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Lithium inhibits Alzheimer's disease‐like tau protein phosphorylation in neurons
Author(s) -
Muñoz-Montaño Juan Ramón,
Moreno Francisco J.,
Avila Jesús,
Dı́az-Nido Javier
Publication year - 1997
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(97)00688-1
Subject(s) - gsk 3 , dephosphorylation , hyperphosphorylation , glycogen synthase , tau protein , gsk3b , phosphatase , phosphorylation , alzheimer's disease , kinase , lithium (medication) , protein kinase a , chemistry , biochemistry , microbiology and biotechnology , biology , neuroscience , medicine , endocrinology , disease
In Alzheimer's disease, tau protein becomes hyperphosporylated, which can contribute to neuronal degeneration. However, the implicated protein kinases are still unknown. Now we report that lithium (an inhibitor of glycogen synthase kinase‐3) causes tau dephosphorylation at the sites recognized by antibodies Tau‐1 and PHF‐1 both in cultured neurons and in vivo in rat brain. This is consistent with a major role for glycogen synthase kinase‐3 in modifying proline‐directed sites on tau protein within living neurons under physiological conditions. Lithium also blocks the Alzheimer's disease‐like proline‐directed hyperphosphorylation of tau protein which is observed in neurons treated with a phosphatase inhibitor. These data raise the possibility of using lithium to prevent tau hyperphosphorylation in Alzheimer's disease.