Internalization and recycling of insulin receptors in hepatoma cells. Absence of regulation by receptor occupancy.
Insulin receptors of Fao hepatoma cells were labelled with a 125I-labelled photoreactive insulin analogue or by surface iodination catalysed by lactoperoxidase. Cells were then incubated at 37 degrees C, and the cellular localization of the labelled receptors was assessed by limited exposure of intact cells to trypsin. The results show that: (1) photolabelled insulin-receptor complexes are internalized and recycled in Fao hepatoma cells; (2) the dynamics of photolabelled insulin receptors (internalization and recycling) is similar before and after down-regulation; (3) the unoccupied receptors labelled by surface iodination are internalized and recycled similarly to covalent insulin-receptor complexes; (4) insulin does not induce internalization of surface-iodinated insulin receptors. We conclude that internalization and recycling of insulin receptors are independent of receptor occupancy by insulin in Fao hepatoma cells.
D000345:Affinity Labels; D000818:Animals; D001386:Azides; D002460:Cell Line; D011232:Chemical Precipitation; D004591:Electrophoresis, Polyacrylamide Gel; D007328:Insulin / Q000031:analogs & derivatives; D007457:Iodine Radioisotopes; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D046911:Macromolecular Substances; D051381:Rats; D011972:Receptor, Insulin / Q000187:drug effects / Q000276:immunology / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology; D014466:Ultraviolet Rays
D000345:Affinity Labels; D001386:Azides; D007328:Insulin; D007457:Iodine Radioisotopes; D046911:Macromolecular Substances; C035459:insulin, (2-nitro-4-azidophenylacetyl)(B2)-des-Phe(B1)-; D011972:Receptor, Insulin; D014357:Trypsin