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- W2007008575 abstract "Abstract Although the accumulation of the neurotoxic peptide β‐amyloid (Aβ) in the central nervous system is a hallmark of Alzheimer's disease, whether Aβ acts in astrocytes is unclear, and downstream functional consequences have yet to be defined. Here, we show that cytosolic Ca 2+ dysregulation, induced by a neurotoxic fragment (Aβ25–35), caused apoptosis in a concentration‐dependent manner, leading to cytoplasmic Ca 2+ mobilization from extra‐ and intracellular sources, mainly from the endoplasmic reticulum ( ER ) via IP 3 receptor activation. This mechanism was related to Aβ‐mediated apoptosis by the intrinsic pathway because the expression of pro‐apoptotic Bax was accompanied by its translocation in cells transfected with GFP ‐Bax. Aβ‐mediated apoptosis was reduced by BAPTA ‐ AM , a fast Ca 2+ chelator, indicating that an increase in intracellular Ca 2+ was involved in cell death. Interestingly, the Bax translocation was dependent on Ca 2+ mobilization from IP 3 receptors because pre‐incubation with xestospongin C, a selective IP 3 receptor inhibitor, abolished this response. Taken together, these results provide evidence that Aβ dysregulation of Ca 2+ homeostasis induces ER depletion of Ca 2+ stores and leads to apoptosis; this mechanism plays a significant role in Aβ apoptotic cell death and might be a new target for neurodegeneration treatments." @default.
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- W2007008575 date "2014-05-15" @default.
- W2007008575 modified "2023-10-04" @default.
- W2007008575 title "Apoptosis induced by Aβ25-35 peptide is Ca<sup>2+</sup>-IP<sub>3</sub>signaling-dependent in murine astrocytes" @default.
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- W2007008575 doi "https://doi.org/10.1111/ejn.12599" @default.
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