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

Authors
  • Kousvelari, E E
  • Grant, S R
  • Baum, B J
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Dec 01, 1983
Volume
80
Issue
23
Pages
7146–7150
Identifiers
PMID: 6316348
Source
Medline
License
Unknown

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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