Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
NeuronPublished 1 January 1992
Michel Goedert, Maria Grazia Spillantini, Nigel J. Cairns, R. Anthony Crowther
Citations1,133
SJR quartileQ1
SJR score6.75
SNIP2.95
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TL;DR
By using antibodies specific for some of the inserts that distinguish the various isoforms and label PHFs, a correspondence betweenPHFs, abnormal bands, and isoforms is established and is a necessary step in unravelling the molecular pathogenesis of PHFs.
Abstract
Preparations of dispersed paired helical filaments (PHFs) from the brains of Alzheimer's disease and Down's syndrome patients display on gels three principal bands corresponding to abnormally modified forms of the microtubule-associated protein tau. Interpretation of the pattern is difficult because there are six tau isoforms in normal brain and phosphorylation changes their mobility. By enzymatic dephosphorylation at high temperature, we have shifted the three abnormal bands obtained from dispersed PHFs to align with the six nonphosphorylated tau isoforms. By using antibodies specific for some of the inserts that distinguish the various isoforms and label PHFs, we have established a correspondence between PHFs, abnormal bands, and isoforms. This identification of isoforms is a necessary step in unravelling the molecular pathogenesis of PHFs.
Keywords
MedicineNeuroscienceBiochemistry, Genetics and Molecular Biology
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