Regulatory aspects of N-linked glycoproteins.
Activation of beta-adrenoreceptors in rat parotid acinar cells leads to copious exocrine protein secretion. Additionally, beta-adrenergic stimulation dramatically increases specific secretory protein synthesis and enhances N-linked glycosylation of secretory glycoproteins. Recently, efforts have been directed toward understanding the mechanisms underlying these biosynthetic events. We have been particularly interested in the receptor-mediated regulation of glycosylation. In this report, we evaluate available mechanistic information from the rat parotid gland and present initial data examining the ability of various regulatory agents to modulate N-linked glycosylation in enzymatically-dispersed cell aggregates from surgical specimens of human parotid glands. We conclude that glycosylation of human parotid N-linked glycoproteins may be regulated by extracellular signaling similar to that operative in the rat parotid gland.
D000818:Animals; D002478:Cells, Cultured; D006023:Glycoproteins / Q000096:biosynthesis*; D006031:Glycosylation; D006801:Humans; D007545:Isoproterenol / Q000494:pharmacology; D007930:Leucine / Q000378:metabolism; D008358:Mannose / Q000378:metabolism; D010306:Parotid Gland / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011943:Receptors, Adrenergic, beta / Q000187:drug effects / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000096:biosynthesis*
D006023:Glycoproteins; D011943:Receptors, Adrenergic, beta; D012471:Salivary Proteins and Peptides; D007930:Leucine; D007545:Isoproterenol; D008358:Mannose