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In vitro studies of the influence of glutathione transferases and epoxide hydrolase on the detoxification of acrylamide and glycidamide in blood

Lookup NU author(s): Dr Alistair Henderson, Professor Bernard Golding

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Abstract

Enzymes involved in the metabolism of xenobiotic substances are often polymorphic in humans. Such genetic polymorphisms may result in inter-individual differences in detoxification of certain chemicals, and as a consequence, possibly affect health-risk assessments. This present work concerns studies of the influence of polymorphic enzymes in the detoxification of acrylamide and its metabolite glycidamide. Enzymes that enhance conjugation with glutathione (GSH), the glutathione transferases (GSTs), may influence the detoxification of both acrylamide and glycidamide, whereas the enzyme epoxide hydrolase (EH) should only catalyse the hydrolysis of glycidamide. In this study, the doses of acrylamide or glycidamide measured as specific adducts to hemoglobin (Hb) were analysed in blood samples after in vitro incubation with these compounds. Blood samples from individuals with different genotypes for GSTT1 and GSTM1 were studied. No significant differences in adduct levels depending on genotype were noted. In a parallel experiment, incubation with ethylene oxide was used as positive control. In this experiment individuals carrying GSTT1 showed lower adduct level increments from ethylene oxide than individuals lacking GSTT1. Furthermore, addition of ethacrynic acid or laurylamine, compounds which inhibit GST and EH, respectively, did not affect the adduct levels. These results suggest that neither GSTs nor EH have any significant effect on the blood dose, measured as Hb-adducts over time, after exposure to acrylamide or glycidamide. © 2004 Elsevier B.V. All rights reserved.


Publication metadata

Author(s): Paulsson B, Rannug A, Henderson AP, Golding BT, Tornqvist M, Warholm M

Publication type: Article

Publication status: Published

Journal: Mutation Research: Genetic Toxicology and Environmental Mutagenesis

Year: 2005

Volume: 580

Issue: 1-2

Pages: 53-59

ISSN (print): 1383-5718

ISSN (electronic): 1568-7864

Publisher: Elsevier BV

URL: http://dx.doi.org/10.1016/j.mrgentox.2004.11.006

DOI: 10.1016/j.mrgentox.2004.11.006

PubMed id: 15668107


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