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Special Issue "TRPM Channels"

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

Deadline for manuscript submissions: 1 July 2021.

Special Issue Editors

Dr. Balazs Istvan Toth
E-Mail Website
Guest Editor
Laboratory of Molecular and Cellular Physiology, Department of Physiology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary
Interests: TRPM channels
Prof. Dr. Thomas Voets
Website
Guest Editor
Laboratory of Ion Channel Research (VIB-KU Leuven Center for Brain & Disease Research) Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium
Interests: TRPM channels

Special Issue Information

Dear Colleagues,

The Melastatin (TRPM) subfamily of the fascinating Transient Receptor Potential (TRP) ion channels forms a structurally and functionally diverse group of eight close relatives of cation channels. They are characterized by diverse gating stimuli, including changes in environmental temperature, osmolarity, ADP-ribose or intra- and extracellular ions. They function as thermosensors, gatekeepers of cellular ion homeostasis, or regulators of secretory functions, inflammatory processes and redox signaling. Some of them possess a unique double identity, simultaneously functioning as ion channels and enzymes (“chanzymes”).

TRPM channels are widely studied in the sensory system, in various immune cells, as well as in epithelial barriers, but they are virtually expressed by every cell-types of the human body. Intense research of the past two decades advanced a lot in their understanding and in the last years we gained a deeper insight into their molecular structure. However, in spite of our rapidly growing knowledge, there are still several mysteries in this intriguing group of ion channels. This Special Issue provides a forum for summarizing our current knowledge and presenting selected chapters of actual research targeting any aspect of these exciting members of TRP channels. 

Dr. Balazs Istvan Toth
Prof. Dr. Thomas Voets
Guest Editors

Manuscript Submission Information

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Keywords

  • TRP ion channels
  • TRPM channels
  • molecular structure
  • ion channels

Published Papers (3 papers)

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Research

Open AccessArticle
Oxaliplatin Causes Transient Changes in TRPM8 Channel Activity
Int. J. Mol. Sci. 2021, 22(9), 4962; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22094962 - 07 May 2021
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Abstract
Oxaliplatin is a third-generation platinum-based anticancer drug that is widely used as first-line treatment for colorectal carcinoma. Patients treated with oxaliplatin develop an acute peripheral pain several hours after treatment, mostly characterized by cold allodynia as well as a long-term chronic neuropathy. These [...] Read more.
Oxaliplatin is a third-generation platinum-based anticancer drug that is widely used as first-line treatment for colorectal carcinoma. Patients treated with oxaliplatin develop an acute peripheral pain several hours after treatment, mostly characterized by cold allodynia as well as a long-term chronic neuropathy. These two phenomena seem to be causally connected. However, the underlying mechanisms that trigger the acute peripheral pain are still poorly understood. Here we show that the activity of the transient receptor potential melastatin 8 (TRPM8) channel but not the activity of any other member of the TRP channel family is transiently increased 1 h after oxaliplatin treatment and decreased 24 h after oxaliplatin treatment. Mechanistically, this is connected with activation of the phospholipase C (PLC) pathway and depletion of phosphatidylinositol 4,5-bisphosphate (PIP2) after oxaliplatin treatment. Inhibition of the PLC pathway can reverse the decreased TRPM8 activity as well as the decreased PIP2-concentrations after oxaliplatin treatment. In summary, these results point out transient changes in TRPM8 activity early after oxaliplatin treatment and a later occurring TRPM8 channel desensitization in primary sensory neurons. These mechanisms may explain the transient cold allodynia after oxaliplatin treatment and highlight an important role of TRPM8 in oxaliplatin-induced acute and neuropathic pain. Full article
(This article belongs to the Special Issue TRPM Channels)
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Open AccessArticle
Species-Specific Regulation of TRPM2 by PI(4,5)P2 via the Membrane Interfacial Cavity
Int. J. Mol. Sci. 2021, 22(9), 4637; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22094637 - 28 Apr 2021
Viewed by 193
Abstract
The human apoptosis channel TRPM2 is stimulated by intracellular ADR-ribose and calcium. Recent studies show pronounced species-specific activation mechanisms. Our aim was to analyse the functional effect of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), commonly referred to as PIP2, on different TRPM2 [...] Read more.
The human apoptosis channel TRPM2 is stimulated by intracellular ADR-ribose and calcium. Recent studies show pronounced species-specific activation mechanisms. Our aim was to analyse the functional effect of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), commonly referred to as PIP2, on different TRPM2 orthologues. Moreover, we wished to identify the interaction site between TRPM2 and PIP2. We demonstrate a crucial role of PIP2, in the activation of TRPM2 orthologues of man, zebrafish, and sea anemone. Utilizing inside-out patch clamp recordings of HEK-293 cells transfected with TRPM2, differential effects of PIP2 that were dependent on the species variant became apparent. While depletion of PIP2 via polylysine uniformly caused complete inactivation of TRPM2, restoration of channel activity by artificial PIP2 differed widely. Human TRPM2 was the least sensitive species variant, making it the most susceptible one for regulation by changes in intramembranous PIP2 content. Furthermore, mutations of highly conserved positively charged amino acid residues in the membrane interfacial cavity reduced the PIP2 sensitivity in all three TRPM2 orthologues to varying degrees. We conclude that the membrane interfacial cavity acts as a uniform PIP2 binding site of TRPM2, facilitating channel activation in the presence of ADPR and Ca2+ in a species-specific manner. Full article
(This article belongs to the Special Issue TRPM Channels)
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Open AccessArticle
TRPM7-Mediated Calcium Transport in HAT-7 Ameloblasts
Int. J. Mol. Sci. 2021, 22(8), 3992; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22083992 - 13 Apr 2021
Viewed by 299
Abstract
TRPM7 plays an important role in cellular Ca2+, Zn2+ and Mg2+ homeostasis. TRPM7 channels are abundantly expressed in ameloblasts and, in the absence of TRPM7, dental enamel is hypomineralized. The potential role of TRPM7 channels in Ca2+ transport [...] Read more.
TRPM7 plays an important role in cellular Ca2+, Zn2+ and Mg2+ homeostasis. TRPM7 channels are abundantly expressed in ameloblasts and, in the absence of TRPM7, dental enamel is hypomineralized. The potential role of TRPM7 channels in Ca2+ transport during amelogenesis was investigated in the HAT-7 rat ameloblast cell line. The cells showed strong TRPM7 mRNA and protein expression. Characteristic TRPM7 transmembrane currents were observed, which increased in the absence of intracellular Mg2+ ([Mg2+]i), were reduced by elevated [Mg2+]i, and were inhibited by the TRPM7 inhibitors NS8593 and FTY720. Mibefradil evoked similar currents, which were suppressed by elevated [Mg2+]i, reducing extracellular pH stimulated transmembrane currents, which were inhibited by FTY720. Naltriben and mibefradil both evoked Ca2+ influx, which was further enhanced by the acidic intracellular conditions. The SOCE inhibitor BTP2 blocked Ca2+ entry induced by naltriben but not by mibefradil. Thus, in HAT-7 cells, TRPM7 may serves both as a potential modulator of Orai-dependent Ca2+ uptake and as an independent Ca2+ entry pathway sensitive to pH. Therefore, TRPM7 may contribute directly to transepithelial Ca2+ transport in amelogenesis. Full article
(This article belongs to the Special Issue TRPM Channels)
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