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Gene Review

ADAM1A  -  ADAM metallopeptidase domain 1A (pseudogene)

Homo sapiens

Synonyms: ADAM1, ADAM1P, FTNAP, Ftna, PH-30a
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Disease relevance of ADAM1


Psychiatry related information on ADAM1

  • Furthermore, given the importance of integrins in maintaining short-term memory, alterations in ADAM proteins or their proteolytic activity could also play a proximal role in the clinico-pathological manifestations of Alzheimer disease [6].
  • Is Adam worth more than Eve? The financial impact of gender bias in the federal reimbursement of gynecological procedures [7].
  • Dr. William Cullen and Mr. Adam Smith: a case of hypochondriasis [8]?
  • The story of Adam and Eve, which depicts a growing self-determination being stymied and coming to grief, is a mythic epitome of this psychodynamic [9].
  • The Adam and Eve story as exemplar of an early-life variant of the oedipus complex [10].

High impact information on ADAM1


Chemical compound and disease context of ADAM1

  • 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) [15].
  • These data demonstrate for the first time that among the 13 different ADAM species, ADAM12m is highly expressed in human glioblastomas, and suggest the possibility that ADAM12m plays a role in the prominent proliferation of the glioblastomas through shedding of heparin-binding epidermal growth factor [16].
  • Moreover, female transgenics expressing ADAM 12-S exhibited increases in body weight, total body fat mass, abdominal fat mass, and herniation, but were normoglycemic and did not exhibit increased serum insulin, cholesterol, or triglycerides [17].
  • However, total oculocutaneous albinism (OCA) associated with deafness has been described only once, by Ziprkowski and Adam (Arch Dermatol 89:151-155, 1964) in an inbred family [18].
  • The existence of the so-called 'andropause' is an irrefutable fact, although the terms 'SLOH' (symptomatic late-onset hypogonadism) or 'symptomatic ADAM' (androgen deficiency of the aging male) are more accurate [19].

Biological context of ADAM1


Anatomical context of ADAM1

  • In this study, which ADAM was specifically expressed in monocytes stimulated with anti-CD98 antibody or RANKL and which factor(s) was functioning in monocytes as a fusion protein were investigated [24].
  • In contrast, the expression of the ADAM1/ADAM2 pair (fertilin alpha/fertilin beta, respectively) is not detected in fetal testis [20].
  • Studies using complementary DNA arrays indicated that the ADAM (A disintegrin and metalloproteinase) genes in gastric epithelial cells are differentially expressed after bacterial-epithelial interactions [25].
  • In this study, we identified the expression and the regulation of ADAM members (a disintegrin and metalloprotease) at both gene and protein levels during human osteoclast differentiation and activity [26].
  • Our results describe the expression and regulation of various ADAMs in human bone cells and the selective expression of ADAM 12L in osteoblasts [26].

Associations of ADAM1 with chemical compounds

  • Tumor necrosis factor-alpha converting enzyme (TACE or ADAM17) is a member of the ADAM (a disintegrin and metalloproteinase) family of type I membrane proteins and mediates the ectodomain shedding of various membrane-anchored signaling and adhesion proteins [27].
  • A disintegrin and metalloprotease (ADAM) transmembrane proteins have metalloprotease, integrin-binding, intracellular signaling and cell adhesion activities [28].
  • Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor [29].
  • Lysophosphatidic acid can generate epidermal growth factor receptor (EGFR) signal transactivation involving processing of EGFR ligands by ADAM (a disintegrin and metalloprotease) family metalloproteases [4].
  • Metargidin (ADAM-15) is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain) family of proteins and is widely expressed in different tissues and cell types [30].

Physical interactions of ADAM1

  • TACE/ADAM17 is a member of the adamalysin class of zinc-binding metalloproteases or ADAM (a disintegrin and metalloprotease) [31].
  • Further studies of the features of TIMP-3 that determine specific binding to both ADAM and glycosaminoglycan are required in order to understand these unique properties [32].

Regulatory relationships of ADAM1

  • TIMP-1 inhibition of TRAIL-induced apoptosis does not depend on its ability to inhibit matrix metalloproteinases or ADAM activities and is unrelated to its ability to stabilize active or decoy death receptors [33].
  • We have found using RNA interference analysis that a disintegrin and metalloproteinase (ADAM) 10 is responsible for the regulated shedding of the ectodomain of CD46 in apoptotic cells [34].

