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Gene Review

ADAM12  -  ADAM metallopeptidase domain 12

Homo sapiens

Synonyms: ADAM 12, ADAM12-OT1, CAR10, Disintegrin and metalloproteinase domain-containing protein 12, MCMP, ...
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Disease relevance of ADAM12


Psychiatry related information on ADAM12

  • ADAM 12 is a member of a family of disintegrin-containing metalloproteases that have been implicated in a variety of diseases including Alzheimer's disease, arthritis, and cancer [5].

High impact information on ADAM12

  • Recent evidence implicates three ADAMs, fertilin-alpha, fertilin-beta, and meltrin-alpha, in sperm-egg fusion and myoblast fusion [6].
  • We have examined the capacity of the major cytoplasmic membrane protein (MCMP) of Legionella pneumophila, a genus common antigen and member of the hsp 60 family of heat shock proteins, to induce protective immunity in a guinea pig model of Legionnaires' disease [7].
  • MCMP has potential as a vaccine against Legionnaires' disease [7].
  • Guinea pigs immunized with MCMP developed a strong cell-mediated immune response to the immunogen manifest by marked cutaneous delayed-type hypersensitivity [7].
  • Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP) [8].

Chemical compound and disease context of ADAM12


Biological context of ADAM12


Anatomical context of ADAM12

  • Northern blot analyses showed that HSCs, but not hepatocytes, expressed transcripts for ADAM9 messenger RNA (mRNA) and both the long and short forms of ADAM12 [1].
  • Finally, the endogenous Dll1 present in primary mouse myoblasts undergoes cleavage in confluent, differentiating myoblast cultures, and this cleavage is decreased by ADAM12 small interfering RNAs [12].
  • All three ADAMs were found to be significantly upregulated in GC compared to non-neoplastic foveolar epithelium, with ADAM12 expression being higher in intestinal- than in diffuse-type tumors [2].
  • Evaluation of the fusion rate with regard to the size of myotubes showed that both ADAM12 antisense oligonucleotides and alpha9beta1 blockade inhibited more importantly formation of large (> or =5 nuclei) myotubes than that of small (2-4 nuclei) myotubes [11].
  • Overexpression of ADAM12 at the cell surface of 3T3-L1 preadipocytes achieved by transient transfection or retroviral transduction led to the disappearance of the extensive network of actin stress fibers that are characteristic of these cells, and its reorganization into a cortical network located beneath the cell membrane [13].

