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At least 19 recordsLinked to original sources
PubMed1992

Regional distribution of neuropeptide-degrading enzyme activity in the rat brain: effects of subacute exposure to carbon disulfide.

Carbon disulfide, a volatile solvent, is widely used in industry. It has been demonstrated that it causes several neuropsychological symptoms. However, the neurochemical basis of its neurotoxic effect is relatively unknown. In this paper we have measured the effect of subacute i.p. administration on neutral and basic aminopeptidase activities in discrete zones of the rat brain using lysine- and leucine-2-naphthylamides as substrates. Neutral aminopeptidase activity showed a significant decrease in the thalamus and cerebellum with marked (not significant) changes in the hypothalamus, hippocampus, medulla, and occipital cortex. There were no changes in basic aminopeptidase activity. It is suggested that aminopeptidase activity could play a role in carbon disulfide neurotoxic action in the aforementioned regions by generating changes in several neuropeptide levels.

2-Naphthylamine↗
PubMed1981

Neurobehavioral toxicity of carbon disulfide.

Carbon disulfide is an exceptionally potent neurotoxicant. In industrial settings its effects are pernicious, producing symptoms and behavioral alterations in the absence of frank poisoning; affective disorders are common, and exposure is associated with an elevated incidence of suicide. With more severe exposure, sensory disturbances are commonplace, as are alterations in sensory and motor nerve function. Alterations in behavior and central nervous system function can be readily produced in the laboratory with acute or chronic carbon disulfide exposure. Profound morphological changes, especially in the basal ganglia, can be produced with intense exposure. Dopamine beta-hydroxylase inhibition has been demonstrated in vivo and in vitro. Despite prolonged interest in its health effects, the toxic sequelae of exposure have not been adequately described using modern techniques of neurobehavioral toxicology, nor have the mechanisms of action been adequately elucidated.

Animals↗
PubMedDate not supplied

Covalent cross-linking of proteins by carbon disulfide.

Carbon disulfide is known to react with amino groups of proteins to generate dithiocarbamates (2). We observed covalent cross-linking of dithiocarbamate-derivatized proteins under physiological conditions which may occur through several mechanisms. Evidence for the structure of these covalent bridges and the reactive intermediate was obtained using 13C NMR spectroscopy in conjunction with specific isotopic labeling. On incubation at 37 degrees C oxidative coupling of dithiocarbamates generated bis(thiocarbamoyl) disulfides (3) which were reduced by cysteine. In addition, an electrophilic isothiocyanate (4) was generated from decomposition of the dithiocarbamate. Nucleophilic addition of sulfhydryl and amine moieties to the isothiocyanate produced dithiocarbamate ester (5) and thiourea linkages (6), respectively. Evidence for the presence of inter- and intramolecular cross-links was obtained using denaturing polyacrylamide gel electrophoresis under reducing conditions. The formation of isothiocyanate in neutral solution, through elimination of sulfhydryl ion, was correlated with increased pKa values of the parent amine of amino acids. Dithiocarbamates derived from terminal amino groups of proteins did not appear to generate isothiocyanate or form thiourea or dithiocarbamate ester. Both the thiourea and the dithiocarbamate ester were stable at reduced pH, whereas in alkaline media the thiourea was stable but dithiocarbamate ester was hydrolyzed. Although the disulfide and ester linkages were formed more rapidly than the thiourea, generation of the latter appeared to be irreversible, leading to its gradual accumulation over a longer period of time. Generation of isothiocyanate by CS2-derived dithiocarbamates and subsequent covalent cross-linking of proteins may provide a molecular mechanism for CS2-induced axonopathy.

Amino Acids↗
PubMed1990

Inhibition of ammonia monooxygenase in Nitrosomonas europaea by carbon disulfide.

Carbon disulfide has long been recognized as a potent inhibitor of nitrification, and it is the likely active component in several nitrification inhibitors suitable for field use. The effects of this compound on Nitrosomonas europaea have been investigated, and the site of action has been determined. Low concentrations of CS2 (less than 400 microM) produced a time-dependent inhibition of ammonia-dependent O2 uptake but did not inhibit hydrazine-oxidizing activity. CS2 also produced distinct changes in difference spectra of whole cells. These results suggest that ammonia monooxygenase (AMO) is the site of action of CS2. Unlike the case for thiourea and acetylene, saturating concentrations of CS2 did not fully inhibit AMO, and the inhibition resulted in a low but significant rate of ammonia-dependent O2 uptake. The effects of CS2 were not competitive with respect to ammonia concentration, and the inhibition by CS2 did not require the turnover of AMO to take effect. The ability of CS2-treated cells to incorporate [14C]acetylene into the 28-kilodalton polypeptide of AMO was used to demonstrate that the effects of CS2 are compatible with a mode of action which involves a reduction of the rate of turnover of AMO without effects on the catalytic mechanism. It is proposed that CS2 may act on AMO by reversibly reacting with a suitable nucleophilic amino acid in close proximity to the active site copper.

