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Title: Benzene toxicity: emphasis on cytosolic dihydrodiol dehydrogenases

Abstract

Blood dyscrasias such as leukopenia and anemia have been clearly identified as consequences of chronic benzene exposure. The metabolites, phenol, catechol, and hydroquinone produced inhibition of /sup 59/Fe uptake in mice which followed the same time course as that produced by benzene. The inhibitor of benzene oxidation, 3-amino-1,2,4-triazole, mitigated the inhibitory effects of benzene and phenol only. These data support the contention that benzene toxicity is mediated by a metabolite and suggest that the toxicity of phenol is a consequence of its metabolism to hydroquinone and that the route of metabolism to catechol may also contribute to the production of toxic metabolite(s). The properties of mouse liver cytosolic dihydrodiol dehydrogenases were examined. These enzymes catalyze the NADP/sup +/-dependent oxidation of trans-1,2-dihydro-1,2-dihydroxybenzene (BDD) to catechol, a possible toxic metabolite of benzene produced via this metabolic route. Four distinct dihydrodiol dehydrogenases (DD1, DD2, DD3, and DD4) were purified to apparent homogeneity as judged by SDS polyacrylamide gel electrophoresis and isoelectric focusing. DD1 appeared to be identical to the major ketone reductase and 17..beta..-hydroxysteroid dehydrogenase activity in the liver. DD2 exhibited aldehyde reductase activity. DD3 and DD4 oxidized 17..beta..-hydroxysteroids, but no carbonyl reductase activity was detected. These relationships between BDD dehydrogenases and carbonylmore » reductase and/or 17..beta..-hydroxysteroid dehydrogenase activities were supported by several lines of evidence.« less

Authors:
Publication Date:
OSTI Identifier:
5741131
Alternate Identifier(s):
OSTI ID: 5741131
Resource Type:
Thesis/Dissertation
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; BENZENE; METABOLISM; TOXICITY; OXIDOREDUCTASES; ENZYME ACTIVITY; STEROIDS; LIVER; MICE; ANIMALS; AROMATICS; BODY; DIGESTIVE SYSTEM; ENZYMES; GLANDS; HYDROCARBONS; MAMMALS; ORGANIC COMPOUNDS; ORGANS; RODENTS; VERTEBRATES 560305* -- Chemicals Metabolism & Toxicology-- Vertebrates-- (-1987)

Citation Formats

Bolcsak, L.E. Benzene toxicity: emphasis on cytosolic dihydrodiol dehydrogenases. United States: N. p., 1982. Web.
Bolcsak, L.E. Benzene toxicity: emphasis on cytosolic dihydrodiol dehydrogenases. United States.
Bolcsak, L.E. Fri . "Benzene toxicity: emphasis on cytosolic dihydrodiol dehydrogenases". United States. doi:.
@article{osti_5741131,
title = {Benzene toxicity: emphasis on cytosolic dihydrodiol dehydrogenases},
author = {Bolcsak, L.E.},
abstractNote = {Blood dyscrasias such as leukopenia and anemia have been clearly identified as consequences of chronic benzene exposure. The metabolites, phenol, catechol, and hydroquinone produced inhibition of /sup 59/Fe uptake in mice which followed the same time course as that produced by benzene. The inhibitor of benzene oxidation, 3-amino-1,2,4-triazole, mitigated the inhibitory effects of benzene and phenol only. These data support the contention that benzene toxicity is mediated by a metabolite and suggest that the toxicity of phenol is a consequence of its metabolism to hydroquinone and that the route of metabolism to catechol may also contribute to the production of toxic metabolite(s). The properties of mouse liver cytosolic dihydrodiol dehydrogenases were examined. These enzymes catalyze the NADP/sup +/-dependent oxidation of trans-1,2-dihydro-1,2-dihydroxybenzene (BDD) to catechol, a possible toxic metabolite of benzene produced via this metabolic route. Four distinct dihydrodiol dehydrogenases (DD1, DD2, DD3, and DD4) were purified to apparent homogeneity as judged by SDS polyacrylamide gel electrophoresis and isoelectric focusing. DD1 appeared to be identical to the major ketone reductase and 17..beta..-hydroxysteroid dehydrogenase activity in the liver. DD2 exhibited aldehyde reductase activity. DD3 and DD4 oxidized 17..beta..-hydroxysteroids, but no carbonyl reductase activity was detected. These relationships between BDD dehydrogenases and carbonyl reductase and/or 17..beta..-hydroxysteroid dehydrogenase activities were supported by several lines of evidence.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Fri Jan 01 00:00:00 EST 1982},
month = {Fri Jan 01 00:00:00 EST 1982}
}

Thesis/Dissertation:
Other availability
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