Modulation of CaV2.3 calcium channel currents by eugenol
1Department of Physiology, School of Dentistry, Seoul National University, 28-2 Yeongeon-Dong, Chongno-Ku, Seoul, 110-749, Korea.
Journal of Dental Research
|January 26, 2008
Summary
Eugenol, a dental analgesic, inhibits Ca(V)2.3 calcium channels, distinct from capsaicin
Area of Science:
- Pharmacology
- Neuroscience
- Molecular Biology
Background:
- Eugenol is a common dental analgesic.
- Its analgesic effects are partly due to inhibition of Ca(V)2.2 and sodium channels.
- The role of Ca(V)2.3 channels in eugenol's action is unknown.
Purpose of the Study:
- To investigate if eugenol modulates Ca(V)2.3 calcium channels.
- To determine the mechanism of eugenol's action on Ca(V)2.3 channels.
- To compare eugenol's mechanism with that of capsaicin.
Main Methods:
- Whole-cell patch-clamp technique.
- Heterologous expression system using E52 cell line stably expressing human Ca(V)2.3 channels.
- Comparison between cells with and without TRPV1 expression.
Main Results:
- Eugenol inhibited Ca(V)2.3 calcium currents.
- TRPV1 expression did not affect the extent of inhibition by eugenol.
- Eugenol's inhibition of Ca(V)2.3 channels is independent of TRPV1, unlike capsaicin.
Conclusions:
- Eugenol modulates Ca(V)2.3 calcium channels through a mechanism distinct from capsaicin.
- Eugenol's inhibition of Ca(V)2.3 channels may contribute to its analgesic properties.
Related Concept Videos
Ligand-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...
Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Voltage-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...
Voltage-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...
Antiepileptic Drugs: Modulators of Neurotransmitter Release Mediated by SV2A Protein
Antiepileptic drugs, such as levetiracetam (Keppra) and brivaracetam (Briviact), have emerged as crucial tools in managing epilepsy. These medications exert their therapeutic effects by targeting the synaptic vesicle protein SV2A, a transmembrane glycoprotein primarily found in the brain.
SV2A is a transmembrane glycoprotein located predominantly in the brain, modulating the release of neurotransmitters for neuronal communication. Both levetiracetam and brivaracetam exhibit a high affinity for...
SV2A is a transmembrane glycoprotein located predominantly in the brain, modulating the release of neurotransmitters for neuronal communication. Both levetiracetam and brivaracetam exhibit a high affinity for...


