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Regulation of tau phosphorylation and protection against β‐amyloid‐induced neurodegeneration by lithium. Possible implications for Alzheimer's disease

Regulation of tau phosphorylation and protection against β‐amyloid‐induced neurodegeneration by... Alzheimer's disease is a neurodegenerative disorder characterized by the accumulation of the β‐amyloid peptide and the hyperphosphorylation of the tau protein, among other features. The most widely accepted hypothesis on the etiopathogenesis of this disease proposes that the aggregates of the β‐amyloid peptide are the main triggers of tau hyperphosphorylation and the subsequent degeneration of affected neurons. In support of this view, fibrillar aggregates of synthetic β‐amyloid peptide induce tau hyperphosphorylation and cell death in cultured neurons. We have previously reported that lithium inhibits tau hyperphosphorylation and also significantly protects cultured neurons from cell death triggered by β‐amyloid peptide. As lithium is a relatively specific inhibitor of glycogen synthase kinase‐3 (in comparison with other protein kinases), and other studies also point to a relevant role of this enzyme, we favor the view that glycogen synthase kinase‐3 is a crucial element in the pathogenesis of Alzheimer's disease. In our opinion, the possibility of using lithium, or other inhibitors of glycogen synthase kinase‐3, in experimental trials aimed to ameliorate neurodegeneration in Alzheimer's disease should be considered. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Bipolar Disorders Wiley

Regulation of tau phosphorylation and protection against β‐amyloid‐induced neurodegeneration by lithium. Possible implications for Alzheimer's disease

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References (145)

Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1398-5647
eISSN
1399-5618
DOI
10.1034/j.1399-5618.2002.01150.x
Publisher site
See Article on Publisher Site

Abstract

Alzheimer's disease is a neurodegenerative disorder characterized by the accumulation of the β‐amyloid peptide and the hyperphosphorylation of the tau protein, among other features. The most widely accepted hypothesis on the etiopathogenesis of this disease proposes that the aggregates of the β‐amyloid peptide are the main triggers of tau hyperphosphorylation and the subsequent degeneration of affected neurons. In support of this view, fibrillar aggregates of synthetic β‐amyloid peptide induce tau hyperphosphorylation and cell death in cultured neurons. We have previously reported that lithium inhibits tau hyperphosphorylation and also significantly protects cultured neurons from cell death triggered by β‐amyloid peptide. As lithium is a relatively specific inhibitor of glycogen synthase kinase‐3 (in comparison with other protein kinases), and other studies also point to a relevant role of this enzyme, we favor the view that glycogen synthase kinase‐3 is a crucial element in the pathogenesis of Alzheimer's disease. In our opinion, the possibility of using lithium, or other inhibitors of glycogen synthase kinase‐3, in experimental trials aimed to ameliorate neurodegeneration in Alzheimer's disease should be considered.

Journal

Bipolar Disorders – Wiley

Published: Jun 1, 2002

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