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© 1993 Oxford University Press

research-article

Glutathione S-transferases in esophageal cancer

Wilbert H.M. Peters, Theo Wobbes 1, Hennie M.J. Roelofs and Jan B.M.J. Jansen

Departments of Gastroenterology, University Hospital St Radboud Nijmegen, The Netherlands
1Departments of General Surgery, University Hospital St Radboud Nijmegen, The Netherlands

Glutathione content and glutathione S-transferase enzyme activity as well as isoenzyme composition were studied in normal gastric cardia, normal squamous esophageal epithelium and corresponding malignant tumor of 10 patients with esophageal cancer. Mean values of glutathione (38 ± 6 versus 36 ± 12 nmol/mg protein) and glutathione S-transferase activity (532 ± 44 versus 532 ± 108 nmol/min mg protein) did not differ significantly between normal esophageal and tumor tissue. However, great individual differences exist. In two patients, glutathione S-transferase activity was much higher in the tumor (1081 and 1381 nmol/min mg protein) due to overexpression of class alpha, mu and pi glutathione S-transferases in one case, and of class mu and pi in the other case. In the other patients, glutathione S-transferase activity was equal (one case) or lower (seven cases) in the tumor. In normal gastric cardia glutathione content as well as glutathione S-transferase activity was significantly lower as compared to normal esophageal epithelium. In conclusion, in contrast to other gastrointestinal tumors, glutathione S-transferases are overexpressed in esophageal tumors in only a limited number of patients.


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