Ethylene oxide-protein adduct formation in humans : influence of glutathione-S-transferase polymorphisms.
The influence of the polymorphic human glutathione-S-transferase (GST) T1 and Ml genotypes (classified as « conjugators » and « nonconjugators ») on the biological effects of nonoccupational ethylene oxide exposure as reflected by the formation of globin N2-hydroxyethylvaline adducts was investigated.
Specific attention was paid to smoking as a potential source of exposure.
A total of 27 Caucasian subjects, including 10 women and 17 men, participated in the study.
Volunteers were grouped as smokers, i.e., 6 subjects (5 male, I female), and nonsmokers, i.e.. 21 subjects (12 male. 9 female).
The regular cigarette consumption in the smoker group ranged from 10 to 25 cigarettes/day.
The amount of N2-hydroxyethylvaline (HEV) bound to the N-terminal valine in human globin was determined following a procedure described by Bader and co-workers and the Deutsche Forschungs-gemeinschaft.
The GST genotypes were determined by a polymerase chain reaction (PCR) analysis outlined by Bell and colleagues (with bêta-globin serving as an internal standard) and Kempkes and co-workers (coamplification of the GSTTI fragment).
The median level of HEV detected in the smoker group was 280 pmol/g globin as compared with the median value of 50 pmol/g globin recorded for the nonsmokers, indicating that ethylene oxide intake from cigarettes may result in a ~5-fold higher overall HEV level in smokers in comparison with nonsmoking individuals. (...)
Mots-clés Pascal : Oxirane, Exposition, Environnement, Toxicité, Homme, Normal, Comparaison interindividuelle, Tabagisme, Polymorphisme, Génétique, Génotype, Adduit moléculaire, Protéine, Hydroxyéthylation, Valine, Aminoacide, Glutathione transferase, Transferases, Enzyme
Mots-clés Pascal anglais : Ethylene oxide, Exposure, Environment, Toxicity, Human, Normal, Interindividual comparison, Tobacco smoking, Polymorphism, Genetics, Genotype, Molecular adduct, Protein, Hydroxyethylation, Valine, Aminoacid, Glutathione transferase, Transferases, Enzyme
Notice produite par :
Inist-CNRS - Institut de l'Information Scientifique et Technique
Cote : 99-0031542
Code Inist : 002B03L06. Création : 31/05/1999.