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Chemical Compound Review

cystamine     2-(2-aminoethyldisulfanyl) ethanamine

Synonyms: Cystinamin, Cystineamine, Lopac-C-7255, CHEMBL61350, AG-F-76066, ...
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Disease relevance of Decarboxycystine

  • When treatment began after the appearance of abnormal movements, cystamine extended survival, reduced associated tremor and abnormal movements and ameliorated weight loss [1].
  • Administration of cystamine in vivo partially corrects susceptibility to malaria in A/J mice, as measured by reduced blood parasitemia and decreased mortality [2].
  • These results show that cystamine potently suppresses HIV replication in human cells by contemporaneously blocking at least two independent steps of the viral life cycle, without affecting cell viability, suggesting that this compound may represent a new possibility towards the treatment of HIV-1 infection [3].
  • Cystamine does not affect viral transcription, translation or protein processing; indeed, all HIV proteins are present in a pattern similar to that of nontreated cells [3].
  • Instead, cystamine interferes with the orderly assembly of HIV virions, as shown by electron microscopy analysis, that reveals only defective viral particles in treated cells [3].

Psychiatry related information on Decarboxycystine


High impact information on Decarboxycystine


Chemical compound and disease context of Decarboxycystine


Biological context of Decarboxycystine

  • The exact contribution of the interrelated factors in cystamine inhibition of sickling (changes in oxygen affinity, mean corpuscular hemoglobin concentration, and minimum gelling concentration) has yet to be determined [12].
  • The combined pharmacological treatment with mithramycin and cystamine down-regulates ESET gene expression and reduces hypertrimethylation of histone H3 (K9) [13].
  • This protection is correlated with reduced apoptosis and inflammation and is reversed by treating mutant animals with cystamine [14].
  • Treatment with cystamine prior to DMN administration completely abolished the depression of protein synthesis and reduced by more than 90% the methylation by [14C]DMN of purine bases in liver DNA [15].
  • The enzyme is potently inactivated by cystamine, which apparently interacts with a sulfhydryl group at the active site to form a mixed disulfide [16].

