Protein Information

Name demethylase
Synonyms DMTase; Demethylase; MBD 2; MBD2; Methyl CpG binding domain protein 2; Methyl CpG binding protein MBD2; NY CO 41; Demethylases…

Compound Information

Name carbon disulfide
CAS carbon disulfide

Reference List

PubMed Abstract RScore(About this table)
174709 Gopinath C, Ford JH: The role of microsomal hydroxylases in the modification of chloroform hepatotoxicity in rats. Br J Exp Pathol. 1975 Oct;56(5):412-22.


Male rats have a greater microsomal amidopyrine N-demethylase activity per unit weight of liver, a shorter hexobarbitone sleeping time and are more susceptible to the hepatotoxic effect of chloroform than female rats.
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932876 Gopinath G, Ford EJ: The influence of hepatic microsomal amidopyrine demethylase activity on halothane hepatotoxicity in the horse. J Pathol. 1976 Jun;119(2):105-12.

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6315019 Masuda Y, Nakayama N: Protective action of diethyldithiocarbamate and carbon disulfide against renal injury induced by chloroform in mice. Biochem Pharmacol. 1983 Nov 1;32(21):3127-35.

In CCl4-treated mice, in which liver microsomal monooxygenase activities were decreased markedly, and kidney microsomal aniline hydroxylase and p-nitroanisole demethylase activities were increased to about twice those of the untreated mice, renal toxicity of CHCl3 was greatly potentiated, and the latter effect was also blocked by both agents.
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1850173 Brady JF, Xiao F, Wang MH, Li Y, Ning SM, Gapac JM, Yang CS: Effects of disulfiram on hepatic P450IIE1, other microsomal enzymes, and hepatotoxicity in rats. Toxicol Appl Pharmacol. 1991 Apr;108(2):366-73.

When a dose of disulfiram was given intragastrically to rats, a very rapid decrease of N-nitrosodimethylamine (NDMA) demethylase activity, possibly due to the inactivation of P450IIE1, was seen.
Carbon disulfide, a putative metabolite of disulfiram, produced similar effects on P450IIE1, but with shorter duration.
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3953292 Dalvi RR, Deoras DP: Metabolism of a dithiocarbamate fungicide thiram to carbon disulfide in the rat and its hepatotoxic implications. Acta Pharmacol Toxicol. 1986 Jan;58(1):38-42.

Furthermore, measurement of the activities of hepatic microsomal and serum enzymes at 5 hrs and 24 hrs following thiram treatment indicated that thiram caused significant loss of cytochrome P-450 and benzphetamine N-demethylase activity only at 24 hrs interval whereas there was significant elevation of sorbitol dehydrogenase (SDH) and serum glutamic oxalacetic transaminase (SGOT) activity at 5 and 24 hrs after treatment.
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131811 Gopinath C, Ford EJ: The effect of induced hepatic microsomal amidopyrine demethylase activity on the susceptibility of the liver of the calf and horse to carbon disulphide. J Comp Pathol. 1976 Apr;86(2):251-8.

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1311644 Lauriault VV, Khan S, O'Brien PJ: Hepatocyte cytotoxicity induced by various hepatotoxins mediated by cytochrome P-450IIE1: protection with diethyldithiocarbamate administration. Chem Biol Interact. 1992 Feb;81(3):271-89.

The objective of this study was to determine whether the thiol drug, diethyldithiocarbamate (DEDC) and its two metabolites, disulfiram (DS) and carbon disulfide (CS2) could be used as inhibitors of cytochrome P-450IIE1 to protect hepatocytes from cytotoxic xenobiotics. (1) Hepatocytes isolated from rats following pyrazole administration to induce cytochrome P-450IIE1 were much more susceptible to carbon tetrachloride (CCl4) and dimethylnitrosamine (DMN) than hepatocytes from untreated rats.
The activities of aniline hydroxylase and p-nitroanisole-O-demethylase increased whereas ethoxyresorufin-O-dealkylase activity was much less induced and pentoxyresorufin-O-dealkylase activity was decreased.
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2302746 Frank N, Bertram B, Scherf HR, Wiessler M: Influence of dithiocarbamates on the metabolism and toxicity of N-nitrosodimethylamine in rats. Carcinogenesis. 1990 Feb;11(2):199-203.

Five secondary amines and secondary amino acids were reacted with carbon disulfide to yield dithiocarbamates.
The following results were found. (i) All dithiocarbamates tested reduced the activity of N-nitrosodiethylamine-deethylase and completely inhibited the N-nitrosodimethylamine-demethylase in the rat liver.
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