Abstract
The effect of the alpha-glucosidase inhibitor N-hydroxyethyl-1-deoxynojirimycin (Bay m 1099) on the glycosylation and secretion of α 1-antitrypsin (three complex type oligosaccharide chains) and of α 1-acid glycoprotein (six complex type oligosaccharide chains) was studied in rat hepatocyte primary cultures. In the presence of 4 mM Bay in 1099 the processing of high-mannose to complex type oligosaccharides was partially inhibited leading to the secretion of α 1-antitrypsin and α 1-acid glycoprotein carrying a mixture of both high-mannose and complex type oligosaccharides. The major part of α 1-antitrypsin secreted by Bay in 1099 treated cells still carried two complex type oligosaccharide chains, the majority of α 1-acid glycoprotein carried three to five. Despite its effects on protein glycosylation Bay m 1099 did not lead to pronounced changes in the synthesis or secretion of α 1-antitrypsin, α 1-acid glycoprotein or albumin. At concentrations of Bay m 1099 lower than 0.5 mM no inhibitory effect on oligosaccharide trimming could be observed. After removal of Bay in 1099 from hepatocytes its inhibitory effect on protein glycosylation was immediately reversible.
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