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Regulation of tau phosphorylation in microtubule fractions by apolipoprotein E
Author(s) -
Flaherty Denise,
Lu Qun,
Soria Jennie,
Wood John G.
Publication year - 1999
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19990501)56:3<271::aid-jnr6>3.0.co;2-5
Subject(s) - hyperphosphorylation , apolipoprotein e , gene isoform , phosphorylation , microtubule , tau protein , cytoskeleton , alzheimer's disease , chemistry , microbiology and biotechnology , disease , neuroscience , biology , medicine , biochemistry , cell , gene
In Alzheimer's disease (AD), a family of proteins collectively named tau are displaced from their normal association with microtubules and are found in in a hyperphosphorylated state deposited into paired helical filaments (PHFs). PHFs are the hallmark cytoskeletal pathology of the disease, and the degree of PHF pathology correlates with the clinical severity of AD. Certain apolipoprotein E (apoE) isoforms have been identified as either risk or protective factors for AD, and one of the proposed mechanisms involves an interaction and potentially modulatory effects on tau hyperphosphorylation by the different apoE isoforms. In these studies, we directly tested the effects of apoE, E2 ,E3, and E4 on AD‐like phosphorylation of tau in brain microtubule fractions. We found that apoE attenuates tau hyperphosphorylation in the fractions, but the pattern was indistinguishable for the different isoforms. J. Neurosci. Res. 56:271–274, 1999. © 1999 Wiley‐Liss, Inc.