Glutathione-S-transferase activity in human superficial transitional cell carcinoma of the bladder comparison with healthy controls
✍ Scribed by Amalia Lafuente; Montserrat Giralt; Isabel Cervello; Francesc Pujol; Jordi Mallol
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 517 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0008-543X
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✦ Synopsis
Glutathione-S-transferase (GST) activity and glutathione (GSH) content have been studied in human urinary bladder (UB) specimens obtained from healthy controls (HC) (n = 8 ) and from patients with superficial transitional cell carcinoma (TCC) (n = 91, either in TCC and in adjacent normal (ANE) tissues of the same patient. The GST activity was significantly higher in TCC in comparison with ANE (ten fold) and with HC (five fold). This activity was also significantly higher in HC than in ANE (two fold). The K, values obtained in the whole population (1.26 I ~I 0.3 X i O P mol/l) suggest that a unique form of isoenzyme is present in the UB epithelium and that it is the same acidic form "p'' described in erythrocytes. The GSH content was significantly higher in TCC than in ANE (2.5 fold) and also that in HC (three fold). A good correlation between GST activity and GSH content was observed in HC hut not in TCC or ANE. These results demonstrate the relation between the activity of the GST system and the development of the TCC as well as its role in the cellular resistance to chemotherapy. A possible decrease of the GST activity before the development of the tumor is also discussed. Cancer 65:2064-2068,1990.
LUTATHIONE-S-TRANSFERASES (GST) are a family G of widely distributed catalytic and binding proteins that facilitate the conjugation of glutathione (GSH) with the electrophilic center of a large variety of hydrophobic molecules. Multiple forms of this enzyme which have different structural, catalytic, and immunologic properties have been reported in a number of rat and human tiss u e ~. ~, ~ Thus, previous studies have indicated that GST activity in human tissues can be expressed by several isoenzymes which, according to their electrical and structural, as well as immunologic properties, can be grouped into