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1337960 
Journal Article 
Review 
GLUTATHIONE TRANSFERASES AND CANCER 
Tsuchida, S; Sato, K 
1992 
Yes 
Critical Reviews in Biochemistry and Molecular Biology
ISSN: 1040-9238
EISSN: 1549-7798 
27 
4-5 
337-384 
English 
1521461 
WOS:A1992JF51100002 
The glutathione transferases, a family of multifunctional
proteins, catalyze the glutathione conjugation reaction with electrophilic compounds
biotransformed from xenobiotics, including carcinogens. In preneoplastic cells as well as
neoplastic cells, specific molecular forms of glutathione tranferase are known to be expressed
and have been known to participate in the mechanisms of their resistance to drugs. In this
article, following a brief description of recently identified molecular forms, we review new
findings regarding the respective molecular forms involved in carcinogenesis and anticancer drug
resistance, with particular emphasis on Pi class forms in preneoplastic tissues. The rat Pi class
form, GST-P (GST 7-7), is strongly expressed not only in hepatic foci and hepatomas, but also in
initiated cells that occur at the very early stages of chemical hepatocarcinogenesis, and is
regarded as one of the most reliable markers for preneoplastic lesions in the rat liver. 12-O-
Tetradecanoylphorbol-13-acetate (TPA)-responsive element-like sequences have been identified in
upstream regions of the GST-P gene, and oncogene products c-jun and c-fos are suggested to
activate the gene. The Pi-class forms possess unique enzymatic properties, including broad
substrate specificity, glutathione peroxidase activity toward lipid hydroperoxides, low
sensitivity to organic anion inhibitors, and high sensitivity to active oxygen species. The
possible functions of Pi class glutathione transferases in neoplastic tissues and drug-resistant
cells are discussed. 
GLUTATHIONE TRANSFERASES; CARCINOGENESIS; TUMOR MARKERS; DRUG-METABOLIZING ENZYMES; INDUCTION; CHEMOPREVENTION