In rat hepatocytes the Golgi complex contains a considerable amount of receptors for asialoglycoproteins (ASGP-R). To establish whether the presence of ASGP-R in the Golgi complex originate from de novo synthesis isolated rat hepatocytes were incubated with 100 micrograms/ml cycloheximide to stop protein synthesis. Provided that protein synthesis was completely inhibited by cycloheximide, uptake and degradation of ligand (asialo-orosomucoid) were unaffected. Also intracellular transport of newly synthesized proteins, as determined by monitoring biosynthesis and intracellular transport of albumin and ASGP-R, was not affected. After culturing the cells for 3.5 h in the presence of cycloheximide, no more albumin could be detected in the Golgi complex with immunofluorescence microscopy. However, immunocytochemical assessment showed that the ASGP-R was still in the Golgi complex. These results suggest that the Golgi complex contains a pool of ASGP-R which is independent of neosynthesis for several hours.
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