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

Deadline for manuscript submissions: closed (31 January 2021) | Viewed by 40814

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Dr. Viktorie Vlachova

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Department of Cellular Neurophysiology, Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic
Interests: thermosensitive TRP channels; membrane biophysics; electrophysiology; nociception; mathematical modeling
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Prof. Peter M. Zygmunt

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Department of Clinical Sciences Malmö, Lund University, SE-214 28 Malmö, Sweden
Interests: TRP channel chemosensitivity; TRP channel thermosensitivity; TRP channel mechanosensitivity; TRP secretory cell signaling; TRP pharmacology; nociception; pain
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Dear Colleagues,

The transient receptor potential ankyrin 1 receptor (TRPA1) is a cation channel expressed in dorsal root, trigeminal, and visceral primary sensory neurons, but also in various non-neuronal cells such as lung fibroblast and epithelial cells, smooth muscle cells, hair cells, keratinocytes, odontoblasts, astroglia, Schwann cells, and arterial vessels. There, TRPA1 acts as a multipurpose sensor of harmful signals, being activated by a wide range of chemical and physical stimuli. Accumulating evidence links the physiological functions of TRPA1 to nociception, inflammation, temperature perception, mechanosensation, insulin secretion, itching, respiratory functions, regulation of the cardiovascular system, and also the homeostatic balance between the immune and nociceptive systems. Given the wide expression pattern of TRPA1, a precise knowledge of the channel function is essential before it can be considered a potential target for the development of new, safe, and clinically relevant drugs.

Until very recently, information about the three-dimensional structure of TRPA1 has lagged behind information obtained from mutational and functional studies. At the break of 2019/2020, high-resolution structures of TRPA1 in different conformations have been published as a result of the recent “resolution revolution” in single-particle cryo-electron microscopy. Obviously, these new findings will further allow the rationalization of structure–activity studies, understanding the functional impact of TRPA1 genetic polymorphisms, and, perhaps more importantly, rational screening of novel modulators as potential selective therapeutic agents.

This Special Issue will provide a platform for original research papers and reviews describing the most recent findings in the TRPA1 field, covering any topics related to the biophysics, structure, pharmacology, physiological/pathophysiological roles, new molecular-based therapeutic strategies, and human genetic association studies.

Dr. Viktorie Vlachova
Prof. Peter M. Zygmunt
Guest Editors

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Keywords

Transient receptor potential ankyrin subtype 1
Structure-function
Pain
Sensory neuron
Inflammation
Thermosensitive TRP channel
Mechanosensitive TRP channel

Published Papers (12 papers)

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14 pages, 1000 KiB

Open AccessArticle

Nitroxyl Delivered by Angeli’s Salt Causes Short-Lasting Activation Followed by Long-Lasting Deactivation of Meningeal Afferents in Models of Headache Generation

by Stephanie K. Stöckl, Roberto de Col, Milos R. Filipovic and Karl Messlinger

Int. J. Mol. Sci. 2022, 23(4), 2330; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23042330 - 19 Feb 2022

Viewed by 1673

Abstract

The role of TRPA1 receptor channels in meningeal nociception underlying the generation of headaches is still unclear. Activating as well as inhibitory effects of TRPA1 agonists have been reported in animal models of headache. The aim of the present study was to clarify the effect of the TRPA1 agonist nitroxyl (HNO) delivered by Angeli’s salt in two rodent models of meningeal nociception. Single fibre recordings were performed using half-skull preparations of mice (C57BL/6) in vitro. Angeli’s salt solution (AS, 300 µM) caused short-lasting vigorous increases in neuronal activity of primary meningeal afferents, followed by deactivation and desensitisation. These effects were similar in TRPA1 knockout and even more pronounced in TRPA1/TRPV1 double-knockout mice in comparison to wild-type mice. The activity of spinal trigeminal neurons with afferent input from the dura mater was recorded in vivo in anesthetised rats. AS (300 µM) or the TRPA1 agonist acrolein (100 and 300 µM) was applied to the exposed dura mater. AS caused no significant changes in spontaneous activity, while the mechanically evoked activity was reduced after acrolein application. These results do not confirm the assumption that activation of trigeminal TRPA1 receptor channels triggers the generation of headaches or contributes to its aggravation. Instead, there is evidence that TRPA1 activation may have an inhibitory function in the nociceptive trigeminal system. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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12 pages, 12298 KiB

Open AccessArticle

Atractylodin Produces Antinociceptive Effect through a Long-Lasting TRPA1 Channel Activation

by Hirosato Kanda, Yanjing Yang, Shaoqi Duan, Yoko Kogure, Shenglan Wang, Emiko Iwaoka, Miku Ishikawa, Saki Takeda, Hidemi Sonoda, Kyoka Mizuta, Shunji Aoki, Satoshi Yamamoto, Koichi Noguchi and Yi Dai

