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Chemical Compound Review

Dithiothreitol     (2S,3S)-1,4-bis- sulfanylbutane-2,3-diol

Synonyms: L-Dtt, AmbotzRL-1103, CHEMBL406270, CHEBI:42106, D9760_SIGMA, ...
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Disease relevance of Dithiothreitol


High impact information on Dithiothreitol

  • The suppression in caspase-3-like activity in hepatocytes exposed to an NO donor was partially blocked by an inhibitor of soluble guanylyl cyclase, 1H-[1,2,4]oxadiazolo[4,3, -a]quinoxalin-1-one, (ODQ), while the incubation of these lysates in DTT almost completely restored caspase-3-like activity to the level of TNFalpha-treated controls [4].
  • NO-dependent inhibition of T cell proliferation was associated with an inhibition of caspase activity and activation, and this effect was reversible by DTT [5].
  • However, neither DTT nor GSH was able to reverse the effect of NO*. In contrast to SIN-1, DTT had no effect when added to the cis (extracellular) side of the chamber [6].
  • In contrast, when intact PAEC or isolated total membranes derived from PAEC were treated with increasing concentrations (1 to 5 mM) of the disulfide-reducing agent dithiothreitol (DTT), but not oxidized DTT, NO synthase activity was increased by 20 to 85% [7].
  • Complete protection from DTT inhibition of [3H]FNZ binding by FNZ (an agonist) or by Ro 15-1788 (an antagonist) suggests the presence of -SS- at, or very close to, the BZD recognition binding site [8].

Biological context of Dithiothreitol


Anatomical context of Dithiothreitol

  • It has been shown previously that the thioredoxin system (thioredoxin + thioredoxin reductase + NADPH) may replace dithiothreitol (DTT) as a cofactor for vitamin KO and K reductase in salt-washed detergent-solubilized bovine liver microsomes [13].
  • Photoaffinity labeling experiments with [3H]FNZ revealed a clear-cut band of 50 kDa in native and alkylated membranes but an extremely weak label in 5 mM DTT/IAA-treated membranes [8].
  • A biphasic response to DTT was obtained with BNF microsomes; inhibition of N-demethylation was seen only at low concentrations (0.1 mM) and a return to control values occurred at higher concentrations [14].
  • AFM inhibition was enhanced by preincubation of barley organelle extract in the presence of DTT [15].
  • Dithiothreitol (DTT), a sulfhydryl (SH) compound, failed to protect against the suppression of lymphocyte function by anthralin [16].

Associations of Dithiothreitol with other chemical compounds

  • These results suggest that Ni(II) and DTT form a reactive species, which may be responsible for causing guanine-specific DNA damage [9].
  • DNA damage induced by Ni(II) plus DTT was observed only when the DNA was treated with piperidine, suggesting that Ni(II) plus DTT caused only base damage [9].
  • Sodium azide, a potent and relatively specific scavenger of (1)O(2), inhibited DNA damage by Ni(II) in the presence of DTT, whereas the sequence specificity of DNA damage was different from that obtained by (1)O(2) generating agent [9].
  • The inactivation could be attenuated by antioxidants such as vitamin E, reduced glutathione, and menadione and also by a K vitamin in combination with DTT, but not by superoxide dismutase and catalase [10].
  • Investigation into the mechanism of this inactivation showed that quinone-like compounds were reduced by DTT establishing a reactive oxygen generating redox cycle the products of which (likely H(2)O(2)) inactivated the enzyme [17].

Gene context of Dithiothreitol

  • Finally, NAC and DTT exhibited significant inhibition of HO-1 mRNA and HO-1 promoter reporter activity induced by 15d-PGJ(2) [18].
  • Neither GSH nor DTT could restore lost ALDH activity after exposure of the enzyme to MeDTC sulfone [19].
  • The concentration of DTT required to obtain maximal enzyme activity may be as much as 485 times greater than the corresponding concentration of reduced thioredoxin that gives the same enzyme activity [20].
  • Activity of enolase inhibited by both acrylamide and DTT could not be restored to pre-inhibition rates following dialysis indicating that an irreversible interaction between acrylamide and enolase had taken place [21].
  • NO-induced loss of the catalytic activity of PKC-zeta was restored by incubation with the disulfide reducing agent dithiothreitol (DTT) as well as by purified thioredoxin or thioredoxin reductase [22].

Analytical, diagnostic and therapeutic context of Dithiothreitol

  • ELISA estimations of rheumatoid factor IgM, IgA, and IgG in sera from RA patients with high disease activity. DTT treatment studies [23].


