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      Oxidation sensitizes TRPV2 to chemical and heat stimuli, but not mechanical stimulation

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          Abstract

          The transient receptor potential vanilloid 2 (TRPV2) ion channel is activated by a chemical ligand (2-aminoethoxydiphenyl borate; 2-APB), noxious heat and mechanical stimulation. In a heterologous mammalian cell expression system, the oxidant chloramine T (ChT) sensitizes TRPV2 activation in response to 2-APB and heat by oxidation of methionine residues at positions 528 and 607 in rat TRPV2. Here, we used a Xenopus oocyte expression system to determine whether ChT-mediated oxidation can also sensitize TRPV2 to mechanical stimulation. In this system, we confirmed that ChT sensitized TRPV2 activation in response to 2-APB and heat, but we detected no sensitization to mechanical stimulation. This result suggests that the activation mechanism of TRPV2 by a chemical ligand and heat differs from that for mechanical stimulation. Further, we demonstrated that two-electrode voltage clamp recording in the Xenopus oocyte expression system is an excellent format for high throughput analysis of oxidization of redox-sensitive TRP channels.

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          Most cited references35

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          The capsaicin receptor: a heat-activated ion channel in the pain pathway.

          Capsaicin, the main pungent ingredient in 'hot' chilli peppers, elicits a sensation of burning pain by selectively activating sensory neurons that convey information about noxious stimuli to the central nervous system. We have used an expression cloning strategy based on calcium influx to isolate a functional cDNA encoding a capsaicin receptor from sensory neurons. This receptor is a non-selective cation channel that is structurally related to members of the TRP family of ion channels. The cloned capsaicin receptor is also activated by increases in temperature in the noxious range, suggesting that it functions as a transducer of painful thermal stimuli in vivo.
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            TRP channels.

            The TRP (Transient Receptor Potential) superfamily of cation channels is remarkable in that it displays greater diversity in activation mechanisms and selectivities than any other group of ion channels. The domain organizations of some TRP proteins are also unusual, as they consist of linked channel and enzyme domains. A unifying theme in this group is that TRP proteins play critical roles in sensory physiology, which include contributions to vision, taste, olfaction, hearing, touch, and thermo- and osmosensation. In addition, TRP channels enable individual cells to sense changes in their local environment. Many TRP channels are activated by a variety of different stimuli and function as signal integrators. The TRP superfamily is divided into seven subfamilies: the five group 1 TRPs (TRPC, TRPV, TRPM, TRPN, and TRPA) and two group 2 subfamilies (TRPP and TRPML). TRP channels are important for human health as mutations in at least four TRP channels underlie disease.
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              TRP channels as cellular sensors.

              TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.
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                Author and article information

                Contributors
                Journal
                Biochem Biophys Rep
                Biochem Biophys Rep
                Biochemistry and Biophysics Reports
                Elsevier
                2405-5808
                18 November 2021
                December 2021
                18 November 2021
                : 28
                : 101173
                Affiliations
                [a ]Department of Molecular and Cellular Neurobiology, Gunma University Graduate School of Medicine, Maebashi, 371-8511, Japan
                [b ]Molecular Physiology & Biophysics, Faculty of Medicine, Kagawa University, Kagawa, 761-0793, Japan
                [c ]Laboratory of Neurochemistry, Graduate School of Human Health Science, University of Nagasaki, 1-1-1 Manabino, Nagasaki, 851-2195, Japan
                Author notes
                []Corresponding author. Laboratory of Neurochemistry, Graduate School of Human Health Science, University of Nagasaki, 1-1-1 Manabino, Nagayo, Nagasaki, 851-2195, Japan. kshibasaki@ 123456sun.ac.jp
                [1]

                Current Affiliation: Cellular & Molecular Physiology, Yale University School of Medicine, New Heaven, CT, 06520-8026.

                Article
                S2405-5808(21)00267-3 101173
                10.1016/j.bbrep.2021.101173
                8605382
                84ef6fee-a809-403b-9264-b633ed889b65
                © 2021 The Authors

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                : 13 October 2021
                : 11 November 2021
                : 13 November 2021
                Categories
                Research Article

                2-apb, 2-aminoethoxydiphenyl borate,cht, chloramine t,lpc, lysophosphatidylcholine,ros, reactive oxygen species,trp, transient receptor potential,trpv, transient receptor potential vanilloid,trp channel,trpv2,oxidation,heat,mechanical stimulus,two-electrode voltage clamp method

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