Title: Sulfation of heparan sulfate associated with amyloid-beta plaques in patients with Alzheimer's disease
Authors: Bruinsma, Ilona B ×
Riet, Luuk Te
Gevers, Tom
ten Dam, Gerdy B
van Kuppevelt, Toin H
David, Guido
Kusters, Benno
de Waal, Robert M. W
Verbeek, Marcel M #
Issue Date: Feb-2010
Publisher: Springer Verlag
Series Title: Acta Neuropathologica vol:119 issue:2 pages:211-220
Abstract: Alzheimer's disease (AD) is characterized by pathological lesions such as amyloid-beta (A beta) plaques and cerebral amyloid angiopathy. Both these lesions consist mainly of aggregated A beta protein and this aggregation is affected by macromolecules such as heparan sulfate (HS) proteoglycans. Previous studies demonstrated that HS enhances fibrillogenesis of A beta and that this enhancement is dependent on the degree of sulfation of HS. In addition, it has been reported that these sulfation epitopes do not occur randomly but have a defined tissue distribution. Until now, the distribution of sulfation epitopes of HS has not yet been studied in human brain. We investigated whether a specific HS epitope is associated with A beta plaques by performing immunohistochemistry on occipital neocortical and hippocampal tissue sections from AD patients using five HS epitope-specific phage display antibodies. Antibodies recognizing highly N-sulfated HS demonstrated the highest level of staining in both fibrillar A beta plaques and non-fibrillar A beta plaques, whereas antibodies recognizing HS regions with a lower degree of N-sulfate modifications were only immunoreactive with fibrillar A beta plaques. Thus, our results suggest that a larger variety of HS epitopes is associated with fibrillar A beta plaques, but the HS epitopes associated with non-fibrillar A beta plaques seem to be more restricted, selectively consisting of highly N-sulfated epitopes.
ISSN: 0001-6322
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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