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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Cationic control of Panx1 channel function.

Junjie Wang1, David George Jackson1, Gerhard Dahl1

  • 1Department of Physiology and Biophysics, University of Miami School of Medicine , Miami, Florida.

American Journal of Physiology. Cell Physiology
|May 3, 2018
PubMed
Summary
This summary is machine-generated.

Pannexin1 (Panx1) channels exhibit distinct conformations. While voltage-gated Panx1 channels are unaffected by multivalent cations, those activated by physiological stimuli are inhibited by di- and trivalent cations.

Keywords:
calciumgadoliniumpannexinpotassiumvoltage

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Area of Science:

  • Molecular biology
  • Cellular physiology
  • Ion channel research

Background:

  • Pannexin1 (Panx1) is a channel protein structurally related to gap junction proteins.
  • Panx1 channels function in the non-junctional membrane and exhibit distinct open states.
  • These states differ in conductance, ion selectivity, and activation mechanisms.

Purpose of the Study:

  • To investigate the pharmacological differences between the two Panx1 channel conformations.
  • To determine the effects of divalent and trivalent cations on voltage-gated versus physiologically activated Panx1 channels.

Main Methods:

  • Electrophysiological recordings of Panx1 channel activity.
  • Application of various stimuli (voltage, extracellular K+, osmotic stress, low oxygen) to activate Panx1.
  • Dose-dependent application of mono-, di-, and trivalent cations (Ca2+, Zn2+, Ba2+, Gd3+).

Main Results:

  • Voltage-gated Panx1 channels (small conductance, chloride-selective) were not affected by Ca2+, Zn2+, Ba2+, or Gd3+.
  • Panx1 channels activated by physiological stimuli (large conductance, non-selective) were inhibited by di- and trivalent cations in a dose-dependent manner.
  • Monovalent cations activated Panx1 to the large conformation, while di- and trivalent cations inhibited this conformation.

Conclusions:

  • Panx1 channels display distinct pharmacological profiles depending on their open conformation.
  • The large, physiologically activated Panx1 channel conformation is sensitive to inhibition by multivalent cations.
  • These findings highlight the differential regulation of Panx1 channel function.