Int. J. Mol. Sci. 2021, 22(7), 3614; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073614 - 31 Mar 2021

Cited by 5 | Viewed by 2606

Abstract

Atractylodin (ATR) is a bioactive component found in dried rhizomes of Atractylodes lancea (AL) De Candolle. Although AL has accumulated empirical evidence for the treatment of pain, the molecular mechanism underlying the anti-pain effect of ATR remains unclear. In this study, we found that ATR increases transient receptor potential ankyrin-1 (TRPA1) single-channel activity in hTRPA1 expressing HEK293 cells. A bath application of ATR produced a long-lasting calcium response, and the response was completely diminished in the dorsal root ganglion neurons of TRPA1 knockout mice. Intraplantar injection of ATR evoked moderate and prolonged nociceptive behavior compared to the injection of allyl isothiocyanate (AITC). Systemic application of ATR inhibited AITC-induced nociceptive responses in a dose-dependent manner. Co-application of ATR and QX-314 increased the noxious heat threshold compared with AITC in vivo. Collectively, we concluded that ATR is a unique agonist of TRPA1 channels, which produces long-lasting channel activation. Our results indicated ATR-mediated anti-nociceptive effect through the desensitization of TRPA1-expressing nociceptors. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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21 pages, 5480 KiB

Open AccessArticle

The Agonist Action of Alkylphenols on TRPA1 Relates to Their Effects on Membrane Lipid Order: Implications for TRPA1-Mediated Chemosensation

by Justyna B. Startek, Alina Milici, Robbe Naert, Andrei Segal, Yeranddy A. Alpizar, Thomas Voets and Karel Talavera

Int. J. Mol. Sci. 2021, 22(7), 3368; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073368 - 25 Mar 2021

Cited by 9 | Viewed by 2429

Abstract

The Transient Receptor Potential Ankyrin 1 cation channel (TRPA1) is a broadly-tuned chemosensor expressed in nociceptive neurons. Multiple TRPA1 agonists are chemically unrelated non-electrophilic compounds, for which the mechanisms of channel activation remain unknown. Here, we assess the hypothesis that such chemicals activate TRPA1 by inducing mechanical perturbations in the plasma membrane. We characterized the activation of mouse TRPA1 by non-electrophilic alkylphenols (APs) of different carbon chain lengths in the para position of the aromatic ring. Having discarded oxidative stress and the action of electrophilic mediators as activation mechanisms, we determined whether APs induce mechanical perturbations in the plasma membrane using dyes whose fluorescence properties change upon alteration of the lipid environment. APs activated TRPA1, with potency increasing with their lipophilicity. APs increased the generalized polarization of Laurdan fluorescence and the anisotropy of the fluorescence of 1,6-diphenyl-1,3,5-hexatriene (DPH), also according to their lipophilicity. Thus, the potency of APs for TRPA1 activation is an increasing function of their ability to induce lipid order and membrane rigidity. These results support the hypothesis that TRPA1 senses non-electrophilic compounds by detecting the mechanical alterations they produce in the plasma membrane. This may explain how structurally unrelated non-reactive compounds induce TRPA1 activation and support the role of TRPA1 as an unspecific sensor of potentially noxious compounds. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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12 pages, 2014 KiB

Open AccessArticle

Transient Receptor Potential Ankyrin 1 (TRPA1)—An Inflammation-Induced Factor in Human HaCaT Keratinocytes

by Samu Luostarinen, Mari Hämäläinen and Eeva Moilanen

Int. J. Mol. Sci. 2021, 22(7), 3322; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073322 - 24 Mar 2021

Cited by 12 | Viewed by 2888

Abstract

Transient receptor potential ankyrin 1 (TRPA1) is an ion channel mainly studied in sensory neurons where it mediates itch, pain and neurogenic inflammation. Recently, some nonneuronal cells have also been shown to express TRPA1 to support inflammatory responses. To address the role of TRPA1 in skin inflammation, we aimed to investigate TRPA1 expression in keratinocytes. HaCaT cells (a model of human keratinocytes) and skin biopses from wild-type and TRPA1 deficient mice were used in the studies. TRPA1 expression in nonstimulated keratinocytes was very low but significantly inducible by the proinflammatory cytokine tumor necrosis factor (TNF) in an nuclear factor kappa B (NF-κB), and mitogen-activated protein (MAP) kinase (p38 and c-Jun N-terminal kinase, JNK)-dependent manner. Interestingly, drugs widely used to treat skin inflammation, the calcineurin inhibitors tacrolimus and cyclosporine and the glucocorticoid dexamethasone, significantly decreased TRPA1 expression. Furthermore, pharmacological inhibition and genetic deletion of TRPA1 reduced the synthesis of TNF-induced monocyte chemoattractant protein 1 (MCP-1) in keratinocytes and mouse skin biopsies. In conclusion, these findings point to an inflammatory role for TRPA1 in keratinocytes and present TRPA1 as a potential drug target in inflammatory skin diseases. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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19 pages, 4467 KiB

