Glutathione-S-transferase and GSH-peroxidase activities during the state of GSH-depletion leading to lipid peroxidation in rat liver
Siegers, C.P.; Hübscher, W.; Younes, M.
Research Communications in Chemical Pathology and Pharmacology 37(2): 163-169
1982
ISSN/ISBN: 0034-5164 PMID: 7134625 Document Number: 194968
Depletion of hepatic glutathione (GSH) in phenobarbital-induced rats by phorone (diisopropylidene acetone; 0.25 g/kg i.p.) or vinylidene chloride (VDC; 0.5 g/kg i.p.) led to an enhanced lipid peroxidation in vitro as evidenced by the measurements of malondialdehyde and conjugated dienes. During this state of GSH-depletion inducing lipid peroxidation no significant alterations in the activity of hepatic GSH-peroxidase were observed whereas the GSH-S-transferase activities towards an aryl substrate (CDNB) and an epoxide substrate (1,2-epoxy(p-nitrophenoxy)propane) significantly decreased under the treatments with VDC. The GSH-reductase activity was significantly reduced after treatment with either agent. These results clearly indicate 1st, that GSH-S-transferases are involved in the conjugation of GSH to VDC, 2nd, that GSH peroxidase remains unaffected during lipid peroxidation induced by GSH-depletion as a consequence of treatment with phorone or VDC, and 3rd, that the availability of reduced GSH may be decreased further under these conditions due to the lower content of glutathione reductase.