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beta-Adrenergic receptor regulation of N-linked protein glycosylation in rat parotid acinar cells.

Authors
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Volume
80
Issue
23
Pages
7146–7150
Identifiers
PMID: 6316348
Source
Medline

Abstract

We have investigated the relationship between beta-adrenergic receptor stimulation and protein glycosylation and secretion in rat parotid gland cells in vitro. The potent beta-adrenergic agonist (-)-isoproterenol increases [3H]mannose incorporation into newly synthesized glycoproteins. This effect is enhanced if cells are first preincubated with dolichyl phosphate and is not observed after muscarinic-cholinergic or alpha-adrenergic stimulation of cells. The increase in [3H]mannose incorporation is abolished by incubation of cells with tunicamycin, suggesting that the glycosylation events being studied involved asparagine-linked oligosaccharides. The extent of increase in glycosylation is dependent on the concentration of (-)-isoproterenol to which cells are exposed. (+/-)-Propanolol totally abolishes the (-)-isoproterenol-induced increase in [3H]mannose incorporation, in a manner similar to its effects on exocrine secretion. Our findings suggest that beta-adrenergic receptor activation has a profound influence on N-linked protein glycosylation in rat parotid cells in addition to eliciting exocrine protein release.

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