Albumin-blunted deleterious effect of amyloid-beta by preventing the internalization of the peptide into neurons.

J Alzheimers Dis

Department of Biochemistry and Molecular Biology, Instituto de Neurociencias de Castilla y León (INCYL), University of Salamanca, Spain.

Published: September 2010

Amyloid-beta (A beta) is the main component of senile plaques, one of the hallmarks of Alzheimer's disease. Our results showed that A beta(25-35) decreased neuronal viability while it increased generation of reactive oxygen species (ROS). Under these circumstances, albumin (BSA) prevented ROS production and neuronal death in a dose- and time-dependent manner. In addition, BSA partially prevented the decrease in the expression of GAP-43, MAP-2, and tubulin, and the phosphorylation of tau protein caused by A beta, suggesting that BSA protects against the loss of plasticity caused by the peptide. Our findings suggest that BSA exerts its protective effect by binding to A beta in an equimolecular way, which prevents heterodimer (A beta-BSA) entry into neurons. In fact, BSA prevented A beta internalization, as shown by confocal immunocytochemistry, suggesting that BSA causes its protective effect by sequestrating A beta, which cannot reach its intracellular targets. This is consistent with the idea that A beta must enter neurons to exert its deleterious effects.

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Source
http://dx.doi.org/10.3233/JAD-2009-1093DOI Listing

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