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Proceedings of the Eighty‐First Meeting of The British Neuropathological Society held at the Institute of Psychiatry 10–11 January 1991

Microtubule-associated protein tau is a major constituent of paired helical filaments (PHF) in Alzheimer’s disease (AD). Modified forms of tau with reduced mobility on SDS-PAGE have been described in preparations from AD brain. We have separated normal tau, which is soluble in a non-denaturing buffer, from abnormal tau, which requires SDS for solubilization, in AD and Down’s syndrome (DS) brains. Western blotting with a polyclonal anti-bovine tau serum revealed the presence of abnormal tau in 9/14 AD, 6/7 adult DS and 0/9 age-matched control brains. We found a semi-quantitative correlation between the quantity of abnormal tau and the presence of Alzheimer-type neuropathology. Additionally, the monoclonal antibody, Tau. 1, labelled abnormal tau on Western blots only after treatment with alkaline phosphatase. These results suggest that abnormal tau in AD and DS is aberrantly phosphorylated and that this modification may precede the formation of SDS-insoluble neurofibrillary tangles in AD and DS.