Jicha G A, Bowser R, Kazam I G, Davies P
Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Neurosci Res. 1997 Apr 15;48(2):128-32. doi: 10.1002/(sici)1097-4547(19970415)48:2<128::aid-jnr5>3.0.co;2-e.
Using a series of recombinant tau and FAC1 mutant proteins, this study demonstrates by Western and dot blot analysis that 1) shared epitopes between tau and FAC1 are responsible for Alz-50 binding; 2) Alz-50 reactivity is dependent on two discontinuous portions of the tau molecule; 3) Alz-50 reactivity is most likely the result of a conformational alteration of tau monomers in Alzheimer's disease; and 4) the epitope for MC-1, a novel monoclonal antibody, maps to similar regions of tau but does not react with FAC1. These data raise questions regarding previous studies which have suggested that tau lacks a specific conformation and illustrate the utility of the Alz-50 and MC-1 antibodies in recognizing a distinct pathological conformation of the tau molecule in Alzheimer's disease.