Open AccessArticle

Renal Tubular Epithelial TRPA1 Acts as An Oxidative Stress Sensor to Mediate Ischemia-Reperfusion-Induced Kidney Injury through MAPKs/NF-κB Signaling

by Chung-Kuan Wu, Chia-Lin Wu, Tzong-Shyuan Lee, Yu Ru Kou and Der-Cherng Tarng

Int. J. Mol. Sci. 2021, 22(5), 2309; https://doi.org/10.3390/ijms22052309 - 25 Feb 2021

Cited by 17 | Viewed by 2804

Abstract

Oxidative stress and inflammation play important roles in the pathophysiology of acute kidney injury (AKI). Transient receptor potential ankyrin 1 (TRPA1) is a Ca2+-permeable ion channel that is sensitive to reactive oxygen species (ROS). The role of TRPA1 in AKI remains unclear. In this study, we used human and animal studies to assess the role of renal TRPA1 in AKI and to explore the regulatory mechanism of renal TRPA1 in inflammation via in vitro experiments. TRPA1 expression increased in the renal tubular epithelia of patients with AKI. The severity of tubular injury correlated well with tubular TRPA1 or 8-hydroxy-2′-deoxyguanosine expression. In an animal model, renal ischemia-reperfusion injury (IR) increased tubular TRPA1 expression in wild-type (WT) mice. Trpa1^−/− mice displayed less IR-induced tubular injury, oxidative stress, inflammation, and dysfunction in kidneys compared with WT mice. In the in vitro model, TRPA1 expression increased in renal tubular cells under hypoxia-reoxygenation injury (H/R) conditions. We demonstrated that H/R evoked a ROS-dependent TRPA1 activation, which elevated intracellular Ca²⁺ level, increased NADPH oxidase activity, activated MAPK/NF-κB signaling, and increased IL-8. Renal tubular TRPA1 may serve as an oxidative stress sensor and a crucial regulator in the activation of signaling pathways and promote the subsequent transcriptional regulation of IL-8. These actions might be evident in mice with IR or patients with AKI. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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21 pages, 1961 KiB

Open AccessArticle

Calmodulin Supports TRPA1 Channel Association with Opioid Receptors and Glutamate NMDA Receptors in the Nervous Tissue

by Elsa Cortés-Montero, María Rodríguez-Muñoz, M. Carmen Ruiz-Cantero, Enrique J. Cobos, Pilar Sánchez-Blázquez and Javier Garzón-Niño

Int. J. Mol. Sci. 2021, 22(1), 229; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22010229 - 28 Dec 2020

Cited by 8 | Viewed by 2567

Abstract

Transient receptor potential ankyrin member 1 (TRPA1) belongs to the family of thermo TRP cation channels that detect harmful temperatures, acids and numerous chemical pollutants. TRPA1 is expressed in nervous tissue, where it participates in the genesis of nociceptive signals in response to noxious stimuli and mediates mechanical hyperalgesia and allodynia associated with different neuropathies. The glutamate N-methyl-d-aspartate receptor (NMDAR), which plays a relevant role in allodynia to mechanical stimuli, is connected via histidine triad nucleotide-binding protein 1 (HINT1) and type 1 sigma receptor (σ1R) to mu-opioid receptors (MORs), which mediate the most potent pain relief. Notably, neuropathic pain causes a reduction in MOR antinociceptive efficacy, which can be reversed by blocking spinal NMDARs and TRPA1 channels. Thus, we studied whether TRPA1 channels form complexes with MORs and NMDARs that may be implicated in the aforementioned nociceptive signals. Our data suggest that TRPA1 channels functionally associate with MORs, delta opioid receptors and NMDARs in the dorsal root ganglia, the spinal cord and brain areas. These associations were altered in response to pharmacological interventions and the induction of inflammatory and also neuropathic pain. The MOR-TRPA1 and NMDAR-TRPA1 associations do not require HINT1 or σ1R but appear to be mediated by calcium-activated calmodulin. Thus, TRPA1 channels may associate with NMDARs to promote ascending acute and chronic pain signals and to control MOR antinociception. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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14 pages, 6065 KiB

