Tau Proteins and Neurofibrillary Degeneration

  title={Tau Proteins and Neurofibrillary Degeneration},
  author={Michel Goedert and Maria Grazia Spillantini and R. Anthony Crowther},
  journal={Brain Pathology},
The paired helical filament is the major fibrous component of neurofibrillary pathology in Alzheimer's disease. Over the last three years evidence has accumulated that the microtubule‐associated protein tau forms an important, if not the sole, constituent of the paired helical filament. Tau protein in normal brain is bound to axonal microtubules by a tandem repeat region. In Alzheimer's disease a proportion of tau protein becomes abnormally phos‐phorylated and is no longer associated with… 
Filamentous Tau Pathology in Nerve Cells, Astrocytes, and Oligodendrocytes of Aged Baboons
The potential usefulness of aged baboons for experimental investigation of neuronal and glial filamentous tau pathology may provide valuable information pertinent to the broad spectrum of human tauopathies is indicated.
Evolution of the neuropathology of Alzheimer's disease
The most conspicuous changes seen in the brain are deposits of insoluble proteins in both extracellular and intraneuronal locations, which correlates with the gradual worsening of clinical symptoms in Alzheimer's disease.
NPT088 reduces both amyloid-β and tau pathologies in transgenic mice


Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)
Light and electron microscopic immunolabeling of neurofibrillary tangles by a monoclonal antibody to the microtubule-associated protein tau suggests that abnormal synthesis, modification, or aggregation of tau may induce aberrant cytoskeletal--cell organelle interactions, subsequent interference with axonal flow, and resultant tangle formation.
Structural aspects of pathology in Alzheimer's disease.
Alzheimer's disease: insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea.
Covalently cross-linked protein polymers occur in lens senile cataracts and in terminally differentiated skin keratinocytes, suggesting that there may be a common mechanism for remodeling some structural proteins during cell aging.
Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders
These antibodies were found to immunostain tangles in normal aged brain and in brains affected by a range of neurodegenerative disorders, including Down's syndrome, Alzheimer's disease plus Parkinson's disease, progressive supranuclear palsy, and the parkinsonism‐dementia complex of Guam, as well as Pick bodies in Pick's disease.
Straight and paired helical filaments in Alzheimer disease have a common structural unit.
  • R. Crowther
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1991
It is reported herein thatPHFs and SFs form hybrid filaments displaying both morphologies, that PHFs andSFs share surface epitopes, and that computed maps reveal a similar C-shaped morphological unit in PHFsand SFs, though differing in relative arrangement in the two types of filament.