Modulation of oligosaccharide processing in an exocrine secretory glycoprotein of rat parotid cells by beta-adrenoreceptor activation.

Such stimulation of rat parotid acinar cells in vitro modulated the rate of processing of N-linked oligosaccharides in a high-molecular weight (220 kdalton) secretory glycoprotein. Conversion of polymannose-type oligosaccharides to complex-type oligosaccharides was evaluated by sensitivity to endoglucosaminidase H and alpha-mannosidase, and with a specific inhibitor of glucosidases I/II. Oligosaccharide maturation in the 220 kdalton glycoprotein required one-third to half less time in cells exposed to the beta-adrenergic agonist isoproterenol than in controls.