Structural and quantitative comparison of cerebrospinal fluid glycoproteins in Alzheimer's disease patients and healthy individuals

Carina Sihlbom, Pia Davidsson, Magnus Sjögren, Lars Olof Wahlund, Carol L. Nilsson

Research output: Contribution to journalArticle

68 Scopus citations

Abstract

Glycoproteins in cerebrospinal fluid (CSF) are altered in Alzheimer's Disease (AD) patients compared to control individuals. We have utilized albumin depletion prior to 2D gel electrophoresis to enhance glycoprotein concentration for image analysis as well as structural glycoprotein determination without glycan release using mass spectrometry (MS). The benefits of a direct glycoprotein analysis approach include minimal sample manipulation and retention of structural details. A quantitative comparison of gel-separated glycoprotein isoforms from twelve AD patients and twelve control subjects was performed with glycoprotein-specific and total protein stains. We have also compared glycoforms in pooled CSF obtained from AD patients and control subjects with mass spectrometry. One isoform of α1-antitrypsin showed decreased glycosylation in AD patients while another glycosylated isoform of an unassigned protein was up-regulated. Protein expression levels of α1- antitrypsin were decreased, while the protein levels of apolipoprotein E and clusterin were increased in AD. No specific glycoform could be specifically assigned to AD.

Original languageEnglish (US)
Pages (from-to)1332-1340
Number of pages9
JournalNeurochemical Research
Volume33
Issue number7
DOIs
StatePublished - Jul 1 2008

Keywords

  • Alzheimer's Disease
  • Apolipoprotein E
  • CSF
  • Cerebrospinal fluid
  • Clusterin
  • Glycoform
  • Glycoprotein
  • Glycoproteomics
  • Glycosylation
  • Haptoglobin
  • Isoform
  • N-linked
  • Proteomics
  • α- antitrypsin
  • α-1-β-glycoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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