Activity of glutathione-dependent enzymes in long term diabetes. I. Activity of glutathione S-transferase and glutathione peroxidase in the liver of alloxan induced diabetic rats.
Cytosolic liver glutathione S-transferase (GST) activity was decreased for CDNB and DCNB as substrates in long term alloxan induced diabetes. Similar to cytosolic, microsomal glutathione S-transferase activity was also decreased for CDNB. In contrast, both microsomal and cytosolic GST activities for ETA as well as cytosolic and microsomal glutathione (GSH) contents were unaffected. The activity of Se-dependent glutathione peroxidase activity, but not nonSe-dependent peroxidase activity was increased in diabetic rats. The results suggest that diabetic state has a different effect on each isoenzyme of hepatic glutathione S-transferase activity. After insulin treatment of diabetic animals the activities of both cytosolic and microsomal GST was not restored and the activity of non Se-GSHPx was significantly lower than the control value.
Suchocka
Z
Z
Department of Biochemistry and Clinical Chemistry, Faculty of Pharmacy, School of Medicine, Warsaw, Poland.
Kobylińska
K
K
Pachecka
J
J
D000496:Alloxan; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D003921:Diabetes Mellitus, Experimental / Q000139:chemically induced / Q000201:enzymology*; D005978:Glutathione / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D051381:Rats
D000496:Alloxan; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D005978:Glutathione