Putative binding sites for arachidonic acid on the human cardiac Kv 1.5 channel.

ABSTRACT:

Background and purpose

In human heart, the Kv 1.5 channel contributes to repolarization of atrial action potentials. This study examined the electrophysiological and molecular mechanisms underlying arachidonic acid (AA)-induced inhibition of the human Kv 1.5 (hKv 1.5) channel.

Experimental approach

Site-directed mutagenesis was conducted to mutate amino acids that reside within the pore domain of the hKv 1.5 channel. Whole-cell patch-clamp method was used to record membrane currents through wild type and mutant hKv 1.5 channels heterologously expressed in CHO cells. Computer docking simulation was conducted to predict the putative binding site(s) of AA in an open-state model of the Kv 1.5 channel.

Key results

The hKv 1.5 current was minimally affected at the onset of

SUBMITTER: Bai JY 

PROVIDER: S-EPMC5341216 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature