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Direct interaction of soluble human recombinant tau protein with Aβ 1–42 results in tau aggregation and hyperphosphorylation by tau protein kinase II
Author(s) -
Rank Kenneth B,
Pauley Adele M,
Bhattacharya Keshab,
Wang Zhigang,
Evans David B,
Fleck Timothy J,
Johnston Jennifer A,
Sharma Satish K
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02376-1
Subject(s) - hyperphosphorylation , tau protein , chemistry , phosphorylation , in vitro , kinase , protein kinase a , amyloid (mycology) , alzheimer's disease , microbiology and biotechnology , biochemistry , biophysics , biology , medicine , disease , inorganic chemistry
We report here that aggregated β‐amyloid (Aβ) 1–42 promotes tau aggregation in vitro in a dose‐dependent manner. When Aβ‐mediated aggregated tau was used as a substrate for tau protein kinase II (TPK II), an 8‐fold increase in the rate of TPK II‐mediated tau phosphorylation was observed. The extent of TPK II‐dependent tau phosphorylation increased as a function of time and Aβ 1–42 concentration, and hyperphosphorylated tau was found to be decorated with an Alzheimer's disease‐related phosphoepitope (P‐Thr‐231). In HEK 293 cells co‐expressing CT‐100 amyloid precursor protein and tau, the release of Aβ 1–42 from these cells was impaired. Taken together, these in vitro results suggest that Aβ 1–42 promotes both tau aggregation and hyperphosphorylation.