Thermodynamics of Heat Activation of Single Capsaicin Ion Channels VR1

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°C in addition to other noxious stimuli, e.g. acids and vanilloids. Although it is understood how ligand- and...

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Bibliographic Details
Published in:Biophysical journal 2003-11, Vol.85 (5), p.2988-3006
Main Authors: Liu, Beiying, Hui, Kwokyin, Qin, Feng
Format: Article
Language:English
Subjects:
Animals
Cell Line
Channels, Receptors, and Transporters
Cholesterol - metabolism
Computer Simulation
Heat
Hot Temperature
Humans
Ion Channel Gating - physiology
Ion Channel Gating - radiation effects
Ions
Kidney - embryology
Kidney - physiology
Kidney - radiation effects
Membrane Potentials - physiology
Membrane Potentials - radiation effects
Models, Biological
Oocytes - physiology
Oocytes - radiation effects
Rats
Receptors, Drug - drug effects
Receptors, Drug - physiology
Species Specificity
Temperature
Thermodynamics
Xenopus laevis
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Summary: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°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
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(03)74719-5