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Related Concept Videos

Voltage-gated Ion Channels01:26

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...
Voltage-gated Ion Channels01:26

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...
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...
Mechanically-gated Ion Channels01:12

Mechanically-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...
Mechanically-gated Ion Channels01:12

Mechanically-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...
Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...

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Updated: May 9, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
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A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

Published on: September 26, 2025

Scorpion venom components that affect ion-channels function.

V Quintero-Hernández1, J M Jiménez-Vargas, G B Gurrola

  • 1Department of Molecular Medicine and Bioprocesses, Instituto de Biotecnologia, Universidad Nacional Autonoma de Mexico (UNAM), Avenida Universidad 2001, Colonia Chamilpa, Apartado Postal 510-3, Cuernavaca 62210, Morelos, Mexico.

Toxicon : Official Journal of the International Society on Toxinology
|July 30, 2013
PubMed
Summary
This summary is machine-generated.

Venomous peptides targeting ion channels like sodium (Na+), potassium (K+), and calcium (Ca++) are crucial for human envenomation. Understanding these venom components aids in developing specific anti-venoms.

Keywords:
BiodiversityFunctional effectIon-channelScorpion toxinStructural features

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Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses

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Electrophysiology of Scorpion Peg Sensilla
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Electrophysiology of Scorpion Peg Sensilla

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Last Updated: May 9, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
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Electrophysiology of Scorpion Peg Sensilla
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Electrophysiology of Scorpion Peg Sensilla

Published on: April 13, 2011

Area of Science:

  • Biochemistry
  • Pharmacology
  • Toxicology

Background:

  • Venoms contain diverse peptides that interact with ion channels.
  • These venom components are significant causes of human intoxication and require medical intervention, often necessitating anti-venom therapy.
  • Current knowledge comprises approximately 1,500 identified venom peptides, with an estimated biodiversity of 300,000.

Purpose of the Study:

  • To review venom components affecting ion-channel function.
  • To emphasize peptides targeting sodium (Na+), potassium (K+), and calcium (Ca++) channels in excitable cells.
  • To discuss the structural characteristics and mechanisms of action of these peptides.

Main Methods:

  • Review of scientific literature on venom component isolation and gene cloning.
  • Analysis of deposited amino acid sequences in databanks.
  • Examination of published structural and mechanistic studies.

Main Results:

  • Na(+)-channel peptides typically modify channel gating kinetics.
  • K(+)-channel peptides primarily act as pore blockers.
  • Ryanodine Ca(++)-channel peptides can induce sub-conducting states and may internalize into muscle cells.

Conclusions:

  • Venom peptides exhibit diverse mechanisms for modulating ion-channel function.
  • Understanding these interactions is vital for clinical toxicology and the development of targeted anti-venoms.
  • Further research into venom biodiversity can reveal novel ion-channel modulators.