Population studies of vitamin D binding protein microheterogeneity by mass spectrometry lead to characterization of its genotype-dependent O-glycosylation patterns

Chad Borges, Jason W. Jarvis, Paul E. Oran, Randall W. Nelson

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

Abstract

Mass spectrometric evidence presented here characterizes the genotype-dependent glycosylation patterns for each of the three major allele products of Vitamin D Binding Protein found in the general human population. Findings based on the analysis of over 100 individual plasma samples demonstrated that all DBP allele products, except GC*2, are modified (10-25 mol%) with a linear (NeuNAc) 1 (Gal) 1(GalNAc) 1 trisaccharide and, to a much lesser extent (1-5 mol%) with a trisaccharide-independent (Gal) 1(GalNAc) 1 dissaccharide. GC*2 protein contains the disaccharide but remains completely free of the trisaccharide, even in heterozygous individuals possessing a second gene product that is modified with the trisaccharide. Thus, all allelic forms of DBP except GC*2 possess two independent O-glycosylation sites occupied by separate, yet consistently isomass oligosaccharides and, despite a consensus sequence, lack N-glycosylation.

Original languageEnglish (US)
Pages (from-to)4143-4153
Number of pages11
JournalJournal of Proteome Research
Volume7
Issue number9
DOIs
StatePublished - Sep 1 2008

Keywords

  • GcG
  • Genotype
  • Mass spectrometric immunoassay
  • O-glycosylation
  • Population proteomics
  • Vitamin D binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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