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  3. Role of stress-activated MAP kinase P38 in cisplatin- and DTT-induced apoptosis of the esophageal carcinoma cell line Eca109. Zhang, Q.X., Feng, R., Zhang, W., Ding, Y., Yang, J.Y., Liu, G.H. World J. Gastroenterol. (2005) [Pubmed]
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  5. Nitric oxide-mediated inhibition of caspase-dependent T lymphocyte proliferation. Mahidhara, R.S., Hoffman, R.A., Huang, S., Wolf-Johnston, A., Vodovotz, Y., Simmons, R.L., Billiar, T.R. J. Leukoc. Biol. (2003) [Pubmed]
  6. Direct activation of K(Ca) channel in airway smooth muscle by nitric oxide: involvement of a nitrothiosylation mechanism? Abderrahmane, A., Salvail, D., Dumoulin, M., Garon, J., Cadieux, A., Rousseau, E. Am. J. Respir. Cell Mol. Biol. (1998) [Pubmed]
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  8. Involvement of a disulfide bond in the binding of flunitrazepam to the benzodiazepine receptor from bovine cerebral cortex. Otero de Bengtsson, M.S., Lacorazza, H.D., Biscoglio de Jiménez Bonino, M.J., Medina, J.H. J. Neurochem. (1993) [Pubmed]
  9. Site-specific hydroxylation at polyguanosine in double-stranded DNA by nickel(II) in the presence of SH compounds: comparison with singlet oxygen-induced DNA damage. Oikawa, S., Hiraku, Y., Fujiwara, T., Saito, I., Kawanishi, S. Chem. Res. Toxicol. (2002) [Pubmed]
  10. The potent antioxidant activity of the vitamin K cycle in microsomal lipid peroxidation. Vervoort, L.M., Ronden, J.E., Thijssen, H.H. Biochem. Pharmacol. (1997) [Pubmed]
  11. Chemical modification and structural analysis of the progesterone membrane binding protein from porcine liver membranes. Falkenstein, E., Eisen, C., Schmieding, K., Krautkrämer, M., Stein, C., Lösel, R., Wehling, M. Mol. Cell. Biochem. (2001) [Pubmed]
  12. Loss of mitochondrial membrane potential is not essential to hepatocyte killing by allyl alcohol. Rikans, L.E., Cai, D.Y., Hornbook, K.R. Toxicol. Lett. (1995) [Pubmed]
  13. Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase. Soute, B.A., Groenen-van Dooren, M.M., Holmgren, A., Lundström, J., Vermeer, C. Biochem. J. (1992) [Pubmed]
  14. Regulation of thiol environment of the N-demethylation and ring hydroxylation of N,N-dimethyl-4-aminoazobenzene (DAB) by rat liver microsomes. Levine, W.G. Drug Metab. Dispos. (1986) [Pubmed]
  15. Effects of the photobleaching herbicide, acifluorfen-methyl, on protoporphyrinogen oxidation in barley organelles, soybean root mitochondria, soybean root nodules, and bacteria. Jacobs, J.M., Jacobs, N.J., Borotz, S.E., Guerinot, M.L. Arch. Biochem. Biophys. (1990) [Pubmed]
  16. Anthralin, a non-phorbol tumor promoter, fails to inhibit metabolic cooperation in mutant human fibroblasts, but inhibits phytohemagglutinin-induced lymphocyte blastogenesis in vitro. Si, E.C., Pfeifer, R.W., Yim, G.K. Toxicology (1988) [Pubmed]
  17. Expression, preparation, and high-throughput screening of caspase-8: discovery of redox-based and steroid diacid inhibition. Smith, G.K., Barrett, D.G., Blackburn, K., Cory, M., Dallas, W.S., Davis, R., Hassler, D., McConnell, R., Moyer, M., Weaver, K. Arch. Biochem. Biophys. (2002) [Pubmed]
  18. Thiol antioxidant and thiol-reducing agents attenuate 15-deoxy-delta 12,14-prostaglandin J2-induced heme oxygenase-1 expression. Liu, J.D., Tsai, S.H., Lin, S.Y., Ho, Y.S., Hung, L.F., Pan, S., Ho, F.M., Lin, C.M., Liang, Y.C. Life Sci. (2004) [Pubmed]
  19. S-methyl N,N-diethylthiocarbamate sulfone, a potential metabolite of disulfiram and potent inhibitor of low Km mitochondrial aldehyde dehydrogenase. Mays, D.C., Nelson, A.N., Fauq, A.H., Shriver, Z.H., Veverka, K.A., Naylor, S., Lipsky, J.J. Biochem. Pharmacol. (1995) [Pubmed]
  20. Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfide. Silverman, R.B., Nandi, D.L. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  21. The etiology of toxic peripheral neuropathies: in vitro effects of acrylamide and 2,5-hexanedione on brain enolase and other glycolytic enzymes. Howland, R.D., Vyas, I.L., Lowndes, H.E., Argentieri, T.M. Brain Res. (1980) [Pubmed]
  22. Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells. Kahlos, K., Zhang, J., Block, E.R., Patel, J.M. Mol. Cell. Biochem. (2003) [Pubmed]
  23. ELISA estimations of rheumatoid factor IgM, IgA, and IgG in sera from RA patients with high disease activity. DTT treatment studies. Espersen, G.T., Ernst, E., Vestergaard, M., Grunnet, N. Scand. J. Rheumatol. Suppl. (1988) [Pubmed]
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