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- W2012190633 abstract "The synaptosomal plasma membrane Ca2+-ATPase (PMCA) plays an essential role in regulating intracellular Ca2+ concentration in brain. We have recently found that PMCA is the only Ca2+ pump in brain which is inhibited by amyloid-β peptide (Aβ), a neurotoxic peptide implicated in the pathology of Alzheimer's disease (AD) [1], but the mechanism of inhibition is lacking. In the present study we have characterized the inhibition of PMCA by Aβ. Results from kinetic assays indicate that Aβ aggregates are more potent inhibitors of PMCA activity than monomers. The inhibitory effect of Aβ could be blocked by pretreating the purified protein with Ca2+-calmodulin, the main endogenous activator of PMCA, and the activity of truncated PMCA lacking the calmodulin binding domain was not affected by Aβ. Dot-overlay experiments indicated a physical association of Aβ with PMCA and also with calmodulin. Thus, calmodulin could protect PMCA from inhibition by Aβ by burying exposed sites on PMCA, making them inaccessible to Aβ, and also by direct binding to the peptide. These results suggest a protective role of calmodulin against neuronal Ca2+ dysregulation by PMCA inhibition induced by Aβ." @default.
- W2012190633 created "2016-06-24" @default.
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- W2012190633 creator A5015694839 @default.
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- W2012190633 date "2012-06-01" @default.
- W2012190633 modified "2023-09-23" @default.
- W2012190633 title "Calmodulin antagonizes amyloid-β peptides-mediated inhibition of brain plasma membrane Ca2+-ATPase" @default.
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- W2012190633 doi "https://doi.org/10.1016/j.bbadis.2012.02.013" @default.
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