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

Artikel i vetenskaplig tidskrift
Författare Zarah Pernber
Kaj Blennow
Nenad Bogdanovic
Jan-Eric Månsson
Maria K. Blomqvist
Publicerad i Dementia and Geriatric Cognitive Disorders
Volym 33
Nummer/häfte 2-3
Sidor 174-188
ISSN 1420-8008
Publiceringsår 2012
Publicerad vid Institutionen för neurovetenskap och fysiologi, sektionen för psykiatri och neurokemi
Sidor 174-188
Språk en
Länkar dx.doi.org/10.1159/000338181
Ämnesord 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
Ämneskategorier Neurologi, Psykiatri

Sammanfattning

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

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