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Isolated rat hepatocytes degraded 125I-insulin with a Km of 150 nmol/l. Degradation was stimulated by the addition of glutathione and dithiothreitol. In cells incubated with diamide, glutathione was oxidised to the disulphide. Regeneration of reduced glutathione commenced after a further 30 min incubation at 37 degrees C. Diamide (1 mmol/l) significantly inhibited insulin degradation by hepatocytes (p less than 0.001). The 'apparent Vmax' for insulin degradation was decreased tenfold and the Km decreased to 25 nmol/l. The diamide-insensitive degrading activity was cell-associated and produced an intermediate of hormone degradation that was apparently of a higher molecular weight than insulin A chain. The biological activity of the intermediate was 0.03% of that of insulin. The diamide-insensitive activity was not due to release of protease into the medium by cell lysis. We conclude that there are at least two pathways capable of degrading insulin existing in rat hepatocytes.

125I-labelled insulin degradation by isolated rat hepatocytes: The roles of glutathione-insulin transhydrogenase and insulin-specific protease