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Alz‐50 and MC‐1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
Author(s) -
Jicha Gregory A.,
Bowser Robert,
Kazam Imrana G.,
Davies Peter
Publication year - 1997
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19970415)48:2<128::aid-jnr5>3.0.co;2-e
Subject(s) - epitope , monoclonal antibody , recombinant dna , western blot , conformational epitope , antibody , chemistry , epitope mapping , mutant , tau protein , microbiology and biotechnology , linear epitope , alzheimer's disease , biology , biochemistry , medicine , immunology , disease , pathology , gene
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. J. Neurosci. Res. 48:128–132, 1997. © 1997 Wiley‐Liss, Inc.