Open AccessDifferential secretion of α1‐acid glycoprotein occurs in the Golgi complex of isolated rat hepatocytes
Author(s) -
POÜS Christian,
GUIBOURDENCHE Jean,
DRECHOU Anne,
DURAND Geneviève
Publication year - 1994
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1994.tb18590.x
Subject(s) - golgi apparatus , glycoprotein , concanavalin a , secretion , biochemistry , biology , microbiology and biotechnology , chemistry , endoplasmic reticulum , in vitro
Using weakly basic amines, we investigated the step at which the secretion kinetics of concanavalin‐A‐retained and nonretained α1‐acid glycoprotein glycoforms diverge in isolated rat hepatocytes. Both chloroquine and primaquine, whose action on protein secretion is targeted to terminal domains of the Golgi apparatus, cancelled the kinetic difference without influencing carbohydrate chain sialylation. To test for a possible interaction of α1‐acid glycoprotein with Golgi membranes, we also permeabilized control and primaquine‐treated hepatocytes, as well as purified Golgi preparations, with saponin. In each case, we found that α1‐acid glycoprotein was associated with Golgi membranes, the association being more marked in primaquine‐treated cells than in control cells. Membrane‐bound α1‐acid glycoprotein appeared to be preferentially retained on concanavalin A. Such retention could account for the divergent secretion kinetics of α1‐acid glycoprotein glycoforms.