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Related Concept Videos

Antihypertensive Drugs: Action of Calcium Channel Blockers01:18

Antihypertensive Drugs: Action of Calcium Channel Blockers

Calcium ions are essential to contract smooth muscle cells in blood vessels. They enter these cells through voltage-dependent calcium channels, specifically L-type calcium channels in the cell membrane. These L-type calcium channels are integral to the excitation-contraction coupling process in smooth muscle. When a stimulus is received by smooth muscle cells, their membrane depolarizes. This alteration in membrane potential instigates the opening of L-type calcium channels. As a result,...
Calmodulin-dependent Signaling01:16

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,...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

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...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Antiarrhythmic Drugs: Class IV Agents as Calcium Channel Blockers01:20

Antiarrhythmic Drugs: Class IV Agents as Calcium Channel Blockers

Class IV antiarrhythmic drugs, such as verapamil and diltiazem, block calcium channels. They primarily affect the heart, slowing the conduction in calcium-dependent tissues like the SA and AV nodes. These drugs manage reentrant supraventricular tachycardia (SVT) and reduce ventricular rate in atrial flutter/fibrillation.
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Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...

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Related Experiment Video

Updated: May 28, 2026

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay
11:49

Characterization of G Protein-coupled Receptors by a Fluorescence-based Calcium Mobilization Assay

Published on: July 28, 2014

Characterization of calcium channel binding.

W Zheng1

  • 1Merck and Company, North Wales, Pennsylvania, USA.

Current Protocols in Pharmacology
|October 1, 2011
PubMed
Summary

This study details radioligand binding assays for voltage-dependent calcium channels using [³H]PN200-100 and [¹²⁵I](conotoxin MVIIA). These methods quantify calcium channel expression and compound affinity in tissues like the heart, muscles, and brain.

Area of Science:

  • Pharmacology
  • Neuroscience
  • Biochemistry

Background:

  • Voltage-dependent calcium channels are crucial proteins found in various tissues, including the heart, muscles, and brain.
  • Radioligand binding assays, particularly saturation binding, are standard techniques for assessing calcium channel expression levels.
  • Compound competition binding assays are widely used for screening and determining the affinity of potential drug compounds for these channels.

Purpose of the Study:

  • To provide detailed experimental protocols for two specific radioligand binding assays.
  • To enable the characterization of voltage-dependent calcium channel expression.
  • To facilitate the determination of compound affinity for calcium channels.

Main Methods:

  • Utilizing saturation binding assays with radioligands to quantify calcium channel expression.

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  • Employing compound competition binding assays to assess the affinity of unlabeled compounds.
  • Detailed methods are provided for assays using [³H]PN200-100 and [¹²⁵I](conotoxin MVIIA).

    • Main Results:

    • Established protocols for radioligand binding assays targeting voltage-dependent calcium channels.
    • Demonstrated methods for characterizing channel protein expression levels.
    • Provided a framework for screening compound affinities.

    Conclusions:

    • The described radioligand binding assays are valuable tools for studying voltage-dependent calcium channels.
    • These methods support research in pharmacology and neuroscience by enabling precise quantification of channel activity and compound interactions.
    • The protocols are applicable to various tissue types where calcium channels are expressed.