Membrane translocation of transient receptor potential ankyrin 1 induced by inflammatory cytokines in lung cancer cells

Takahashi, Kenji; Ohta, Toshio

doi:10.1016/j.bbrc.2017.06.082

Cited by 11 publications

(9 citation statements)

References 41 publications

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“…Activation of TRPA1 potentially TALAVERA ET AL. 774 Physiol Rev • VOL 100 • APRIL 2020 • www.prv.org induces the release of chemokines in inflamed airways (561), and conversely, inflammatory cytokines can enhance TRPA1 translocation to the membrane (791). An in vitro model of respiratory virus infection of human bronchial epithelial cells showed that cytokines released in the supernatants lead to increased TRPA1 expression (631).…”

Section: G Trpa1 In Respiratory Diseasementioning

confidence: 99%

Mammalian Transient Receptor Potential TRPA1 Channels: From Structure to Disease

Talavera

Startek

Alvarez‐Collazo

et al. 2020

Physiological Reviews

288

274

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The transient receptor potential ankyrin (TRPA) channels are Ca2+-permeable nonselective cation channels remarkably conserved through the animal kingdom. Mammals have only one member, TRPA1, which is widely expressed in sensory neurons and in non-neuronal cells (such as epithelial cells and hair cells). TRPA1 owes its name to the presence of 14 ankyrin repeats located in the NH2 terminus of the channel, an unusual structural feature that may be relevant to its interactions with intracellular components. TRPA1 is primarily involved in the detection of an extremely wide variety of exogenous stimuli that may produce cellular damage. This includes a plethora of electrophilic compounds that interact with nucleophilic amino acid residues in the channel and many other chemically unrelated compounds whose only common feature seems to be their ability to partition in the plasma membrane. TRPA1 has been reported to be activated by cold, heat, and mechanical stimuli, and its function is modulated by multiple factors, including Ca2+, trace metals, pH, and reactive oxygen, nitrogen, and carbonyl species. TRPA1 is involved in acute and chronic pain as well as inflammation, plays key roles in the pathophysiology of nearly all organ systems, and is an attractive target for the treatment of related diseases. Here we review the current knowledge about the mammalian TRPA1 channel, linking its unique structure, widely tuned sensory properties, and complex regulation to its roles in multiple pathophysiological conditions.

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Section: G Trpa1 In Respiratory Diseasementioning

confidence: 99%

Mammalian Transient Receptor Potential TRPA1 Channels: From Structure to Disease

Talavera

Startek

Alvarez‐Collazo

et al. 2020

Physiological Reviews

288

274

View full text Add to dashboard Cite

show abstract

“…Under certain pathological conditions such as tissue injury or inflammation, TRPA1 may undergo a wide range of posttranslational modifications that lead to various levels of functional modulation. Ca 2+ influx through TRPA1 can release mediators such as calcitonin gene-related peptide, substance P, neurokinin A and bradykinin, which modulate the channel via G-protein-coupled receptor signaling cascades (Andrade et al, 2012;Petho and Reeh, 2012;Voolstra and Huber, 2014;Kadkova et al, 2017) and/or promote the recruitment of the channels to the cell surface (Schmidt et al, 2009;Takahashi and Ohta, 2017).…”

Section: Introductionmentioning

confidence: 99%

Proximal C-Terminus Serves as a Signaling Hub for TRPA1 Channel Regulation via Its Interacting Molecules and Supramolecular Complexes

et al. 2020

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Our understanding of the general principles of the polymodal regulation of transient receptor potential (TRP) ion channels has grown impressively in recent years as a result of intense efforts in protein structure determination by cryo-electron microscopy. In particular, the high-resolution structures of various TRP channels captured in different conformations, a number of them determined in a membrane mimetic environment, have yielded valuable insights into their architecture, gating properties and the sites of their interactions with annular and regulatory lipids. The correct repertoire of these channels is, however, organized by supramolecular complexes that involve the localization of signaling proteins to sites of action, ensuring the specificity and speed of signal transduction events. As such, TRP ankyrin 1 (TRPA1), a major player involved in various pain conditions, localizes into cholesterol-rich sensory membrane microdomains, physically interacts with calmodulin, associates with the scaffolding A-kinase anchoring protein (AKAP) and forms functional complexes with the related TRPV1 channel. This perspective will contextualize the recent biochemical and functional studies with emerging structural data with the aim of enabling a more thorough interpretation of the results, which may ultimately help to understand the roles of TRPA1 under various physiological and pathophysiological pain conditions. We demonstrate that an alteration to the putative lipid-binding site containing a residue polymorphism associated with human asthma affects the cold sensitivity of TRPA1. Moreover, we present evidence that TRPA1 can interact with AKAP to prime the channel for opening. The structural bases underlying these interactions remain unclear and are definitely worth the attention of future studies.

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“…Thus, it is well known that these transcription factors play a pivotal role in inflammatory diseases and cancer. Furthermore, it has been reported that the expression and membrane translocation of TRPA1 was induced by inflammatory cytokines in A549 cells [35,36]. Acrolein naturally induces an inflammatory response [37].…”

Section: Discussionmentioning

confidence: 99%

Transient Receptor Potential Ankyrin 1 (TRPA1) Channel Mediates Acrolein Cytotoxicity in Human Lung Cancer Cells

Sakamoto

Terui

Igarashi

et al. 2023

IJMS

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Transient receptor potential ankyrin 1 (TRPA1) is a nonselective ion channel implicated in thermosensation and inflammatory pain. It has been reported that expression of the TRPA1 channel is induced by cigarette smoke extract. Acrolein found in cigarette smoke is highly toxic and known as an agonist of the TRPA1 channel. However, the role of TRPA1 in the cytotoxicity of acrolein remains unclear. Here, we investigated whether the TRPA1 channel is involved in the cytotoxicity of acrolein in human lung cancer A549 cells. The IC50 of acrolein in A549 cells was 25 μM, and acrolein toxicity increased in a concentration- and time-dependent manner. When the effect of acrolein on TRPA1 expression was examined, the expression of TRPA1 in A549 cells was increased by treatment with 50 μM acrolein for 24 h or 500 μM acrolein for 30 min. AP-1, a transcription factor, was activated in the cells treated with 50 μM acrolein for 24 h, while induction of NF-κB and HIF-1α was observed in the cells treated with 500 μM acrolein for 30 min. These results suggest that acrolein induces TRPA1 expression by activating these transcription factors. Overexpression of TRPA1 in A549 cells increased acrolein sensitivity and the level of protein-conjugated acrolein (PC-Acro), while knockdown of TRPA1 in A549 cells or treatment with a TRPA1 antagonist caused tolerance to acrolein. These findings suggest that acrolein induces the TRPA1 channel and that an increase in TRPA1 expression promotes the cytotoxicity of acrolein.

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Membrane translocation of transient receptor potential ankyrin 1 induced by inflammatory cytokines in lung cancer cells

Cited by 11 publications

References 41 publications

Mammalian Transient Receptor Potential TRPA1 Channels: From Structure to Disease

Mammalian Transient Receptor Potential TRPA1 Channels: From Structure to Disease

Proximal C-Terminus Serves as a Signaling Hub for TRPA1 Channel Regulation via Its Interacting Molecules and Supramolecular Complexes

Transient Receptor Potential Ankyrin 1 (TRPA1) Channel Mediates Acrolein Cytotoxicity in Human Lung Cancer Cells

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