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The cellular pathology of Alzheimer's disease includes an accumulation of microglia surrounding the amyloid plaques. We report that human amyloid beta-protein is chemotactic for murine resident peritoneal macrophages and rat microglia, which may account for the increased density of microglia in plaques. A maximal chemotactic response was observed at 1-10nM, with a 2.5 fold increase in activity over controls for both classes of mononuclear phagocytes. The neurotoxic peptide fragment (25-35) of amyloid beta-protein is similarly chemotactic, while a control scrambled version and the precursor protein are not chemotactic. These results indicate that beta-protein may influence plaque formation via the recruitment of phagocytes, with consequent implications for the future development of treatments for Alzheimer's disease.

Original publication




Journal article


Biochem Biophys Res Commun

Publication Date





1096 - 1100


Amino Acid Sequence, Amyloid beta-Peptides, Animals, Chemotaxis, Humans, Macrophages, Mice, Molecular Sequence Data, Peptide Fragments, Poly I, Structure-Activity Relationship