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Jensen LE, Bultynck G, Luyten T, et al. Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca(2+) via InsP3R-dependent and -independent mechanisms. Front Mol Neurosci. 2013;6:36doi: 10.3389/fnmol.2013.00036.
Jensen, L. E., Bultynck, G., Luyten, T., Amijee, H., Bootman, M. D., & Roderick, H. L. (2013). Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca(2+) via InsP3R-dependent and -independent mechanisms. Frontiers in molecular neuroscience, 636. https://doi.org/10.3389/fnmol.2013.00036
Jensen, Laura E, et al. "Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca(2+) via InsP3R-dependent and -independent mechanisms." Frontiers in molecular neuroscience vol. 6 (2013): 36. doi: https://doi.org/10.3389/fnmol.2013.00036
Jensen LE, Bultynck G, Luyten T, Amijee H, Bootman MD, Roderick HL. Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca(2+) via InsP3R-dependent and -independent mechanisms. Front Mol Neurosci. 2013 Nov 05;6:36. doi: 10.3389/fnmol.2013.00036. eCollection 2013. PMID: 24204331; PMCID: PMC3817845.
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Front Mol Neurosci. 2013 Nov 05;6:36. doi: 10.3389/fnmol.2013.00036. eCollection 2013.

Alzheimer's disease-associated peptide Aβ42 mobilizes ER Ca(2+) via InsP3R-dependent and -independent mechanisms.

Frontiers in molecular neuroscience

Laura E Jensen, Geert Bultynck, Tomas Luyten, Hozeefa Amijee, Martin D Bootman, H Llewelyn Roderick

Affiliations

  1. Babraham Institute, Babraham Research Campus Babraham, Cambridge, UK.

PMID: 24204331 PMCID: PMC3817845 DOI: 10.3389/fnmol.2013.00036

Abstract

Dysregulation of Ca(2+) homeostasis is considered to contribute to the toxic action of the Alzheimer's disease (AD)-associated amyloid-β-peptide (Aβ). Ca(2+) fluxes across the plasma membrane and release from intracellular stores have both been reported to underlie the Ca(2+) fluxes induced by Aβ42. Here, we investigated the contribution of Ca(2+) release from the endoplasmic reticulum (ER) to the effects of Aβ42 upon Ca(2+) homeostasis and the mechanism by which Aβ42 elicited these effects. Consistent with previous reports, application of soluble oligomeric forms of Aβ42 induced an elevation in intracellular Ca(2+). The Aβ42-stimulated Ca(2+) signals persisted in the absence of extracellular Ca(2+) indicating a significant contribution of Ca(2+) release from the ER Ca(2+) store to the generation of these signals. Moreover, inositol 1,4,5-trisphosphate (InsP3) signaling contributed to Aβ42-stimulated Ca(2+) release. The Ca(2+) mobilizing effect of Aβ42 was also observed when applied to permeabilized cells deficient in InsP3 receptors, revealing an additional direct effect of Aβ42 upon the ER, and a mechanism for induction of toxicity by intracellular Aβ42.

Keywords: Alzheimer's disease; Aβ oligomers; InsP3 receptors/InsP3Rs; InsP3/IP3; calcium/Ca2+; endoplasmic reticulum/ER

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