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Gene Review

AMD1  -  adenosylmethionine decarboxylase 1

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Disease relevance of AMD1


High impact information on AMD1


Biological context of AMD1

  • This increase was fully explained by a stabilization of the enzyme, probably caused by the binding of aminoguanidine to the active site of AdoMetDC [5].
  • These changes in the rates of SDC synthesis and degradation fully account for the observed biphasic enzyme induction curve [6].
  • A second elevation of SDC activity coincided with the entry of the cells into S phase at 24 hours [6].
  • Our findings suggest that RA treatment increases the intracellular polyamine concentration of RPE cells via activation of ODC, SAMDC and SAT and that this results in the promotion of RPE cell growth until the cells reach full confluency [7].

Associations of AMD1 with chemical compounds


Other interactions of AMD1


  1. Regulation of ornithine decarboxylase by hypoxia in pulmonary artery smooth muscle cells. Harrod, K.S., Olson, J.W., Gillespie, M.N. Am. J. Physiol. (1996) [Pubmed]
  2. Increased cellular levels of spermidine or spermine are required for optimal DNA synthesis in lymphocytes activated by concanavalin A. Fillingame, R.H., Jorstad, C.M., Morris, D.R. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  3. Cell-specific translation of S-adenosylmethionine decarboxylase mRNA. Regulation by the 5' transcript leader. Hill, J.R., Morris, D.R. J. Biol. Chem. (1992) [Pubmed]
  4. Isolation of a cDNA clone encoding S-adenosylmethionine decarboxylase. Expression of the gene in mitogen-activated lymphocytes. Mach, M., White, M.W., Neubauer, M., Degen, J.L., Morris, D.R. J. Biol. Chem. (1986) [Pubmed]
  5. Stabilization of S-adenosylmethionine decarboxylase by aminoguanidine. Stjernborg, L., Persson, L. Biochem. Pharmacol. (1993) [Pubmed]
  6. Regulation of the level of S-adenosylmethionine decarboxylase during lymphocyte mitogenesis. Morris, D.R., Degen, J.L., Oleinik, O.E., Seyfried, C.E. Med. Biol. (1981) [Pubmed]
  7. Effect of retinoic acid on proliferation and polyamine metabolism in cultured bovine retinal pigment epithelial cells. Yasunari, T., Yanagihara, N., Komatsu, T., Moriwaki, M., Shiraki, K., Miki, T., Yano, Y., Otani, S. Ophthalmic Res. (1999) [Pubmed]
  8. Inhibition of S-adenosylmethionine decarboxylase and diamine oxidase activities by analogues of methylglyoxal bis(guanylhydrazone) and their cellular uptake during lymphocyte activation. Jänne, J., Morris, D.R. Biochem. J. (1984) [Pubmed]
  9. The involvement of polyamines in the proliferation of cultured retinal pigment epithelial cells. Yanagihara, N., Moriwaki, M., Shiraki, K., Miki, T., Otani, S. Invest. Ophthalmol. Vis. Sci. (1996) [Pubmed]
  10. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain. Pajula, R.L., Raina, A., Eloranta, T. Eur. J. Biochem. (1979) [Pubmed]
  11. Polyamine synthesis in mammalian tissues. Isolation and characterization of spermidine synthase from bovine brain. Raina, A., Hyvönen, T., Eloranta, T., Voutilainen, M., Samejima, K., Yamanoha, B. Biochem. J. (1984) [Pubmed]
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