ArticleBiophysical journal2003
Thermodynamics of heat activation of single capsaicin ion channels VR1.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Thermodynamic coupling between cold and heat activations of TRPV2.Scientific reports · 2026Article
- Mechanism of lipid-dependent cold sensitivity in a model ion channel.Nature communications · 2026Article
- Review
- Structural basis of the inhibition of TRPV1 by analgesic sesquiterpenes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Thermo-TRP regulation by endogenous factors and its physiological function at core body temperature.Physiological reports · 2025Review
- Residues of TRPM8 at the Lipid-Water-Interface have Coevolved with Cholesterol Interaction and are Relevant for Diverse Health Disorders.The Journal of membrane biology · 2024Article
- TRPV2: a universal regulator in cellular physiology with a yet poorly defined thermosensitivity.The journal of physiological sciences : JPS · 2024Review
- Structural basis of TRPV1 inhibition by SAF312 and cholesterol.Nature communications · 2024Article
- Article
- Temperature gating in thermoTRPs may depend on temperature-dependent heat capacity differences.Temperature (Austin, Tex.) · 2024Article
- Extracting thermodynamic properties from van 't Hoff plots with emphasis on temperature-sensing ion channels.Temperature (Austin, Tex.) · 2024Article
- Temperature sensitive contact modes allosterically gate TRPV3.PLoS computational biology · 2023Article
- A suicidal mechanism for the exquisite temperature sensitivity of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Implications of a temperature-dependent heat capacity for temperature-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A molecular perspective on identifying TRPV1 thermosensitive regions and disentangling polymodal activation.Temperature (Austin, Tex.) · 2023Review
- A journey from molecule to physiology andFrontiers in pharmacology · 2023Review
- The triple function of the capsaicin-sensitive sensory neurons: In memoriam János Szolcsányi.Temperature (Austin, Tex.) · 2023Review
- Effect of Lipid Raft Disruptors on Cell Membrane Fluidity Studied by Fluorescence Spectroscopy.International journal of molecular sciences · 2022Article
- The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain.Nature communications · 2022Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
Abstract
Temperature affects functions of all ion channels, but few of them can be gated directly. The vanilloid receptor VR1 provides one exception. As a pain receptor, it is activated by heat >42 degrees C in addition to other noxious stimuli, e.g. acids and vanilloids. Although it is understood how ligand- and voltage-gated channels might detect their stimuli, little is known on how heat could be sensed and activate a channel. In this study, we characterized the heat-induced single-channel activity of VR1, in an attempt to localize the temperature-dependent components involved in the activation of the channel. At <42 degrees C, openings were few and brief. Raising the ambient temperature rapidly increased the frequency of openings. Despite the large temperature coefficient of the apparent activity (Q(10) approximately 27), the unitary current, the open dwell-times, and the intraburst closures were all only weakly temperature dependent (Q(10) < 2). Instead, heat had a localized effect on the reduction of long closures between bursts (Q(10) approximately 7) and the elongation of burst durations (Q(10) approximately 32). Both membrane lipids and solution ionic strength affected the temperature threshold of the activation, but neither diminished the response. The thermodynamic basis of heat activation is discussed, to elucidate what makes a thermal-sensitive channel unique.
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