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Life
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Channel Proteins and Transporters in Human Health and Disease
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Channel Proteins and Transporters in Human Health and Disease

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".

Deadline for manuscript submissions: 30 June 2026 | Viewed by 2209

Special Issue Editors

Dr. Giorgia Scarpellino

E-Mail Website
Guest Editor
Department of Biology and Biotechnology “L. Spallanzani”, University of Pavia, 27100 Pavia, Italy
Interests: cell physiology; ion channel; transporters; calcium; signal transduction; endothelial cells; cell migration; angiogenesis; ion imaging; cell biology
Dr. Giorgia Chinigò

E-Mail Website
Guest Editor
Department of Life Sciences and Systems Biology, University of Torino, 10123 Torino, Italy
Interests: physiology; calcium signaling; cell migration; cell adhesion; endothelial cells; angiogenesis; ion channels; cancer cells; signal transduction; cellular crosstalk
Dr. Roberta De Zio

E-Mail Website
Guest Editor
Department of Biosciences, Biotechnologies and Environment, University of Bari Aldo Moro, 70125 Bari, Italy
Interests: cell physiology; electrophysiology, ion channels and channelopathies; signal transduction pathways; cardiac cell physiology; cardiomyopathy; stem cells and regenerative medicine; optogenetic modulation

Special Issue Information

Dear Colleagues,

Channel proteins and transporters; which mediate the flow of ions; water; and biomolecules across cell membranes; represent the main molecular machinery responsible for cellular functional adaptation in response to environmental stimuli. Indeed; they regulate membrane potential and cell excitability; intercellular communication and intracellular signal transduction; systemic and cellular pH; and salt and water homeostasis. Their functional expression is crucial for the proper functioning of cells; tissues; and organs; and they play a central role in cellular physiology; neuroscience; and cardiovascular research. In addition to their primary function; they have been linked to the onset of neurological/neurodegenerative disorders; cardiovascular diseases; and cancer. For instance; their dysregulation affects cell cycle dynamics; apoptosis; cell migration; vascularization; with potential dramatic consequences for cell and organ physiology and; ultimately; human health. As a result; they have gained increased attention as molecular biomarkers and promising pharmaceutical targets.

This special issue aims to illustrate new and promising findings; stimulating future research on these important proteins. Original manuscripts and reviews exploring different roles of channel proteins/transporters in various aspects of human health and disease; are welcome (e.g., new approaches to study their expression; structure; and function or current insights into molecular mechanisms of pathological dysregulation that open new avenues for therapy and drug design).

Dr. Giorgia Scarpellino
Dr. Giorgia Chinigò
Dr. Roberta De Zio
Guest Editors

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 250 words) can be sent to the Editorial Office for assessment.

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. Life is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). 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

  • channel proteins
  • transporters
  • ion channel

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Published Papers (2 papers)

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Research

19 pages, 1663 KB  
Article
Aglianico Grape Pomace Extract Reduces Cardiac Pacemaker Activity by Decreasing Hyperpolarization-Activated Current Density Independently of cAMP Signaling
by Roberta De Zio, Maira Certini, Eugenia Pignataro, Daniela Russo, Simona Ida Scorza, Serena Milano, Giuseppe Procino, René Massimiliano Marsano, Maria Svelto, Isabella Maiellaro, Luigi Milella, Monica Carmosino and Andrea Gerbino
Life 2026, 16(5), 786; https://doi.org/10.3390/life16050786 - 8 May 2026
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Abstract
Grape pomace extract (GPE) from Vitis vinifera L. cv. Aglianico is rich in polyphenols with recognized cardioprotective properties, yet its direct electrophysiological effects on spontaneous cardiac activity have not been previously investigated. Here, we examined the chronotropic effects of GPE using two complementary [...] Read more.
Grape pomace extract (GPE) from Vitis vinifera L. cv. Aglianico is rich in polyphenols with recognized cardioprotective properties, yet its direct electrophysiological effects on spontaneous cardiac activity have not been previously investigated. Here, we examined the chronotropic effects of GPE using two complementary models: HL-1 cardiomyocytes, assessed by whole-cell patch-clamp and intracellular Ca2+ imaging, and the Drosophila melanogaster larval heart tube, evaluated by optical recording. In HL-1 cells, chronic treatment with 25 µg/mL GPE for 48 h significantly reduced potential spontaneous action frequency and selectively prolonged the diastolic depolarization phase without altering action potential morphology, depolarization-activated currents, or cytosolic Ca2+ homeostasis. GPE reduced the hyperpolarization-activated funny current (If) density without shifting its voltage dependence. GPE-treated cells retained cAMP sensitivity, as both isoproterenol and intracellular 8-Br-cAMP significantly increased If amplitude, while ELISA quantification confirmed that global cAMP levels were unaffected by GPE. In Drosophila larvae, a cAMP-independent myogenic preparation, GPE administered in the diet significantly reduced heart rate. These findings demonstrate that Aglianico GPE exerts a negative chronotropic effect through a mechanism that reduces functional If density without altering cAMP availability or HCN channel voltage dependence, and reveal a cAMP-independent component of action conserved across phylogenetically distant species. Full article
(This article belongs to the Special Issue Channel Proteins and Transporters in Human Health and Disease)
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10 pages, 1108 KB  
Article
HPLC Purification of TRPM8 and Experimental Confirmation of Its Cholesterol Affinity on Synthetic Lipid Raft-like Models
by Clotilde Beatrice Angelucci, Annalaura Sabatucci, Alexandrine Kurtz, Davide Laurenti, Beatrice Dufrusine, Enrico Dainese and Antonio Francioso
Life 2026, 16(3), 392; https://doi.org/10.3390/life16030392 - 28 Feb 2026
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Abstract
This study presents the successful expression, purification, and functional characterization of the human TRPM8 ion channel, a key player in temperature sensing and pain modulation. Using a modified bacterial expression protocol and DDM-based solubilization, TRPM8 was purified via HPLC-SEC and analyzed for its [...] Read more.
This study presents the successful expression, purification, and functional characterization of the human TRPM8 ion channel, a key player in temperature sensing and pain modulation. Using a modified bacterial expression protocol and DDM-based solubilization, TRPM8 was purified via HPLC-SEC and analyzed for its membrane-binding properties. FRET-based assays with synthetic lipid rafts revealed a strong and selective affinity of TRPM8 for cholesterol-containing membranes, suggesting cholesterol’s role in modulating TRPM8 localization and activity. These findings provide quantitative in vitro evidence of TRPM8–cholesterol interactions and establish a robust model system for future structural and functional studies of membrane-associated proteins. Full article
(This article belongs to the Special Issue Channel Proteins and Transporters in Human Health and Disease)
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