Open AccessWeakly basic amines inhibit the proteolytic conversion of proalbumin to serum albumin in cultured rat hepatocytes
Author(s) -
ODA Kimimitsu,
IKEHARA Yukio
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09238.x
Subject(s) - monensin , albumin , chemistry , bovine serum albumin , endosome , serum albumin , biochemistry , golgi apparatus , cell , intracellular
Effects of weak amines on the proteolytic conversion of proalbumin to serum albumin were studied in primary culture of rat hepatocytes. In control culture proalbumin was converted to serum albumin before discharge into the medium. However, in the presence of chloroquine the conversion to serum albumin was inhibited and proalbumin 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 NH 4 Cl. Thus weak amines mimic the carboxylic ionophore monensin with regard to the effect on proalbumin conversion [Oda & Ikehara (1982) Biochem. Biophys. Res. Commun. 105 , 766–772]. Since proteolytic conversion of proalbumin 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.