The β‐amyloid protein of Alzheimer’s disease binds to membrane lipids but does not bind to the α7 nicotinic acetylcholine receptor

• DOI: 10.1111/j.1471-4159.2006.04444.x
• Publication Date: 2007-02-05T12:43:30Z
• Authors: David H. Small; Danuta Maksel; Megan L. Kerr; Judy Ng; Xu Hou; Cindy Chu; Hossein Mehrani; Sharon Unabia; Michael F. Azari; Richard Loiacono; Marie‐Isabel Aguilar; Mary Chebib
• Keywords: 0301 basic medicine; Amyloid beta-Peptides; Membrane Fluidity; Aconitine; Cell Membrane; Fluorescence Polarization; Receptors, Nicotinic; Surface Plasmon Resonance; Bungarotoxins; Transfection; Hippocampus; Rats; Rats, Sprague-Dawley; Membrane Lipids; Neuroblastoma; Xenopus laevis; 03 medical and health sciences; Cell Line, Tumor; Oocytes; Animals; Humans; Female

Abstract Accumulation of the amyloid protein (Aβ) in brain is an important step pathogenesis Alzheimer’s disease. However, mechanism by which Aβ exerts its neurotoxic effect largely unknown. It has been suggested that peptide can bind to α7 nicotinic acetylcholine receptor (α7nAChR). In this study, we examined binding Aβ1‐42 endogenous and recombinantly expressed α7nAChRs. did neither inhibit specific α7nAChR ligands rat homogenate or slice preparations, nor it influence activity α7nAChRs Xenopus oocytes. Similarly, not compete for α‐bungarotoxin‐binding sites on SH‐SY5Y cells stably expressing The tau phosphorylation was also examined. Although altered α7nAChR‐transfected cells, unrelated expression activity. Binding studies using surface plasmon resonance indicated majority bound membrane lipid, rather than a component. Fluorescence anisotropy experiments may disrupt lipid structure fluidity. We conclude effects are unlikely be mediated direct α7nAChR. Instead, speculate exert altering packing lipids within plasma membrane, could, turn, function variety receptors channels cell surface.