Related Experiment Video
Updated: May 6, 2026

Identification of Specific Sensory Neuron Populations for Study of Expressed Ion Channels
Published on: December 24, 2013
A novel acid-sensitive K+ channel in rat dorsal root ganglia neurons
Jun-Ho La1, Dawon Kang, Jae-Yong Park
1Medical Research Center for Neural Dysfunction, Department of Physiology, College of Medicine and Institute of Health Sciences, Gyeongsang National University, 90 Chilam-dong, Jinju, Gyeongnam, South Korea.
Abstract:
Recent studies have suggested that acid-sensitive background K+ channels such as TASK-1 and TASK-3, members of two-pore domain K+ (K2P) channel family, express and contribute to extracellular acidification-induced responses in dorsal root ganglia (DRG) neurons. However, it has remained to address whether other acid-sensitive background K+ channels are functionally expressed in DRG neurons. Here we characterized biophysical and pharmacological properties of a novel acid-sensitive background K+ channel in DRG neurons isolated from neonatal rats. We recorded an 80-pS K+ channel with a weak inward rectification current-voltage relationship in cell-attached patches in 150mM KCl bath solution. The 80-pS K+ channel was inhibited by extracellular low pH (pHo 6.3). Interestingly, the channel was similar to TASK-2 cloned from mouse and rat in biophysical and pharmacological properties. However, extracellular alkaline condition which activates TASK-2 channel, failed to activate the 80-pS K+ channel. Lidocaine and quinine more inhibited the channel activity of 80-pS K+ channel than that of TASK-2 channel. Our results suggest that the acid-sensitive 80-pS K+ channels may regulate resting membrane potential and may play a critical role in various processes such as cell metabolism, pH, and pain sensation in DRG neurons.
More Related Videos
Related Concept Videos
Non-gated Ion Channels
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
Voltage-gated Ion Channels
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...
Mechanically-gated Ion Channels
Ligand-Gated Ion Channel Receptor: Gating Mechanism

