Lysosomal and non-lysosomal pathways of intracellular insulin degradation in isolated rat hepatocytes.
The amount of 125I-insulin associated with freshly isolated hepatocytes was increased 50% in the presence of 0.2 mM chloroquine (CQ) after 2 h of incubation. The degradation of insulin by the hepatocytes incubated with CQ was significantly diminished as compared with control cells. Hepatocytes incubated with 125I-insulin in the presence of CQ showed a slower rate of ligand dissociation than control cells. More TCA-precipitable and less TCA-soluble material appeared in the dissociation buffer of CQ-treated cells. However, CQ inhibited only 25-35% of intracellular insulin degradation. Non-lysosomal intracellular insulin degradation appears to be responsible for the remaining portion of the ligand degradation by isolated hepatocytes.
D000818:Animals; D002103:Cadaverine / Q000031:analogs & derivatives / Q000494:pharmacology; D002738:Chloroquine / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000378:metabolism*; D007424:Intracellular Fluid / Q000378:metabolism; D008099:Liver / Q000166:cytology* / Q000378:metabolism / Q000648:ultrastructure; D008247:Lysosomes / Q000502:physiology*; D011868:Radioisotopes; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000187:drug effects / Q000502:physiology
D007328:Insulin; D011868:Radioisotopes; D002738:Chloroquine; D011972:Receptor, Insulin; C008542:monodansylcadaverine; D002103:Cadaverine