Co-expression of KCNE2 and KChlP2c modulates the electrophysiologi- cal properties of Kv4.2 current in COS-7 cells

Aim: Several β-subunits have been suggested to modulate the electrophysiological properties of the transient outward current (Ito) in cardiac myocytes, including the obligatory β-subunit K^+-channel interacting protein (KChIP2) and KCNE2. However, neither KChIP2 nor KCNE2 modulation of Kv4.x (x=2 an...

Full description

Saved in:
Bibliographic Details
Published inActa pharmacologica Sinica Vol. 29; no. 6; pp. 653 - 660
Main Author Wen-juan LIU Hai-tang WANG Wei-wei Chen Jian-xin DENG Yong JIANG Jie LIU
Format Journal Article
LanguageEnglish
Published 2008
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Aim: Several β-subunits have been suggested to modulate the electrophysiological properties of the transient outward current (Ito) in cardiac myocytes, including the obligatory β-subunit K^+-channel interacting protein (KChIP2) and KCNE2. However, neither KChIP2 nor KCNE2 modulation of Kv4.x (x=2 and/or 3) can fully recapitulate the electrophysiological properties of nativeIto. The present study is to investigate howIto current is modulated when both KChIP2 and KCNE2 are coexpressed. Methods: Kv4.2, KChIP2c, and KCNE2 cDNA were simultaneously transfected into COS-7 cells at a molar ratio of 3:1:1. Whole-cell currents were recorded by the patch-clamp method. Results: In comparison with the current regulated by KChIP2c alone, the co-expression of KCNE2 further slowed Kv4.2 current inactivation kinetics, but diminished KChIP2c-induced positive shift of the voltage-dependent activation of Kv4.2 current. Importantly, co-expression of KCNE2 accelerated the current recovery from inactivation, and caused an "overshoot" of peak current amplitude during Kv4.2 current recovery, a phenomenon which has been uniquely described for humanIto. However, co-expression of KCNE2 exerted no further effect on Kv4.2 current amplitude, the rate of Kv4.2 current activation and voltage-dependent inactivation. Conclusion: Co-expression of Kv4.2 with KChIP2c and KCNE2, but not with KChIP2c or KCNE2 alone, yields a current profile similar to nativeIto. Both KChIP2c and KCNE2 simultaneously participate in recapitulation of the electrophysiological properties of Ito in cardiac myocytes.
Bibliography:KCNE2
electrophysiology
transient outward current; Kv4.2; K^+-channel interacting protein; KCNE2; electrophysiology
transient outward current
Kv4.2
R96
K^+-channel interacting protein
31-1347/R
ISSN:1671-4083
1745-7254