Anatomical context of Decarboxycystine


Associations of Decarboxycystine with other chemical compounds


Gene context of Decarboxycystine


Analytical, diagnostic and therapeutic context of Decarboxycystine


  1. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Karpuj, M.V., Becher, M.W., Springer, J.E., Chabas, D., Youssef, S., Pedotti, R., Mitchell, D., Steinman, L. Nat. Med. (2002) [Pubmed]
  2. Complex genetic control of susceptibility to malaria: positional cloning of the Char9 locus. Min-Oo, G., Fortin, A., Pitari, G., Tam, M., Stevenson, M.M., Gros, P. J. Exp. Med. (2007) [Pubmed]
  3. Cystamine potently suppresses in vitro HIV replication in acutely and chronically infected human cells. Bergamini, A., Capozzi, M., Ghibelli, L., Dini, L., Salanitro, A., Milanese, G., Wagner, T., Beninati, S., Pesce, C.D., Amici, C. J. Clin. Invest. (1994) [Pubmed]
  4. Cystamine treatment is neuroprotective in the YAC128 mouse model of Huntington disease. Van Raamsdonk, J.M., Pearson, J., Bailey, C.D., Rogers, D.A., Johnson, G.V., Hayden, M.R., Leavitt, B.R. J. Neurochem. (2005) [Pubmed]
  5. Suppression of aggregate formation and apoptosis by transglutaminase inhibitors in cells expressing truncated DRPLA protein with an expanded polyglutamine stretch. Igarashi, S., Koide, R., Shimohata, T., Yamada, M., Hayashi, Y., Takano, H., Date, H., Oyake, M., Sato, T., Sato, A., Egawa, S., Ikeuchi, T., Tanaka, H., Nakano, R., Tanaka, K., Hozumi, I., Inuzuka, T., Takahashi, H., Tsuji, S. Nat. Genet. (1998) [Pubmed]
  6. Vanin-1 licenses inflammatory mediator production by gut epithelial cells and controls colitis by antagonizing peroxisome proliferator-activated receptor {gamma} activity. Berruyer, C., Pouyet, L., Millet, V., Martin, F.M., Legoffic, A., Canonici, A., Garcia, S., Bagnis, C., Naquet, P., Galland, F. J. Exp. Med. (2006) [Pubmed]
  7. Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher glutathione stores. Martin, F., Penet, M.F., Malergue, F., Lepidi, H., Dessein, A., Galland, F., de Reggi, M., Naquet, P., Gharib, B. J. Clin. Invest. (2004) [Pubmed]
  8. Cystamine inhibits human immunodeficiency virus-1 replication in cord blood-derived mononuclear phagocytes and lymphocytes. Ho, W.Z., Kaufman, D., Song, L., Cutillii, J.R., Douglas, S.D. Blood (1996) [Pubmed]
  9. Cystamine induces toxicity in hepatocytes through the elevation of cytosolic Ca2+ and the stimulation of a nonlysosomal proteolytic system. Nicotera, P., Hartzell, P., Baldi, C., Svensson, S.A., Bellomo, G., Orrenius, S. J. Biol. Chem. (1986) [Pubmed]
  10. Inhibition of melanin synthesis by cystamine in human melanoma cells. Qiu, L., Zhang, M., Sturm, R.A., Gardiner, B., Tonks, I., Kay, G., Parsons, P.G. J. Invest. Dermatol. (2000) [Pubmed]
  11. Neuroprotective effects of cystamine in aged parkinsonian mice. Tremblay, M.E., Saint-Pierre, M., Bourhis, E., Lévesque, D., Rouillard, C., Cicchetti, F. Neurobiol. Aging (2006) [Pubmed]
  12. Inhibition of erythrocyte sickling by cystamine, a thiol reagent. Hassan, W., Beuzard, Y., Rosa, J. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  13. ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease. Ryu, H., Lee, J., Hagerty, S.W., Soh, B.Y., McAlpin, S.E., Cormier, K.A., Smith, K.M., Ferrante, R.J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  14. Vanin-1-/- mice exhibit a glutathione-mediated tissue resistance to oxidative stress. Berruyer, C., Martin, F.M., Castellano, R., Macone, A., Malergue, F., Garrido-Urbani, S., Millet, V., Imbert, J., Duprè, S., Pitari, G., Naquet, P., Galland, F. Mol. Cell. Biol. (2004) [Pubmed]
  15. Dimethylnitrosamine-induced inhibition of hepatic protein synthesis in vitro and the effect of pretreatment with cystamine or pregnenolone-16alpha-carbonitrile. Kleihues, P., Margison, J.M., Margison, G.P. Cancer Res. (1975) [Pubmed]
  16. Gamma-glutamylcysteine synthetase. Interactions of an essential sulfhydryl group. Seelig, G.F., Meister, A. J. Biol. Chem. (1984) [Pubmed]
  17. Pantethine and cystamine deplete cystine from cystinotic fibroblasts via efflux of cysteamine-cysteine mixed disulfide. Butler, J.D., Zatz, M. J. Clin. Invest. (1984) [Pubmed]
  18. Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. Mishra, S., Murphy, L.J. J. Biol. Chem. (2004) [Pubmed]
  19. Trypanosoma brucei gamma-glutamylcysteine synthetase. Characterization of the kinetic mechanism and the role of Cys-319 in cystamine inactivation. Brekken, D.L., Phillips, M.A. J. Biol. Chem. (1998) [Pubmed]
  20. Interaction of L- and D-3-amino-1-chloro-2-pentanone with gamma-glutamylcysteine synthetase. Beamer, R.L., Griffith, O.W., Gass, J.D., Anderson, M.E., Meister, A. J. Biol. Chem. (1980) [Pubmed]
  21. Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase. Borrell-Pagès, M., Canals, J.M., Cordelières, F.P., Parker, J.A., Pineda, J.R., Grange, G., Bryson, E.A., Guillermier, M., Hirsch, E., Hantraye, P., Cheetham, M.E., Néri, C., Alberch, J., Brouillet, E., Saudou, F., Humbert, S. J. Clin. Invest. (2006) [Pubmed]
  22. Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities. Janowiak, B.E., Griffith, O.W. J. Biol. Chem. (2005) [Pubmed]
  23. The protective effects of cystamine in the R6/2 Huntington's disease mouse involve mechanisms other than the inhibition of tissue transglutaminase. Bailey, C.D., Johnson, G.V. Neurobiol. Aging (2006) [Pubmed]
  24. Cystamine inhibits HIV type 1 replication in cells of monocyte/macrophage and T cell lineages. Ho, W.Z., Zhu, X.H., Song, L., Lee, H.R., Cutilli, J.R., Douglas, S.D. AIDS Res. Hum. Retroviruses (1995) [Pubmed]
  25. Activation of latent transforming growth factor-beta1 is induced by mannose 6-phosphate/insulin-like growth factor-II receptor. Yang, L., Tredget, E.E., Ghahary, A. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society. (2000) [Pubmed]
  26. Inactivation of cathepsin B by active site-directed disulfide exchange. Application in covalent affinity chromatography. Evans, B., Shaw, E. J. Biol. Chem. (1983) [Pubmed]
  27. Modification of the proteolytic fragmentation pattern upon oxidation of cysteines from ribulose 1,5-bisphosphate carboxylase/oxygenase. Marín-Navarro, J., Moreno, J. Biochemistry (2003) [Pubmed]
  28. Putrescine accumulation in human pulmonary tumours. Hoet, P.H., Dinsdale, D., Verbeken, E.K., Demedts, M., Nemery, B. Br. J. Cancer (1996) [Pubmed]
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