Open AccessArticle

Phospho-Mimetic Mutation at Ser602 Inactivates Human TRPA1 Channel

by Kristyna Barvikova, Ivan Barvik, Viktor Sinica, Lucie Zimova and Viktorie Vlachova

Int. J. Mol. Sci. 2020, 21(21), 7995; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21217995 - 27 Oct 2020

Viewed by 2190

Abstract

The Transient Receptor Potential Ankyrin 1 (TRPA1) channel is an integrative molecular sensor for detecting environmental irritant compounds, endogenous proalgesic and inflammatory agents, pressure, and temperature. Different post-translational modifications participate in the discrimination of the essential functions of TRPA1 in its physiological environment, but the underlying structural bases are poorly understood. Here, we explored the role of the cytosolic N-terminal residue Ser602 located near a functionally important allosteric coupling domain as a potential target of phosphorylation. The phosphomimetic mutation S602D completely abrogated channel activation, whereas the phosphonull mutations S602G and S602N produced a fully functional channel. Using mutagenesis, electrophysiology, and molecular simulations, we investigated the possible structural impact of a modification (mutation or phosphorylation) of Ser602 and found that this residue represents an important regulatory site through which the intracellular signaling cascades may act to reversibly restrict or “dampen” the conformational space of the TRPA1 channel and promote its transitions to the closed state. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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17 pages, 3127 KiB

Open AccessArticle

Electrophile-Induced Conformational Switch of the Human TRPA1 Ion Channel Detected by Mass Spectrometry

by Lavanya Moparthi, Sven Kjellström, Per Kjellbom, Milos R. Filipovic, Peter M. Zygmunt and Urban Johanson

Int. J. Mol. Sci. 2020, 21(18), 6667; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21186667 - 11 Sep 2020

Cited by 5 | Viewed by 2313

Abstract

The human Transient Receptor Potential A1 (hTRPA1) ion channel, also known as the wasabi receptor, acts as a biosensor of various potentially harmful stimuli. It is activated by a wide range of chemicals, including the electrophilic compound N-methylmaleimide (NMM), but the mechanism of activation is not fully understood. Here, we used mass spectrometry to map and quantify the covalent labeling in hTRPA1 at three different concentrations of NMM. A functional truncated version of hTRPA1 (Δ1-688 hTRPA1), lacking the large N-terminal ankyrin repeat domain (ARD), was also assessed in the same way. In the full length hTRPA1, the labeling of different cysteines ranged from nil up to 95% already at the lowest concentration of NMM, suggesting large differences in reactivity of the thiols. Most important, the labeling of some cysteine residues increased while others decreased with the concentration of NMM, both in the full length and the truncated protein. These findings indicate a conformational switch of the proteins, possibly associated with activation or desensitization of the ion channel. In addition, several lysines in the transmembrane domain and the proximal N-terminal region were labeled by NMM, raising the possibility that lysines are also key targets for electrophilic activation of hTRPA1. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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Review

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17 pages, 1253 KiB

Open AccessReview

TRPA1 Expression and Pathophysiology in Immune Cells

by Robbe Naert, Alejandro López-Requena and Karel Talavera

Int. J. Mol. Sci. 2021, 22(21), 11460; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms222111460 - 24 Oct 2021

Cited by 25 | Viewed by 4688

Abstract

The non-selective cation channel TRPA1 is best known as a broadly-tuned sensor expressed in nociceptive neurons, where it plays key functions in chemo-, thermo-, and mechano-sensing. However, in this review we illustrate how this channel is expressed also in cells of the immune system. TRPA1 has been detected, mainly with biochemical techniques, in eosinophils, mast cells, macrophages, dendritic cells, T cells, and B cells, but not in neutrophils. Functional measurements, in contrast, remain very scarce. No studies have been reported in basophils and NK cells. TRPA1 in immune cells has been linked to arthritis (neutrophils), anaphylaxis and atopic dermatitis (mast cells), atherosclerosis, renal injury, cardiac hypertrophy and inflammatory bowel disease (macrophages), and colitis (T cells). The contribution of TRPA1 to immunity is dual: as detector of cell stress, tissue injury, and exogenous noxious stimuli it leads to defensive responses, but in conditions of aberrant regulation it contributes to the exacerbation of inflammatory conditions. Future studies should aim at characterizing the functional properties of TRPA1 in immune cells, an essential step in understanding its roles in inflammation and its potential as therapeutic target. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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14 pages, 973 KiB

