Studies on the subcellular localization and role of glutathione-insulin transhydrogenase in rat liver.
125I-insulin was shown to be internalized in vivo to a discrete population of low-density membranes (ligandosomes), distinct from the +Golgi, endoplasmic reticulum, plasma membrane, and lysosomes. However, analytical subcellular fractionation shows that glutathione-insulin transhydrogenase is localized to the endoplasmic reticulum. Measurement of the specific enzyme activity of glutathione-insulin transhydrogenase showed no differences between normal, diabetic, and hyperinsulinaemic rats. These results suggest that glutathione-insulin transhydrogenase is not directly involved in the subcellular processing of receptor-bound internalized insulin.
D000818:Animals; D006946:Hyperinsulinism / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008297:Male; D010088:Oxidoreductases / Q000032:analysis*; D011490:Protein Disulfide Reductase (Glutathione) / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology
D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione)