title: The amyloid beta-protein of Alzheimer's disease is chemotactic for mononuclear phagocytes.
abstract: 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.
authors: Salk Institute for Biological Studies, San Diego, CA 92186-5800.
authors: J B
authors: JB
authors: Davis
authors: H F
authors: HF
authors: McMurray
authors: D
authors: D
authors: Schubert
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000494:pharmacology*; D000818:Animals; D002633:Chemotaxis / Q000187:drug effects / Q000502:physiology*; D006801:Humans; D008264:Macrophages / Q000187:drug effects / Q000502:physiology*; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology; D011069:Poly I / Q000494:pharmacology; D013329:Structure-Activity Relationship
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D011069:Poly I