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Glutathione S-transferase isoenzymes in human lung tumors
Authors:Singh  Shivendra V; Haque  Abida K; Ahmad  Hassan; Medh  Rheem D; Awasthi  Yogesh C
Institution:Departments of Human Biological Chemistry and Genetics, The University of Texas Medical Branch Galveston, TX 77550, USA
1Pathology, The University of Texas Medical Branch Galveston, TX 77550, USA
Abstract:In the present studies we have compared the levels of glutathione(GSH) and GSH-related enzymes in lung tumors and correspondingnormal tissues obtained from the same individuals. We have alsoimmunologically quantitated the relative amounts of glutathioneS-transferase {pi} (or GST-P) type antigen in tumors and adjacentnormal tissues from five patients. GST activities towards 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid were found to beelevated in tumors from two out of five patients (patients #1and 4), whereas the activity towards these substrates was markedlysuppressed in the tumor tissue from one of the patients (#5).Immunotitration and Western blot studies using antibodies raisedagainst {pi}-type GST isoenzymes of human lung and placenta indicatedinduction of GST {pi}-type isoenzyme in tumors from patients #1and 4 and suppression of this isoenzyme in tumor from patient#5. The tumors from patients #2 and 3 did not show any increasein GST activity or GST {pi}-type antigen. Except for the tumor frompatient #5, the GSH content was higher in the tumors from otherpatients. GSH reductase activity was found to be elevated intumors of all the patients examined in this study. These resultsindicate that GSH and GSH related enzymes are differentiallyaltered in lung tumors and GSH levels and GST {pi}- or GST-P-typeisoenzyme(s) are not uniformly elevated in all tumors.
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