To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

Altered Distribution of t… - University of Gothenburg, Sweden Till startsida
To content Read more about how we use cookies on

Altered Distribution of the Gangliosides GM1 and GM2 in Alzheimer's Disease

Journal article
Authors Zarah Pernber
Kaj Blennow
Nenad Bogdanovic
Jan-Eric Månsson
Maria K. Blomqvist
Published in Dementia and Geriatric Cognitive Disorders
Volume 33
Issue 2-3
Pages 174-188
ISSN 1420-8008
Publication year 2012
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 174-188
Language en
Keywords Glycosphingolipids, Alzheimer's disease, Frontotemporal dementia, Immunohistochemistry, Temporal, amyloid precursor protein, frontotemporal lobar degeneration, lipid, rafts, beta-protein, monoclonal-antibody, endogenous seed, gamma-secretase, membrane microdomains, binding epitope, senile plaques, khann g, 1984, neurology, v34, p939
Subject categories Neurology, Psychiatry


Background: Alzheimer's disease (AD) is a neurodegenerative disorder where beta-amyloid tends to aggregate and form plaques. Lipid raft-associated ganglioside GM1 has been suggested to facilitate beta-amyloid aggregation; furthermore, GM1 and GM2 are increased in lipid rafts isolated from cerebral cortex of AD cases. Aim/Method: The distribution of GM1 and GM2 was studied by immunohistochemistry in the frontal and temporal cortex of AD cases. Frontotemporal dementia (FTD) was included as a contrast group. Results: The distribution of GM1 and GM2 changes during the process of AD (n = 5) and FTD (n = 3) compared to controls (n = 5). Altered location of the GM1-positive small circular structures seems to be associated with myelin degradation. In the grey matter, the staining of GM1-positive plasma membranes might reflect neuronal loss in the AD/FTD tissue. The GM1-positive compact bundles were only visible in cells located in the AD frontal grey matter, possibly reflecting raft formation of GM1 and thus a pathological connection. Furthermore, our results suggest GM2 to be enriched within vesicles of pyramidal neurons of the AD/FTD brain. Conclusion: Our study supports the biochemical finding of ganglioside accumulation in cellular membranes of AD patients and shows a redistribution of these molecules. Copyright (C) 2012 S. Karger AG, Basel

Page Manager: Webmaster|Last update: 9/11/2012

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?