The discovery and characterization of a proton-gated sodium current in rat retinal ganglion cells

J Neurosci. 2004 Feb 4;24(5):1013-22. doi: 10.1523/JNEUROSCI.3191-03.2004.

Abstract

The conduction of acid-evoked currents in central and sensory neurons is now primarily attributed to a family of proteins called acid-sensing ion channels (ASICs). In peripheral neurons, their physiological function has been linked to nociception, mechanoreception, and taste transduction; however, their role in the CNS remains unclear. This study describes the discovery of a proton-gated current in rat retinal ganglion cells termed I(Na(H+)), which also appears to be mediated by ASICs. RT-PCR confirmed the presence of ASIC mRNA (subunits la, 2a, 2b, 3, and 4) in the rat retina. Electrophysiological investigation showed that all retinal ganglion cells respond to rapid extracellular acidification with the activation of a transient Na+ current, the size of which increases with increasing acidification between pH 6.5 and pH 3.0. I(Na(H+)) desensitizes completely in the continued presence of acid, its current-voltage relationship is linear and its reversal potential shifts with E(Na). I(Na(H+)) is reversibly inhibited by amiloride (IC(50), 188 microm) but is resistant to block by TTX (0.5 microm), Cd2+ (100 microm), procaine (10 mm), and is not activated by capsaicin (0.5 microm). I(Na(H+)) is not potentiated by Zn2+ (300 microm) or Phe-Met-Arg-Phe-amide (50microm) but is inhibited by neuropeptide-FF (50microm). Acute application of pH 6.5 to retinal ganglion cells causes sustained depolarization and repetitive firing similar to the trains of action potentials normally associated with current injection into these cells. The presence of a proton-gated current in the neural retina suggests that ASICs may have a more diverse role in the CNS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Sensing Ion Channels
  • Acids / pharmacology
  • Action Potentials / drug effects
  • Action Potentials / physiology
  • Amiloride / pharmacology
  • Animals
  • Cells, Cultured
  • Extracellular Fluid / metabolism
  • Female
  • Hydrogen-Ion Concentration / drug effects
  • Ion Channel Gating / drug effects
  • Ion Channel Gating / physiology*
  • Male
  • Membrane Proteins / drug effects
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Nerve Tissue Proteins / drug effects
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Patch-Clamp Techniques
  • Protein Subunits / drug effects
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Protons
  • RNA, Messenger / metabolism
  • Rats
  • Rats, Inbred Strains
  • Retinal Ganglion Cells / cytology
  • Retinal Ganglion Cells / drug effects
  • Retinal Ganglion Cells / metabolism*
  • Sodium / metabolism*
  • Sodium Channel Blockers / pharmacology
  • Sodium Channels / drug effects
  • Sodium Channels / genetics
  • Sodium Channels / metabolism*
  • Zinc / pharmacology

Substances

  • Acid Sensing Ion Channels
  • Acids
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Protein Subunits
  • Protons
  • RNA, Messenger
  • Sodium Channel Blockers
  • Sodium Channels
  • Amiloride
  • Sodium
  • Zinc