Related Experiment Video
Updated: Aug 9, 2026
12:09
Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
Published on: December 31, 2013
Reducing and oxidizing agents sensitize heat-activated vanilloid receptor (TRPV1) current
Klara Susankova1, Karolina Tousova, Ladislav Vyklicky
1Department of Cellular Neurophysiology, Institute of Physiology AS CR, Vídenská 1083, 142 20 Prague 4, Czech Republic.
Molecular Pharmacology
|April 15, 2006
Summary
Both reducing and oxidizing agents enhance heat-induced activation of the transient receptor potential vanilloid receptor-1 (TRPV1) channel. This suggests an optimal redox state is crucial for TRPV1 channel function.
Area of Science:
- Neuroscience
- Molecular Biology
- Biophysics
Background:
- The transient receptor potential vanilloid receptor-1 (TRPV1) channel is activated by heat.
- Previous studies showed dithiothreitol (DTT), a reducing agent, increases TRPV1 thermal activity.
Purpose of the Study:
- To investigate the effects of oxidizing agents on TRPV1 heat-induced activation.
- To identify the specific sites and mechanisms of redox modulation on TRPV1.
Main Methods:
- Examined heat-evoked whole-cell membrane currents in TRPV1-transfected cells.
- Utilized various sulfhydryl modifiers (oxidizing and reducing agents) and site-directed mutagenesis.
Main Results:
- Membrane-permeable oxidizing agents (diamide, chloramine-T, copper-o-complex) enhanced heat-induced TRPV1 activation.
- Extracellular glutathione mimicked DTT's potentiation of heat- and voltage-induced currents.
- Cys621 was identified as the extracellular site for redox modulation by reducing agents.
Conclusions:
- Redox-active substances directly modulate TRPV1 channel activity at extracellular and cytoplasmic sites.
- Both reduced and oxidized states can increase TRPV1 responsiveness to thermal stimuli.
- An optimal redox state is essential for proper TRPV1 channel function.
Related Concept Videos
01:43Thermosensation
Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
01:12Mechanically-gated Ion Channels
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
01:26Voltage-gated Ion Channels
Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
01:26Voltage-gated Ion Channels
Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
01:30Ligand-Gated Ion Channel Receptor: Gating Mechanism
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
01:24Non-gated Ion Channels
Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.