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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.
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Salts with Acidic Ions
Salts are ionic compounds composed of cations and anions, either of which may be capable of undergoing an acid or base ionization reaction with water. Aqueous salt solutions, therefore, may be acidic, basic, or neutral, depending on the relative acid-base strengths of the salt’s constituent ions. For example, dissolving the ammonium chloride in water results in its dissociation, as described by the equation:
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Non-gated Ion Channels01:24

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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.
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Mechanically-gated Ion Channels01:12

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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...
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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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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.
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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Zinc Permeation Through Acid-Sensing Ion Channels.

Xiang-Ping Chu1, Koichi Inoue2,3, Zhi-Gang Xiong2

  • 1Department of Biomedical Sciences, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.

Cells
|January 28, 2026
PubMed
Summary
This summary is machine-generated.

Acid-sensing ion channels (ASICs) are involved in brain injury. This study shows ASIC2a channels facilitate zinc influx, potentially contributing to neurotoxicity.

Keywords:
ASICacidosisneurotoxicitystrokezinc

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Area of Science:

  • Neuroscience
  • Ion Channel Physiology
  • Cellular Signaling

Background:

  • Acid-sensing ion channels (ASICs) are crucial in ischemic brain injury.
  • ASIC1a activation increases calcium influx, contributing to neuronal damage.
  • Mechanisms of ASIC-mediated neurotoxicity, especially involving other ions, are not fully understood.

Purpose of the Study:

  • To investigate the role of ASIC2a-containing channels in ion flux and neurotoxicity.
  • To determine if ASIC2a channels mediate zinc influx.
  • To explore the contribution of zinc to acid-mediated neurotoxicity.

Main Methods:

  • Utilized cultured mouse cortical neurons and Chinese Hamster Ovary (CHO) cells expressing ASIC subunits.
  • Measured ASIC currents using electrophysiology under varying pH and extracellular cation conditions (Na+, Zn2+).
  • Employed fluorescence imaging to visualize zinc influx and assessed neurotoxicity in the presence of zinc and acidic conditions.

Main Results:

  • ASIC currents insensitive to PcTx1 were potentiated by extracellular zinc.
  • ASIC2a-containing channels (homomeric ASIC2a and heteromeric ASIC1a/2a) facilitated zinc influx upon acid stimulation, unlike homomeric ASIC1a.
  • Zinc exacerbated acid-mediated neurotoxicity in cells expressing ASIC2a-containing channels.

Conclusions:

  • ASIC2a-containing channels represent a novel pathway for zinc entry into neurons.
  • Acid-induced activation of ASIC2a channels can lead to zinc influx.
  • This zinc influx mediated by ASIC2a channels may contribute to neurotoxicity.