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American Journal of Pathology, Vol 137, 711-723, Copyright © 1990 by American Society for Investigative Pathology

REGULAR ARTICLES

Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study

W Bondareff, CM Wischik, M Novak, WB Amos, A Klug and M Roth
Department of Psychiatry and Biological Sciences, University of Southern California, Los Angeles 90033.

Antibodies directed against three regions of tau, ubiquitin, and B- amyloid were used in a histologic study of neurofibrillary degeneration in Alzheimer's disease to distinguish two populations of neurofibrillary tangles. Intracellular tangles were immunolabeled exclusively by two antibodies raised against antigens in the fuzzy coat of the paired helical filament (PHF). Extracellular tangles were distinguished by selective immunolabeling with a monoclonal antibody raised against antigens in the PHF core. This was associated with removal of the fuzzy coat and exposure of PHF-core epitopes. In the transition from intracellular to extracellular compartments in vivo, tangles appeared to undergo changes similar to protease digestion in vitro. The transition was associated with the appearance of amyloid immunoreactivity. These findings suggest that tangle degradation occurs in a series of distinct stages, including ubiquitination of some unknown molecule, a change in tau immunoreactivity, and partial proteolysis of tangle-bound tau in extracellular tangles.


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D. B. Evans, K. B. Rank, K. Bhattacharya, D. R. Thomsen, M. E. Gurney, and S. K. Sharma
Tau Phosphorylation at Serine 396 and Serine 404 by Human Recombinant Tau Protein Kinase II Inhibits Tau's Ability to Promote Microtubule Assembly
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Copyright © 1990 by the American Society for Investigative Pathology.