Acetylene↗
PubMed1989

[Inhalation of carbon disulfide--studies of carbon disulfide uptake in dynamic dose administration lasting 4 hours].

Experiments of CS2 inhalation were accomplished with both constant loads at the ergometer combined with constant concentration of inhalation and discontinuous offered doses combined with various physical loads during 240 minutes. The conditions of the experiment were approximated to the real conditions of exposure at a viscose rayon fibres production. The intake of CS2 increased by 20 percent in case of various conditions. The cause of this finding is a different adaptation during the intake phase in opposition to the breath off phase. The profile of the exposure affected by changed CS2 concentrations and various physical activities is decisive for the intake dosage and thus for the health risk.

Administration, Inhalation↗
PubMed1983

Blood-bound carbon disulfide: an indicator of carbon disulfide exposure, and its accumulation in repeatedly exposed rats.

Carbon disulfide is present in exposed subjects in free and bound or acid-labile forms. Sensitivities of the blood acid-labile CS2 (AL CS2) concentration and the modified iodine-azide test (IAT) were compared as indicators of CS2 exposure. Rats were exposed to 15 (approximately 5 ppm), 30, 60, or 120 mg/m3 of CS2. Exposure to 15 or 30 mg/m3 of CS2 could not be detected by the modified IAT. However, a linear relationship between blood CS2 (free or AL CS2) concentrations and these exposure levels was observed. Free CS2 is eliminated rapidly, while AL CS2 is eliminated very slowly from the exposed subjects. Repetitive daily exposures (8 hr/day) to 120 mg/m3 of CS2 were carried out in rats. Blood AL CS2 concentrations in exposed rats increased with each successive exposure while the free CS2 level remained relatively constant. By the sixth or seventh daily exposure the blood AL CS2 concentration was about 2.5 times that of the first 8-hr exposure and about 3 times the level of free CS2. These results indicated an appreciable accumulation of CS2 in subjects repeatedly exposed to low concentrations of the solvent. Rats were also exposed to CS2 8 hr/day for 5 days. After a 2-day nonexposure period (Days 6 and 7), the animals were reexposed on Day 8. The blood AL CS2 concentration in animals exposed on Day 8 was substantially higher than in those that received a single 8-hr exposure (Day 1), despite the hiatus on Days 6 and 7. These results indicated that blood AL CS2 was not totally eliminated during the 2-day nonexposure period. In in vitro experiments, the binding profile of CS2 to human blood was remarkably similar to that of rats exposed to CS2 by inhalation.

Animals↗
PubMed1987

Experimental human exposure to carbon disulfide. I. Respiratory uptake and elimination of carbon disulfide under rest and physical exercise.

Six human volunteers were exposed to 10 and 20 ppm carbon disulfide at rest and to 3 and 10 ppm carbon disulfide under a 50 W level of physical exercise during four consecutive periods of 50 min. Every 5 min a sample was taken from the mixed exhaled air in which the concentration of carbon disulfide was determined. It was established that only an apparent steady state was reached during this exposure period. The retention values were established as 0.374 (SD = 0.106; n = 239) for exposure to 10 ppm carbon disulfide at rest and as 0.410 (SD = 0.103; n = 239) for exposure to 20 ppm carbon disulfide at rest. During exposure to 10 ppm and 3 ppm carbon disulfide, combined with a 50 W level of physical exercise, the retention values decreased to 0.286 (SD = 0.083; n = 239) and 0.277 (SD = 0.049; n = 239) respectively. Thereby, the measured individual retention values of carbon disulfide show considerable interindividual differences. The respiratory uptake of carbon disulfide (mg CS2) proved significantly influenced by the amount of body fat estimated from skinfold thickness measurements. The respiratory elimination of carbon disulfide in the exhaled air can be described by means of a two-exponential decay.

Adult↗