Soluble β-Amyloid Oligomers Selectively Upregulate TRPC3 in Excitatory Neurons via Calcineurin-Coupled NFAT

To investigate how dysregulated transient receptor potential canonical channels (TRPCs) are associated with Alzheimer’s disease (AD), we challenged primary neurons with amyloid-β (Aβ). Both the naturally secreted or synthetic Aβ oligomers (AβOs) induced long-lasting increased TRPC3 and downregulated...

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Main Authors: Zhengjun Wang, Dongyi Ding, Jiaxing Wang, Ling Chen, Qingming Dong, Moumita Khamrai, Yuyang Zhou, Akihiro Ishii, Kazuko Sakata, Wei Li, Jianyang Du, Thirumalini Vaithianathan, Fu-Ming Zhou, Francesca-Fang Liao
Format: Article
Language:English
Published: MDPI AG 2025-06-01
Series:Cells
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Online Access:https://www.mdpi.com/2073-4409/14/11/843
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Summary:To investigate how dysregulated transient receptor potential canonical channels (TRPCs) are associated with Alzheimer’s disease (AD), we challenged primary neurons with amyloid-β (Aβ). Both the naturally secreted or synthetic Aβ oligomers (AβOs) induced long-lasting increased TRPC3 and downregulated the TRPC6 expression in mature excitatory neurons (CaMKIIα-high) via a Ca<sup>2+</sup>-dependent calcineurin-coupled NFAT transcriptionally and calpain-mediated protein degradation, respectively. The TRPC3 expression was also found to be upregulated in pyramidal neurons of human AD brains. The selective downregulation of the <i>Trpc6</i> gene induced synaptotoxicity, while no significant effect was observed from the Trpc3-targeting siRNA, suggesting potentially differential roles of TRPC3 and 6 in modulating the synaptic morphology and functions. Electrophysiological recordings of mouse hippocampal slices overexpressing TRPC3 revealed increased neuronal hyperactivity upon the TRPC3 channel activation by its agonist. Furthermore, the AβO-mediated synaptotoxicity appeared to be positively correlated with the degrees of the induced dendritic Ca<sup>2+</sup> flux in neurons, which was completely prevented by the co-treatment with two pyrazole-based TRPC3-selective antagonists Pyr3 or Pyr10. Taken together, our findings suggest that the aberrantly upregulated TRPC3 is another ion channel critically contributing to the process of AβO-induced Ca<sup>2+</sup> overload, neuronal hyperexcitation, and synaptotoxicity, thus representing a potential therapeutic target of AD.
ISSN:2073-4409