Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

Journal Browser

Ion Channels and Biosignal Transduction

Print Special Issue Flyer
Special Issue Editors
Special Issue Information
Keywords
Published Papers

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 10527

Share This Special Issue

Special Issue Editor

Dr. Ye Chun Ruan

E-Mail Website
Guest Editor

Department of Biomedical Engineering, The Hong Kong Polytechnic University, Kowloon, Hong Kong
Interests: ion channels; cell biology; physiology

Special Issue Information

Dear Colleagues,

Ion channels are membrane proteins that mediate the flow of ions across cell membranes. In excitable cells such as neurons and muscle cells, the activities of ion channels account for electrical-signal transduction underlying essential physiological events such as neuromuscular conjunction and cardiovascular contractions. In non-excitable cells such as epithelial cells, ion channels are crucial to pH and electrolyte homeostasis. Many other new roles of ion channels have emerged such as connecting environmental (e.g., mechanical) cues to intracellular signaling transduction, functional alterations, and gene expression changes. Problems in ion channels result in human diseases. Given their cellular localization in relatively accessible plasma membranes, many ion channels have been the molecular targets for pharmaceutical drugs for treating various diseases. More recently, ion channels are being developed as the molecular sensors for physical interventions (e.g., light, mechanical forces) to modulate cellular signaling and thus cell functions.

This Special Issue warmly welcomes recent studies in a broad range of disciplines including molecular biology, physiology, cell biology and biomedical engineering with a focus on ion channels, either to explore new physiological roles of ion channels in biosignal transduction or to develop ion channels as mediators for chemical or physical interventions.

Dr. Ye Chun Ruan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

ion channel
signal transduction
bioelectrical signals
biophysical signals
mechanotransduction
cellular homeostasis
ion channel drugs
physical intervention
optogenetics
molecular sensors

Published Papers (6 papers)

Download All Papers

Research

Jump to: Review

13 pages, 2613 KiB

Open AccessArticle

CFTR Modulates Hypothalamic Neuron Excitability to Maintain Female Cycle

by Yong Wu, Yanting Que, Junjiang Chen, Lei Sun, Jinghui Guo and Ye Chun Ruan

Int. J. Mol. Sci. 2023, 24(16), 12572; https://doi.org/10.3390/ijms241612572 - 08 Aug 2023

Viewed by 1057

Abstract

Cystic fibrosis transmembrane conductance regulator (CFTR), known as an epithelial Cl⁻ channel, is increasingly noted to be expressed in the nervous system, although whether and how it plays a role in neuronal excitability is unclear. Given the association of CFTR with fertility, we tested here possible involvement of CFTR in regulating hypothalamic neuron excitability. Patch-clamp and Ca²⁺ imaging showed that pharmacological inhibition of CFTR evoked electrical pulses and Ca²⁺ spikes in primary rat hypothalamic neurons, which was dependent on extracellular Cl⁻. Hypothalamic neurons in brain-slice preparations from adult female mice with CFTR mutation (DF508) exhibited significantly reduced electrical pulses as compared to the wild-type controls. Removal of extracellular Cl⁻ eliminated hypothalamic electrical pulses in the wild-type brain slices, which was reversible by subsequent addition of Cl⁻. In adult female mice, Ca²⁺ indicator (GCaMP6s)-based fiber-photometry showed that hypothalamic Ca²⁺ activities in vivo were enhanced at the proestrus/estrus phase as compared to the diestrus phase of the female cycle. Such estrus-associated hypothalamic activities were largely diminished in DF508 female mice, together with delayed puberty and disturbed female cycles. Therefore, these findings suggest a critical role of CFTR in modulating hypothalamic neuron excitability, which may account for the disturbed female cycles and reduced female fertility associated with CFTR mutations. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

23 pages, 4621 KiB

Open AccessArticle

5-HT₃ Receptors on Mitochondria Influence Mitochondrial Function

by Santosh T. R. B. Rao, Ilona Turek, Julian Ratcliffe, Simone Beckham, Cassandra Cianciarulo, Siti S. B. M. Y. Adil, Christine Kettle, Donna R. Whelan and Helen R. Irving

Int. J. Mol. Sci. 2023, 24(9), 8301; https://doi.org/10.3390/ijms24098301 - 05 May 2023

Cited by 3 | Viewed by 1735

Abstract

The 5-hydroxytryptamine 3 (5-HT₃) receptor belongs to the pentameric ligand-gated cation channel superfamily. Humans have five different 5-HT₃ receptor subunits: A to E. The 5-HT₃ receptors are located on the cell membrane, but a previous study suggested that mitochondria could also contain A subunits. In this article, we explored the distribution of 5-HT₃ receptor subunits in intracellular and cell-free mitochondria. Organelle prediction software supported the localization of the A and E subunits on the inner membrane of the mitochondria. We transiently transfected HEK293T cells that do not natively express the 5-HT₃ receptor with an epitope and fluorescent protein-tagged 5HT3A and 5HT3E subunits. Fluorescence microscopy and cell fractionation indicated that both subunits, A and E, localized to the mitochondria, while transmission electron microscopy revealed the location of the subunits on the mitochondrial inner membrane, where they could form heteromeric complexes. Cell-free mitochondria isolated from cell culture media colocalized with the fluorescent signal for A subunits. The presence of A and E subunits influenced changes in the membrane potential and mitochondrial oxygen consumption rates upon exposure to serotonin; this was inhibited by pre-treatment with ondansetron. Therefore, it is likely that the 5-HT₃ receptors present on mitochondria directly impact mitochondrial function and that this may have therapeutic implications. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

