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- W2015824963 abstract "Low concentrations of amyloid β proteins (Aβs, 1–10 nM) were recently demonstrated to reduce Cl−-ATPase activity in parallel with an increase in the intracellular Cl− concentration ([Cl−]i) and decreases in plasma membrane phosphorylated phosphatidylinositol (PIP and PIP2) levels in cultured rat hippocampal neurons (Yagyu et al., 2001). In this study, 17 β-estradiol (estradiol) at a therapeutic concentration (1.8 nM) for Alzheimer’s disease was found to block these Aβ (Aβ25–35)-induced changes. This protective effect of estradiol on Cl−-ATPase activity was antagonized by a pure estrogen receptor antagonist, ICI182780 and inhibitors for cyclic GMP-dependent protein kinase (PKG) (KT5823), Ca2+-calmodulin-dependent protein kinase II (CaMKII) (KN62) and phosphatidylinositol (PI) 4-kinase (wortmannin and quercetin). Estradiol recovered Aβ-induced decreases in plasma membrane phosphoinositide (PIP and PIP2) levels, this effect being inhibited by KT5823 and KN62. Glutamate toxicity was augmented in neurons with elevated [Cl−]i either by Aβ-treatment or carbachol+KCl+LiCl-treatment. The increased glutamate toxicity in the Aβ-treated neurons was attenuated by estradiol. Thus, a therapeutic concentration of estradiol protected Aβ-treated neurons against inhibition of Cl−-ATPase activity and an increase in [Cl−]i through its receptor, probably via PKG- and CaMKII−mediated recovery of PI4P formation. Elevated [Cl−]i may be related to enhancement of glutamate toxicity." @default.
- W2015824963 created "2016-06-24" @default.
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- W2015824963 date "2002-12-01" @default.
- W2015824963 modified "2023-10-11" @default.
- W2015824963 title "Protective effects of estradiol against amyloid β protein-induced inhibition of neuronal CI−-ATPase activity" @default.
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- W2015824963 doi "https://doi.org/10.1016/s0028-3908(02)00304-0" @default.
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