Hypokalemic periodic paralysis (HypoPP) is a rare genetic disease associated with mutations in CACNA1S or SCN4A encoding the voltage-gated Ca2+ channel Cav1.1 or the voltage-gated Na+ channel Nav1.4, respectively. Most HypoPP-associated missense changes occur at the arginine residues within the voltage-sensing domain (VSD) of these channels. It is established that such mutations destroy the hydrophobic seal that separates external fluid and the internal cytosolic crevices, resulting in the generation of aberrant leak currents called gating pore currents. Presently, the gating pore currents are thought to underlie HypoPP. Here, based on HEK293T cells and by using the Sleeping Beauty transposon system, we generated HypoPP-model cell lines that co-express the mouse inward-rectifier K+ channel (mKir2.1) and HypoPP2-associated Nav1.4 channel. Whole-cell patch-clamp measurements confirmed that mKir2.1 successfully hyperpolarizes the membrane potential to levels comparable to those of myofibers, and that some Nav1.4 variants induce notable proton-based gating pore currents. Importantly, we succeeded in fluorometrically measuring the gating pore currents in these variants by using a ratiometric pH indicator. Our optical method provides a potential in vitro platform for high-throughput drug screening, not only for HypoPP but also for other channelopathies caused by VSD mutations.
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http://dx.doi.org/10.1242/dmm.049704 | DOI Listing |
ACS Appl Bio Mater
January 2025
College of Chemical and Biological Engineering, Zhejiang Provincial Key Laboratory of Advanced Chemical Engineering Manufacture Technology, Zhejiang University, Hangzhou 310027, China.
Traditional drug-delivery methods are limited by low bioavailability and nonspecific drug distribution, resulting in poor therapeutic efficacy and potential risks of toxicity. Mesoporous silica nanoparticles (MSNs) have attracted wide attention as drug-delivery carriers due to their large specific surface area, adjustable pore size, good mechanical strength, good biocompatibility, and rich hydroxyl groups on their surface. In this paper, MSNs were synthesized by a template method, and the morphology and pore structure were regulated.
View Article and Find Full Text PDFThe big potassium (BK) channels remain open with a small limiting probability of ∼ 10 at minimal Ca and negative voltages < -100 mV. The molecular origin and functional significance of such "intrinsic opening" are not understood. Here we combine atomistic simulations and electrophysiological experiments to show that the intrinsic opening of BK channels is an inherent property of the vapor barrier, generated by hydrophobic dewetting of the BK inner pore in the deactivated state.
View Article and Find Full Text PDFBackground And Purpose: Polycystins (PKD2, PKD2L1) are voltage-gated and Ca -modulated members of the transient receptor potential (TRP) family of ion channels. Loss of PKD2L1 expression results in seizure-susceptibility and autism-like features in mice, whereas variants in PKD2 cause autosomal dominant polycystic kidney disease. Despite decades of evidence clearly linking their dysfunction to human disease and demonstrating their physiological importance in the brain and kidneys, the polycystin pharmacophore remains undefined.
View Article and Find Full Text PDFbioRxiv
January 2025
Vollum Institute, Oregon Health and Science University, 3232 SW Research Drive, Portland, OR, USA.
The bile acid-sensitive ion channel (BASIC) is the least understood member of the mammalian epithelial Na channel/degenerin (ENaC/DEG) superfamily of ion channels, which are involved in a variety of physiological processes. While some members of this superfamily, including BASIC, are inhibited by extracellular Ca (Ca ), the molecular mechanism underlying Ca modulation remains unclear. Here, by determining the structure of human BASIC in the presence and absence of Ca using single particle cryo-electron microscopy (cryo-EM), we reveal Ca-dependent conformational changes in the transmembrane domain and β-linkers.
View Article and Find Full Text PDFJ Gen Physiol
March 2025
Department of Biomolecular Sciences, School of Pharmacy, University of Mississippi, Oxford, MS, USA.
Voltage-gated sodium (Nav) channels are pivotal for cellular signaling, and mutations in Nav channels can lead to excitability disorders in cardiac, muscular, and neural tissues. A major cluster of pathological mutations localizes in the voltage-sensing domains (VSDs), resulting in either gain-of-function, loss-of-function effects, or both. However, the mechanism behind this functional diversity of mutations at equivalent positions remains elusive.
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