Other interactions of ADAM1

  • Indeed we found that alpha(9)beta(1) bound avidly to the disintegrin domains of ADAM1, 2, 3, and 9 but not to the disintegrin domains of ADAM10 and 17 [35].
  • Human ADAM15 is the only ADAM with the RGD motif in the disintegrin domain [35].
  • Interestingly, fertilin-alpha, ADAM9, and ADAM11 have potential fusion peptides [24].
  • Although this EGFR transactivation reportedly requires a disintegrin and metalloproteinase (ADAM) that sheds the ectodomain of EGFR ligands, the detailed mechanisms are still unknown [36].
  • By using inhibitors with differing potency toward different members of the ADAM (a disintegrin and metalloproteinase) family of proteases, we identified ADAM17 as a candidate mediator of stimulated ACE2 shedding [37].

Analytical, diagnostic and therapeutic context of ADAM1


  1. The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone. McCulloch, D.R., Harvey, M., Herington, A.C. Mol. Cell. Endocrinol. (2000) [Pubmed]
  2. 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]
  3. 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]
  4. Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cancer. Tanaka, Y., Miyamoto, S., Suzuki, S.O., Oki, E., Yagi, H., Sonoda, K., Yamazaki, A., Mizushima, H., Maehara, Y., Mekada, E., Nakano, H. Clin. Cancer Res. (2005) [Pubmed]
  5. 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]
  6. Altered cell-matrix associated ADAM proteins in Alzheimer disease. Gerst, J.L., Raina, A.K., Pirim, I., McShea, A., Harris, P.L., Siedlak, S.L., Takeda, A., Petersen, R.B., Smith, M.A. J. Neurosci. Res. (2000) [Pubmed]
  7. Is Adam worth more than Eve? The financial impact of gender bias in the federal reimbursement of gynecological procedures. Goff, B.A., Muntz, H.G., Cain, J.M. Gynecol. Oncol. (1997) [Pubmed]
  8. Dr. William Cullen and Mr. Adam Smith: a case of hypochondriasis? Barfoot, M. Proceedings of the Royal College of Physicians of Edinburgh. (1991) [Pubmed]
  9. The role of an early-life variant of the oedipus complex in motivating religious endeavors. Osman, M.P. Journal of the American Psychoanalytic Association. (2004) [Pubmed]
  10. The Adam and Eve story as exemplar of an early-life variant of the oedipus complex. Osman, M.P. Journal of the American Psychoanalytic Association. (2000) [Pubmed]
  11. Y chromosomes point to Native American Adam. Hutardo de Mendoza, D., Braginski, R. Science (1999) [Pubmed]
  12. ADAMs and cell fusion. Huovila, A.P., Almeida, E.A., White, J.M. Curr. Opin. Cell Biol. (1996) [Pubmed]
  13. An interpretation of Michelangelo's Creation of Adam based on neuroanatomy. Meshberger, F.L. JAMA (1990) [Pubmed]
  14. Shedding light on ADAM metalloproteinases. Huovila, A.P., Turner, A.J., Pelto-Huikko, M., Kärkkäinen, I., Ortiz, R.M. Trends Biochem. Sci. (2005) [Pubmed]
  15. 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]
  16. 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]
  17. ADAM 12 protease induces adipogenesis in transgenic mice. Kawaguchi, N., Xu, X., Tajima, R., Kronqvist, P., Sundberg, C., Loechel, F., Albrechtsen, R., Wewer, U.M. Am. J. Pathol. (2002) [Pubmed]
  18. Is autosomal recessive deafness associated with oculocutaneous albinism a "coincidence syndrome"? Lezirovitz, K., Nicastro, F.S., Pardono, E., Abreu-Silva, R.S., Batissoco, A.C., Neustein, I., Spinelli, M., Mingroni-Netto, R.C. J. Hum. Genet. (2006) [Pubmed]
  19. Andropause (or symptomatic late-onset hypogonadism): facts, fiction and controversies. Morales, A. The aging male : the official journal of the International Society for the Study of the Aging Male. (2004) [Pubmed]
  20. The ADAM-integrin-tetraspanin complex in fetal and postnatal testicular cords. Tres, L.L., Kierszenbaum, A.L. Birth Defects Res. C Embryo Today (2005) [Pubmed]
