Research article summary (published 5 Jan 2009):

Amyloid beta induces cellular relocalization and production of agrin and glypican-1.

Full Abstract

The major component of senile plaques and vascular amyloid in Alzheimer's disease (AD) brains is the amyloid beta protein (Abeta). Besides Abeta, several other proteins have been identified in these lesions, in particular heparan sulfate proteoglycans (HSPG). However, it is still unclear, what causes the excessive accumulation of HSPG in AD brains. Therefore, we investigated if Abeta may influence production and expression of two major Abeta-associated HSPG species, agrin and glypican-1. When human brain pericytes (HBP) were cultured in the presence of Abeta, protein and mRNA expression of both agrin and glypican-1 were increased and more radioactive sulfate was incorporated in the glycosaminoglycan fraction of Abeta-treated HBP. Furthermore, after Abeta treatment, these HSPG were found in association with the amyloid fibrils attached to the cell membrane, in contrast to the intracellular agrin and glypican-1 staining observed in untreated cells. We conclude that Abeta can modulate the cellular expression of agrin and glypican-1, which may contribute to the accumulation of these HSPG in AD lesions.

Author information

Author/s: Timmer, Nienke M (NM); van Horssen, Jack (J); Otte-Holler, Irene (I); Wilhelmus, Micha M M (MM); David, Guido (G); van Beers, Joyce (J); de Waal, Rob M W (RM); Verbeek, Marcel M (MM);

Affiliation: Department of Neurology, Laboratory of Pediatrics and Neurology, Donders Centre for Brain, Cognition and Behaviour, Alzheimer Centre Nijmegen, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands. n.timmer(-atsign-)cukz.umcn.nl

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Brain research (Brain Res), published in Netherlands. (Language: eng)

Reference: 2009-Mar; vol 1260 (issue ) : pp 38-46

Dates: Created 2009/03/02; Completed 2009/03/26;

PMID: 19166823, status: MEDLINE (last retrieval date: 3/26/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Agrin - metabolism Amyloid beta-Protein - metabolism Blotting, Western Brain - cytology; metabolism Cell Membrane - metabolism Cells, Cultured Fluorescent Antibody Technique

Glypicans - metabolism Heparan Sulfate Proteoglycans - metabolism Humans Microscopy, Electron Pericytes - metabolism; ultrastructure RNA, Messenger - metabolism Sulfur Radioisotopes

Associated Chemicals: Agrin (0) ; Amyloid beta-Protein (0) ; Glypicans (0) ; Heparan Sulfate Proteoglycans (0) ; RNA, Messenger (0) ; Sulfur Radioisotopes (0)

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