TY - JOUR
AU - X Hu, A Pal, J Krzeminski, S Amin, Y C Awasthi, P Zimniak, S V Singh
AB - The specificities of human glutathione (GSH) S-transferase (GST) isozymes of class alpha (hGSTA1-1), mu (hGSTM1-1) and pi (hGSTP1-1), including the three allelic forms of hGSTP1-1 (hGSTP1-1(I104,A113), hGSTP1-1(V104,A113) and hGSTP1-1(V104,V113)), in catalyzing the GSH conjugation of anti-diol epoxide stereoisomers of 5-methylchrysene (anti-5-MeCDE) have been examined. The specific activities of human GSTs were significantly higher toward (+)-anti-5-MeCDE than toward the (-)-enantiomer of anti-5-MeCDE. All three variants of hGSTP1-1 were significantly more efficient than either hGSTA1-1 or hGSTM1-1 in GSH conjugation of (+)-anti-5-MeCDE. The catalytic efficiencies of hGSTP1-1 variants toward (+)-anti-5-MeCDE were in the order hGSTP1-1(I104,A113) > hGSTP1-1(V104,V113) > hGSTP1-1(V104,A113). The present study suggests that the I104,A113 allele, which is most frequent in human populations, may play a major role in the detoxification of (+)-anti-5-MeCDE. This may point to specificity, because previous studies from our laboratory have shown that the hGSTP1-1(V104,V113) isoform is significantly more efficient than the other two variants of hGSTP1-1 in catalyzing GSH conjugation of (+)-anti-7R,8S-dihydroxy-9S,10R-epoxy-7,8,9,10-tetrahydrobenzo(a)pyrene ((+)-anti-BPDE), the ultimate carcinogen of benzo(a)pyrene. Even though the mechanism of the differences in the activities of hGSTP1-1 variants toward anti-5-MeCDE versus anti-BPDE remains to be elucidated, it seems that the molecular configuration of the diol epoxide is an important determinant of the activity of hGSTP1-1 isoforms toward polycyclic aromatic hydrocarbon diol epoxides. « Previous | Next Article » Table of Contents This Article Carcinogenesis (1998) 19 (9): 1685-1689. doi: 10.1093/carcin/19.9.1685 » Abstract Free Full Text (PDF) Free Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Hu, X. Articles by Singh, S. V. 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TI - Specificities of human glutathione S-transferase isozymes toward anti-diol epoxides of methylchrysenes.
JO - Carcinogenesis
DO - 10.1093/carcin/19.9.1685
DA - 1998-09-01
UR - https://www.deepdyve.com/lp/oxford-university-press/specificities-of-human-glutathione-s-transferase-isozymes-toward-anti-mMfZsWz2Z2
SP - 1685
VL - 19
IS - 9
DP - DeepDyve
ER -