Structural and quantitative comparison of cerebrospinal fluid glycoproteins in Alzheimer's disease patients and healthy individuals
(2008) In Neurochemical Research 33(7). p.1332-1340- 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... (More)
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 alpha1-antitrypsin showed decreased glycosylation in AD patients while another glycosylated isoform of an unassigned protein was up-regulated. Protein expression levels of alpha1-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.
(Less)
- author
- Sihlbom, Carina ; Davidsson, Pia ; Sjögren, Magnus ; Wahlund, Lars -Olof and Nilsson, Carol L LU
- publishing date
- 2008-07
- type
- Contribution to journal
- publication status
- published
- keywords
- Adult, Aged, Aged, 80 and over, Albumins, Alzheimer Disease, Chromatography, Affinity, Electrophoresis, Gel, Two-Dimensional, Female, Glycoproteins, Humans, Hydrogen-Ion Concentration, Image Processing, Computer-Assisted, Male, Mass Spectrometry, Middle Aged, Spectroscopy, Fourier Transform Infrared, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- in
- Neurochemical Research
- volume
- 33
- issue
- 7
- pages
- 9 pages
- publisher
- Springer
- external identifiers
-
- scopus:44549087658
- pmid:18288611
- ISSN
- 0364-3190
- DOI
- 10.1007/s11064-008-9588-x
- language
- English
- LU publication?
- no
- id
- dcce551d-cea0-4648-afac-42ce33049d95
- date added to LUP
- 2017-05-16 10:31:33
- date last changed
- 2024-01-13 21:00:52
@article{dcce551d-cea0-4648-afac-42ce33049d95,
abstract = {{<p>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 alpha1-antitrypsin showed decreased glycosylation in AD patients while another glycosylated isoform of an unassigned protein was up-regulated. Protein expression levels of alpha1-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.</p>}},
author = {{Sihlbom, Carina and Davidsson, Pia and Sjögren, Magnus and Wahlund, Lars -Olof and Nilsson, Carol L}},
issn = {{0364-3190}},
keywords = {{Adult; Aged; Aged, 80 and over; Albumins; Alzheimer Disease; Chromatography, Affinity; Electrophoresis, Gel, Two-Dimensional; Female; Glycoproteins; Humans; Hydrogen-Ion Concentration; Image Processing, Computer-Assisted; Male; Mass Spectrometry; Middle Aged; Spectroscopy, Fourier Transform Infrared; Comparative Study; Journal Article; Research Support, Non-U.S. Gov't}},
language = {{eng}},
number = {{7}},
pages = {{1332--1340}},
publisher = {{Springer}},
series = {{Neurochemical Research}},
title = {{Structural and quantitative comparison of cerebrospinal fluid glycoproteins in Alzheimer's disease patients and healthy individuals}},
url = {{http://dx.doi.org/10.1007/s11064-008-9588-x}},
doi = {{10.1007/s11064-008-9588-x}},
volume = {{33}},
year = {{2008}},
}