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. 1983 Dec;80(23):7146–7150. doi: 10.1073/pnas.80.23.7146

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

E E Kousvelari, S R Grant, B J Baum
PMCID: PMC390010  PMID: 6316348

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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