M., Verma, S., Weisel, R.D., Li, R.K. Circulation (2006) [Pubmed]
  16. Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion. Iba, K., Albrechtsen, R., Gilpin, B.J., Loechel, F., Wewer, U.M. Am. J. Pathol. (1999) [Pubmed]
  17. Metalloproteinase expression in PMA-stimulated THP-1 cells. Effects of peroxisome proliferator-activated receptor-gamma (PPAR gamma) agonists and 9-cis-retinoic acid. Worley, J.R., Baugh, M.D., Hughes, D.A., Edwards, D.R., Hogan, A., Sampson, M.J., Gavrilovic, J. J. Biol. Chem. (2003) [Pubmed]
  18. Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling. Böhm, B.B., Aigner, T., Roy, B., Brodie, T.A., Blobel, C.P., Burkhardt, H. Arthritis Rheum. (2005) [Pubmed]
  19. ADAM15 upregulation and interaction with multiple binding partners in inflammatory bowel disease. Mosnier, J.F., Jarry, A., Bou-Hanna, C., Denis, M.G., Merlin, D., Laboisse, C.L. Lab. Invest. (2006) [Pubmed]
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