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American Journal of Pathology, Vol 143, 1586-1593, Copyright © 1993 by American Society for Investigative Pathology
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G Perry, PL Richey, SL Siedlak, MA Smith, P Mulvihill, DA DeWitt, J Barnett, BD Greenberg and RN Kalaria
Division of Neuropathology, Case Western Reserve University, Cleveland, Ohio 44106-4907.
Amyloid beta (A beta) immunoreactivity has been demonstrated in all extracellular neurofibrillary tangles (E-NFT) and most intraneuronal neurofibrillary tangles (I-NFT). We undertook this immunocytochemical study to understand the relationship between A beta immunoreactivity localized in NFT and beta-protein precursor (beta PP). We found epitopes of amino-, mid-, and carboxyl-terminal domains of beta PP in I- NFT and the majority of E-NFT. NFT retained beta PP after ionic detergent extraction, demonstrating that beta PP is an integral component of NFT. Finding beta PP in regions of A beta immunoreactivity raises the possibility that beta PP or its fragments associate with amyloid, and that the stability of A beta is responsible for its dominance in amyloid deposits.
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