16 pages, 4827 KiB

Open AccessArticle

Intracellular Helix-Loop-Helix Domain Modulates Inactivation Kinetics of Mammalian TRPV5 and TRPV6 Channels

by Lisandra Flores-Aldama, Daniel Bustos, Deny Cabezas-Bratesco, Wendy Gonzalez and Sebastian E. Brauchi

Int. J. Mol. Sci. 2023, 24(5), 4470; https://doi.org/10.3390/ijms24054470 - 24 Feb 2023

Viewed by 1474

Abstract

TRPV5 and TRPV6 are calcium-selective ion channels expressed at the apical membrane of epithelial cells. Important for systemic calcium (Ca²⁺) homeostasis, these channels are considered gatekeepers of this cation transcellular transport. Intracellular Ca²⁺ exerts a negative control over the activity of these channels by promoting inactivation. TRPV5 and TRPV6 inactivation has been divided into fast and slow phases based on their kinetics. While slow inactivation is common to both channels, fast inactivation is characteristic of TRPV6. It has been proposed that the fast phase depends on Ca²⁺ binding and that the slow phase depends on the binding of the Ca²⁺/Calmodulin complex to the internal gate of the channels. Here, by means of structural analyses, site-directed mutagenesis, electrophysiology, and molecular dynamic simulations, we identified a specific set of amino acids and interactions that determine the inactivation kinetics of mammalian TRPV5 and TRPV6 channels. We propose that the association between the intracellular helix-loop-helix (HLH) domain and the TRP domain helix (TDh) favors the faster inactivation kinetics observed in mammalian TRPV6 channels. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

Review

Jump to: Research

17 pages, 1388 KiB

Open AccessReview

Proteolytic Activation of the Epithelial Sodium Channel (ENaC): Its Mechanisms and Implications

by Mohammed Aufy, Ahmed M. Hussein, Tamara Stojanovic, Christian R. Studenik and Mohamed H. Kotob

Int. J. Mol. Sci. 2023, 24(24), 17563; https://doi.org/10.3390/ijms242417563 - 16 Dec 2023

Cited by 1 | Viewed by 1306

Abstract

Epithelial sodium channel (ENaC) are integral to maintaining salt and water homeostasis in various biological tissues, including the kidney, lung, and colon. They enable the selective reabsorption of sodium ions, which is a process critical for controlling blood pressure, electrolyte balance, and overall fluid volume. ENaC activity is finely controlled through proteolytic activation, a process wherein specific enzymes, or proteases, cleave ENaC subunits, resulting in channel activation and increased sodium reabsorption. This regulatory mechanism plays a pivotal role in adapting sodium transport to different physiological conditions. In this review article, we provide an in-depth exploration of the role of proteolytic activation in regulating ENaC activity. We elucidate the involvement of various proteases, including furin-like convertases, cysteine, and serine proteases, and detail the precise cleavage sites and regulatory mechanisms underlying ENaC activation by these proteases. We also discuss the physiological implications of proteolytic ENaC activation, focusing on its involvement in blood pressure regulation, pulmonary function, and intestinal sodium absorption. Understanding the mechanisms and consequences of ENaC proteolytic activation provides valuable insights into the pathophysiology of various diseases, including hypertension, pulmonary disorders, and various gastrointestinal conditions. Moreover, we discuss the potential therapeutic avenues that emerge from understanding these mechanisms, offering new possibilities for managing diseases associated with ENaC dysfunction. In summary, this review provides a comprehensive discussion of the intricate interplay between proteases and ENaC, emphasizing the significance of proteolytic activation in maintaining sodium and fluid balance in both health and disease. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

19 pages, 2073 KiB

Open AccessReview

Piezo1 in Digestive System Function and Dysfunction

by Jing He, Xiaotian Xie, Zhuanglong Xiao, Wei Qian, Lei Zhang and Xiaohua Hou

Int. J. Mol. Sci. 2023, 24(16), 12953; https://doi.org/10.3390/ijms241612953 - 19 Aug 2023

Cited by 2 | Viewed by 2027

Abstract

Piezo1, a non-selective cation channel directly activated by mechanical forces, is widely expressed in the digestive system and participates in biological functions physiologically and pathologically. In this review, we summarized the latest insights on Piezo1’s cellular effect across the entire digestive system, and discussed the role of Piezo1 in various aspects including ingestion and digestion, material metabolism, enteric nervous system, intestinal barrier, and inflammatory response within digestive system. The goal of this comprehensive review is to provide a solid foundation for future research about Piezo1 in digestive system physiologically and pathologically. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

14 pages, 2570 KiB

Open AccessReview

Spotlight on P2X7 Receptor PET Imaging: A Bright Target or a Failing Star?

by Stephan Schmidt, Andreas Isaak and Anna Junker

Int. J. Mol. Sci. 2023, 24(2), 1374; https://doi.org/10.3390/ijms24021374 - 10 Jan 2023

Cited by 3 | Viewed by 1886

Abstract

The homotrimeric P2X7 receptor (P2X7R) is expressed by virtually all cells of the innate and adaptive immune system and plays a crucial role in various pathophysiological processes such as autoimmune and neurodegenerative diseases, inflammation, neuropathic pain and cancer. Consequently, the P2X7R is considered a promising target for therapy and diagnosis. As the development of tracers comes hand-in-hand with the development of potent and selective receptor ligands, there is a rising number of PET tracers available in preclinical and clinical studies. This review analyzes the development of P2X7R positron emission tomography (PET) tracers and their potential in various PET imaging applications. Full article

(This article belongs to the Special Issue Ion Channels and Biosignal Transduction)

► Show Figures

Figure 1

Journal Menu

Journal Browser

Ion Channels and Biosignal Transduction

Share This Special Issue

Special Issue Editor

Special Issue Information

Keywords

Published Papers (6 papers)

Research

Review

Further Information

Guidelines

MDPI Initiatives

Follow MDPI