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Sodium Channel Isoform Diversity Underlies Chamber-Specific Cardiac Excitability
Journal article   Peer reviewed

Sodium Channel Isoform Diversity Underlies Chamber-Specific Cardiac Excitability

Colin J Clark, Christian E Anderson, Alex Dou, Jason M Dierdorff, Jason D Galpin, Lionel Gissot, Samantha G Thompson, Hannah Choi, Jin-Young Yoon, Daniel T Infield, …
Circulation research
03/25/2026
DOI: 10.1161/CIRCRESAHA.125.328159
PMID: 41878815

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Abstract

BACKGROUND: NaV (voltage-gated sodium) channels drive cardiac excitability. Although NaV1.5 is the primary cardiac isoform, the composition and functional contributions of non-NaV1.5 isoforms in the heart remain unclear. METHODS: Here, we developed a chemical-genetic mouse model (NaV1.5GX/GX) in which NaV1.5 can be selectively and reversibly inhibited by acyl- and aryl-sulfonamide compounds (GX [acyl- and aryl-sulfonamide compounds typically denoted by the name GX-### and associated items] drugs). Cardiac activity was assessed by electrocardiograms in vivo, and optical mapping was used for imaging of ex vivo hearts. Whole-cell voltage-clamp in tandem with validated toxins and isoform-selective inhibitors were used to examine sodium current composition. RESULTS: NaV1.5GX/GX mice exhibited normal cardiac function at baseline, but acute GX drug administration caused profound conduction defects and arrhythmias. Whole-heart optical mapping revealed dose-dependent chamber-specific sensitivity to NaV1.5 inhibition, with the right ventricle being the most sensitive, followed by the left ventricle, left atrium, and right atrium. Patch-clamp recordings of isolated cardiomyocytes with application of NaV isoform-selective inhibitors showed that NaV1.5 contributed 93% of sodium current in the left ventricle, 79% in the right ventricle, and 78% in the atria. Non-NaV1.5 isoforms were differentially enriched across chambers: NaV1.8 in the left ventricle, NaV1.1/1.3 in the right ventricle, and NaV1.2/1.6/1.7 in the atria. CONCLUSIONS: These results reveal a surprising chamber-specific isoform landscape of cardiac sodium currents, which may underlie the right ventricular predominant phenotype of Brugada syndrome. These data highlight non-NaV1.5 isoforms as potential mediators of chamber-specific cardiac pathologies and as pharmacological targets.
Protein Engineering arrhythmias, cardiac sodium Brugada syndrome protein isoforms

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