Open AccessReview

Role of TRPA1 in Tissue Damage and Kidney Disease

by Chung-Kuan Wu, Ji-Fan Lin, Tzong-Shyuan Lee, Yu Ru Kou and Der-Cherng Tarng

Int. J. Mol. Sci. 2021, 22(7), 3415; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073415 - 26 Mar 2021

Cited by 10 | Viewed by 3987

Abstract

TRPA1, a nonselective cation channel, is expressed in sensory afferent that innervates peripheral targets. Neuronal TRPA1 can promote tissue repair, remove harmful stimuli and induce protective responses via the release of neuropeptides after the activation of the channel by chemical, exogenous, or endogenous irritants in the injured tissue. However, chronic inflammation after repeated noxious stimuli may result in the development of several diseases. In addition to sensory neurons, TRPA1, activated by inflammatory agents from some non-neuronal cells in the injured area or disease, might promote or protect disease progression. Therefore, TRPA1 works as a molecular sentinel of tissue damage or as an inflammation gatekeeper. Most kidney damage cases are associated with inflammation. In this review, we summarised the role of TRPA1 in neurogenic or non-neurogenic inflammation and in kidney disease, especially the non-neuronal TRPA1. In in vivo animal studies, TRPA1 prevented sepsis-induced or Ang-II-induced and ischemia-reperfusion renal injury by maintaining mitochondrial haemostasis or via the downregulation of macrophage-mediated inflammation, respectively. Renal tubular epithelial TRPA1 acts as an oxidative stress sensor to mediate hypoxia–reoxygenation injury in vitro and ischaemia–reperfusion-induced kidney injury in vivo through MAPKs/NF-kB signalling. Acute kidney injury (AKI) patients with high renal tubular TRPA1 expression had low complete renal function recovery. In renal disease, TPRA1 plays different roles in different cell types accordingly. These findings depict the important role of TRPA1 and warrant further investigation. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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15 pages, 1941 KiB

Open AccessReview

Interactions between Chemesthesis and Taste: Role of TRPA1 and TRPV1

by Mee-Ra Rhyu, Yiseul Kim and Vijay Lyall

Int. J. Mol. Sci. 2021, 22(7), 3360; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22073360 - 25 Mar 2021

Cited by 25 | Viewed by 5032

Abstract

In addition to the sense of taste and olfaction, chemesthesis, the sensation of irritation, pungency, cooling, warmth, or burning elicited by spices and herbs, plays a central role in food consumption. Many plant-derived molecules demonstrate their chemesthetic properties via the opening of transient receptor potential ankyrin 1 (TRPA1) and transient receptor potential vanilloid 1 (TRPV1) channels. TRPA1 and TRPV1 are structurally related thermosensitive cation channels and are often co-expressed in sensory nerve endings. TRPA1 and TRPV1 can also indirectly influence some, but not all, primary taste qualities via the release of substance P and calcitonin gene-related peptide (CGRP) from trigeminal neurons and their subsequent effects on CGRP receptor expressed in Type III taste receptor cells. Here, we will review the effect of some chemesthetic agonists of TRPA1 and TRPV1 and their influence on bitter, sour, and salt taste qualities. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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13 pages, 720 KiB

Open AccessReview

The Role of TRPA1 in Skin Physiology and Pathology

by Roberto Maglie, Daniel Souza Monteiro de Araujo, Emiliano Antiga, Pierangelo Geppetti, Romina Nassini and Francesco De Logu

Int. J. Mol. Sci. 2021, 22(6), 3065; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22063065 - 17 Mar 2021

Cited by 33 | Viewed by 6315

Abstract

The transient receptor potential ankyrin 1 (TRPA1), a member of the TRP superfamily of channels, acts as ‘polymodal cellular sensor’ on primary sensory neurons where it mediates the peripheral and central processing of pain, itch, and thermal sensation. However, the TRPA1 expression extends far beyond the sensory nerves. In recent years, much attention has been paid to its expression and function in non-neuronal cell types including skin cells, such as keratinocytes, melanocytes, mast cells, dendritic cells, and endothelial cells. TRPA1 seems critically involved in a series of physiological skin functions, including formation and maintenance of physico-chemical skin barriers, skin cells, and tissue growth and differentiation. TRPA1 appears to be implicated in mechanistic processes in various immunological inflammatory diseases and cancers of the skin, such as atopic and allergic contact dermatitis, psoriasis, bullous pemphigoid, cutaneous T-cell lymphoma, and melanoma. Here, we report recent findings on the implication of TRPA1 in skin physiology and pathophysiology. The potential use of TRPA1 antagonists in the treatment of inflammatory and immunological skin disorders will be also addressed. Full article

(This article belongs to the Special Issue TRPA1 Channel)

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