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. 2003 Jan 15;42(2):173–181. doi: 10.1016/0047-6374(88)90072-3

N-linked protein glycosylation in the rat parotid gland during aging

Eleni E Kousvelari 1,∗, Dipak K Banerjee 1,∗∗, Lalita Murty 1, Bruce J Baum 1
PMCID: PMC7130591  PMID: 2834612

Abstract

N-Linked protein glycosylation was examined in vitro in dispersed rat parotid acinar cells from young adult (3–6 months) and aged (22–24 months) rats. A small decrease in general protein production was observed with cells from aged animals (∼20% lower incorporation of [14C]leucine into 10% CCI3 COOH insoluble protein during continuous pulse labeling). Incorporation of [3H]mannose into N-linked glycoproteins by aged cells was further reduced (∼35%). Similarly microsomal membranes from parotid glands of aged animals showed ∼50% reduction in the synthesis of mannosylphosphoryl dolichol, a key intermediate in the dolichol pathway of protein N-glycosylation. Man-P-Dol synthase, the microsomal enzyme responsible for production of this saccharide-lipid, displayed no change in apparent Km for GDP-mannose when preparations from aged animals were utilized, but did show ∼50% reduction in Vmax. Following β-adrenoreceptor activation, cells from both young adult and aged glands showed increased N-linked protein glycosylation almost to the same extent (∼2-fold). The data suggested that in aged rat parotid cells there is a basal reduction of activity in the pathway responsible for asparagine-linked protein glycosylation, but that following exocytotic stimuli this pathway responds in a manner comparable to cells from young adult glands.

Keywords: Asparagine-linked oligosaccharides, Man-P-Dol synthase, Dolichol pathway, Salivary gland, β-Adrenoreceptor

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