  21. 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]
  22. The human fertilin alpha gene is non-functional: implications for its proposed role in fertilization. Jury, J.A., Frayne, J., Hall, L. Biochem. J. (1997) [Pubmed]
  23. Identification and preliminary characterization of mouse Adam33. Gunn, T.M., Azarani, A., Kim, P.H., Hyman, R.W., Davis, R.W., Barsh, G.S. BMC Genet. (2002) [Pubmed]
  24. 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]
  25. ADAMs (a disintegrin and metalloproteinase) messenger RNA expression in Helicobacter pylori-infected, normal, and neoplastic gastric mucosa. Yoshimura, T., Tomita, T., Dixon, M.F., Axon, A.T., Robinson, P.A., Crabtree, J.E. J. Infect. Dis. (2002) [Pubmed]
  26. ADAM gene expression and regulation during human osteoclast formation. Verrier, S., Hogan, A., McKie, N., Horton, M. Bone (2004) [Pubmed]
  27. Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Endres, K., Anders, A., Kojro, E., Gilbert, S., Fahrenholz, F., Postina, R. Eur. J. Biochem. (2003) [Pubmed]
  28. The ADAMs family: Coordinators of nervous system development, plasticity and repair. Yang, P., Baker, K.A., Hagg, T. Prog. Neurobiol. (2006) [Pubmed]
  29. Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor. Fischer, O.M., Hart, S., Gschwind, A., Prenzel, N., Ullrich, A. Mol. Cell. Biol. (2004) [Pubmed]
  30. Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells. Nath, D., Slocombe, P.M., Stephens, P.E., Warn, A., Hutchinson, G.R., Yamada, K.M., Docherty, A.J., Murphy, G. J. Cell. Sci. (1999) [Pubmed]
  31. Characterization of the cDNA and gene for mouse tumour necrosis factor alpha converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25. Cerretti, D.P., Poindexter, K., Castner, B.J., Means, G., Copeland, N.G., Gilbert, D.J., Jenkins, N.A., Black, R.A., Nelson, N. Cytokine (1999) [Pubmed]
  32. Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail. Murphy, G., Knäuper, V., Lee, M.H., Amour, A., Worley, J.R., Hutton, M., Atkinson, S., Rapti, M., Williamson, R. Biochem. Soc. Symp. (2003) [Pubmed]
  33. Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells from extrinsic cell death: a potential oncogenic activity of tissue inhibitor of metalloproteinase-1. Liu, X.W., Taube, M.E., Jung, K.K., Dong, Z., Lee, Y.J., Roshy, S., Sloane, B.F., Fridman, R., Kim, H.R. Cancer Res. (2005) [Pubmed]
  34. ADAM10-mediated release of complement membrane cofactor protein during apoptosis of epithelial cells. Hakulinen, J., Keski-Oja, J. J. Biol. Chem. (2006) [Pubmed]
  35. 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]
  36. The mechanism of cleavage of EGFR ligands induced by inflammatory cytokines in gastric cancer cells. Tanida, S., Joh, T., Itoh, K., Kataoka, H., Sasaki, M., Ohara, H., Nakazawa, T., Nomura, T., Kinugasa, Y., Ohmoto, H., Ishiguro, H., Yoshino, K., Higashiyama, S., Itoh, M. Gastroenterology (2004) [Pubmed]
  37. Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2). Lambert, D.W., Yarski, M., Warner, F.J., Thornhill, P., Parkin, E.T., Smith, A.I., Hooper, N.M., Turner, A.J. J. Biol. Chem. (2005) [Pubmed]
  38. Role of integrins, tetraspanins, and ADAM proteins during the development of apoptotic bodies by spermatogenic cells. Kierszenbaum, A.L., Rosselot, C., Rivkin, E., Tres, L.L. Mol. Reprod. Dev. (2006) [Pubmed]
  39. The importance of shedding of membrane proteins for cytokine biology. Müllberg, J., Althoff, K., Jostock, T., Rose-John, S. Eur. Cytokine Netw. (2000) [Pubmed]
  40. Altered expression of ADAMs (A Disintegrin And Metalloproteinase) in fibrillating human atria. Arndt, M., Lendeckel, U., Röcken, C., Nepple, K., Wolke, C., Spiess, A., Huth, C., Ansorge, S., Klein, H.U., Goette, A. Circulation (2002) [Pubmed]
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