Influence of β-adrenergic stimulation on glycosylation of a major, secretory N-linked glycoprotein from rat parotid salivary gland

B. J. Baum, C. K. Yeh, E. E. Kousvelari

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

β-Adrenergic stimulation with 10 μM isoproterenol increased the [3H]-mannose/[14C]-leucine ratio (three- to six-fold) of protein extracts in double-radiolabelled rat parotid acinar cells. Characteristics of oligosaccharides in a major parotid glycoprotein (Mr ~ 220,000; gp 220) were studied. Gp 220 from control and experimental cells was endoglycosidase H-insensitive, endoglycosidase F-sensitive and bound both concanavalin A and wheat germ agglutinin. Gp 220 was removed from concanavalin A-Sepharose by sequential elution with 10mM α-methyl glucoside and 0.5 M α-methyl mannoside. These findings suggest that (1) oligosaccharides in gp 220 have both a biantennary complex and hybrid oligosaccharide chains, and (2) β-adrenoreceptor stimulation has little effect on the gross oligosaccharide structures of this glycoprotein.

Original languageEnglish (US)
Pages (from-to)201-207
Number of pages7
JournalArchives of Oral Biology
Volume35
Issue number3
DOIs
StatePublished - 1990
Externally publishedYes

Keywords

  • oligosaccharides
  • parotid
  • salivary glycoprotein
  • secretion
  • β-adrenoreceptor

ASJC Scopus subject areas

  • Otorhinolaryngology
  • Dentistry(all)
  • Cell Biology

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