Weakly basic amines inhibit the proteolytic conversion of proalbumin to serum albumin in cultured rat hepatocytes.

Effects of weak amines on the proteolytic conversions of proalbumin to serum were studied in primary culture of rat hepatocytes. In control culture proalbumin was converted to serum albunin was inhibited and proalbunin per se was released into, medium. A similar inhibition of the processing was also observed in the presence of other amines such as methylamine and NH4Cl. Thus weak amines mimic the carboxylic ionophore monensin with regard to the effet on proalbunin conversion [Oda & Ikehara (1982) Biochem, Biophys. Res. Commun, 105, 766-772]. Since proteolytic conversion of proalbunin is believed to occur at the Golgi complex, these results suggest that weakly basic amines perturb the Golgi complex in addition to lysosomes and endosomes. [ABSTRACT FROM AUTHOR]