Associations of ADAM12 with chemical compounds


Enzymatic interactions of ADAM12


Regulatory relationships of ADAM12


Other interactions of ADAM12


Analytical, diagnostic and therapeutic context of ADAM12


  1. 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]
  2. 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]
  3. Regulation of ADAM12 cell-surface expression by protein kinase C epsilon. Sundberg, C., Thodeti, C.K., Kveiborg, M., Larsson, C., Parker, P., Albrechtsen, R., Wewer, U.M. J. Biol. Chem. (2004) [Pubmed]
  4. ADAM12 is selectively overexpressed in human glioblastomas and is associated with glioblastoma cell proliferation and shedding of heparin-binding epidermal growth factor. Kodama, T., Ikeda, E., Okada, A., Ohtsuka, T., Shimoda, M., Shiomi, T., Yoshida, K., Nakada, M., Ohuchi, E., Okada, Y. Am. J. Pathol. (2004) [Pubmed]
  5. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. Roy, R., Wewer, U.M., Zurakowski, D., Pories, S.E., Moses, M.A. J. Biol. Chem. (2004) [Pubmed]
  6. ADAMs and cell fusion. Huovila, A.P., Almeida, E.A., White, J.M. Curr. Opin. Cell Biol. (1996) [Pubmed]
  7. Major cytoplasmic membrane protein of Legionella pneumophila, a genus common antigen and member of the hsp 60 family of heat shock proteins, induces protective immunity in a guinea pig model of Legionnaires' disease. Blander, S.J., Horwitz, M.A. J. Clin. Invest. (1993) [Pubmed]
  8. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. Iba, K., Albrechtsen, R., Gilpin, B., Fröhlich, C., Loechel, F., Zolkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, J.K., Sanderson, R.D., Brakebusch, C., Fässler, R., Wewer, U.M. J. Cell Biol. (2000) [Pubmed]
  9. ADAM 12 as a first-trimester maternal serum marker in screening for Down syndrome. Laigaard, J., Spencer, K., Christiansen, M., Cowans, N.J., Larsen, S.O., Pedersen, B.N., Wewer, U.M. Prenat. Diagn. (2006) [Pubmed]
  10. PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. Mori, S., Tanaka, M., Nanba, D., Nishiwaki, E., Ishiguro, H., Higashiyama, S., Matsuura, N. J. Biol. Chem. (2003) [Pubmed]
  11. ADAM12 and alpha9beta1 integrin are instrumental in human myogenic cell differentiation. Lafuste, P., Sonnet, C., Chazaud, B., Dreyfus, P.A., Gherardi, R.K., Wewer, U.M., Authier, F.J. Mol. Biol. Cell (2005) [Pubmed]
  12. Proteolytic Processing of Delta-like 1 by ADAM Proteases. Dyczynska, E., Sun, D., Yi, H., Sehara-Fujisawa, A., Blobel, C.P., Zolkiewska, A. J. Biol. Chem. (2007) [Pubmed]
  13. ADAM12 induces actin cytoskeleton and extracellular matrix reorganization during early adipocyte differentiation by regulating beta1 integrin function. Kawaguchi, N., Sundberg, C., Kveiborg, M., Moghadaszadeh, B., Asmar, M., Dietrich, N., Thodeti, C.K., Nielsen, F.C., Möller, P., Mercurio, A.M., Albrechtsen, R., Wewer, U.M. J. Cell. Sci. (2003) [Pubmed]
  14. 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]
  15. Involvement of the serine/threonine p70S6 kinase in TGF-beta1-induced ADAM12 expression in cultured human hepatic stellate cells. Le Pabic, H., L'Helgoualc'h, A., Coutant, A., Wewer, U.M., Baffet, G., Clément, B., Théret, N. J. Hepatol. (2005) [Pubmed]
  16. Amyloid-beta neurotoxicity is mediated by FISH adapter protein and ADAM12 metalloprotease activity. Malinin, N.L., Wright, S., Seubert, P., Schenk, D., Griswold-Prenner, I. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  17. Heparan sulfate regulates ADAM12 through a molecular switch mechanism. Sørensen, H.P., Vivès, R.R., Manetopoulos, C., Albrechtsen, R., Lydolph, M.C., Jacobsen, J., Couchman, J.R., Wewer, U.M. J. Biol. Chem. (2008) [Pubmed]
  18. Reduction of the disintegrin and metalloprotease ADAM12 in preeclampsia. Laigaard, J., Sørensen, T., Placing, S., Holck, P., Fröhlich, C., Wøjdemann, K.R., Sundberg, K., Shalmi, A.C., Tabor, A., Nørgaard-Pedersen, B., Ottesen, B., Christiansen, M., Wewer, U.M. Obstetrics and gynecology. (2005) [Pubmed]
  19. Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity. Yoshinaka, T., Nishii, K., Yamada, K., Sawada, H., Nishiwaki, E., Smith, K., Yoshino, K., Ishiguro, H., Higashiyama, S. Gene (2002) [Pubmed]
  20. Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. McKie, N., Edwards, T., Dallas, D.J., Houghton, A., Stringer, B., Graham, R., Russell, G., Croucher, P.I. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  21. RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis. Bourd-Boittin, K., Le Pabic, H., Bonnier, D., L'Helgoualc'h, A., Théret, N. J. Biol. Chem. (2008) [Pubmed]
  22. The level of ADAM12-S in maternal serum is an early first-trimester marker of fetal trisomy 18. Laigaard, J., Christiansen, M., Fröhlich, C., Pedersen, B.N., Ottesen, B., Wewer, U.M. Prenat. Diagn. (2005) [Pubmed]
  23. ADAM12 is a four-leafed clover: the excised prodomain remains bound to the mature enzyme. Wewer, U.M., Mörgelin, M., Holck, P., Jacobsen, J., Lydolph, M.C., Johnsen, A.H., Kveiborg, M., Albrechtsen, R. J. Biol. Chem. (2006) [Pubmed]
  24. Molecular profiling of ADAM12 in human bladder cancer. Fröhlich, C., Albrechtsen, R., Dyrskjøt, L., Rudkaer, L., Ørntoft, T.F., Wewer, U.M. Clin. Cancer Res. (2006) [Pubmed]
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