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CARCINOGENESIS: Expression of cytochrome P450s and glutathione S-transferases in human esophagus with squamous-cell carcinomas
1Departments of Hygiene, Shinshu University School of Medicine Matsumoto 390, Japan
2Second Surgery, Shinshu University School of Medicine Matsumoto 390, Japan
3Biochemistry, Shinshu University School of Medicine Matsumoto 390, Japan
4Department of Thoracic Surgery, Fourth Affiliated Hospital of Hebei Medical University 5 Jiankang Road, Shijiazhuang, 050011, China
5Department of Industrial Hygiene and Toxicology, Finnish Institute of Occupational Health Topeliuksenkatu 41 a A, SF-00250 Helsinki, Finland
6To whom correspondence should be addressed
In order to clarify the expression of cytochrome P450 and glutathione S-transferase in human esophagus, 41 samples of human esophagus with squamous-cell carcinoma were investigated by immunoblot analysis and enzyme assays. Cytochrome P450 1A2/1 was clearly expressed in micro-somes, and the amount in samples with tumorous tissue was significantly greater than that in samples without tumorous tissues or in liver; cytochrome P450 2B6 and 3A4/3 were expressed polymorphically. Aryl hydrocarbon hydroxylase activity was detected in microsomes and was greater in samples from smokers than non-smokers. Patients who both smoked and drank alcohol, however, had activity similar to that of patients without these habits. Glutathione S-transferase Ml and A1/2 protein existed polymorphically in cytosol, and glutathione S-transferase Pl-1 was detected in all samples.The frequency of expression of the glutathione S-transferase A1/2 protein was greater in patients with Ml protein than in those without; no difference in the expression was seen for glutathione S-transferase Pl-1. Neither smoking nor drinking influenced the expression or activity of glutathione S-transferase. Our data support the idea that some carcinogens can be directly activated or inactivated in human esophageal epithelium.
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