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Related Experiment Video

Updated: Jun 23, 2026

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

Accessory subunit KChIP2 modulates the cardiac L-type calcium current.

Morten B Thomsen¹, Chaojian Wang, Nazira Ozgen

¹Department of Medicine, Duke University Medical Center, Box 103030 Medical Center, Durham, NC 27710, USA.

Circulation Research

|May 23, 2009

Summary

K+ channel interacting protein 2 (KChIP2) directly regulates cardiac L-type Ca2+ current (ICa,L) by binding to the Ca(V)1.2 alpha(1C) subunit. This interaction increases ICa,L density, suggesting KChIP2 is a multimodal regulator of cardiac ionic currents.

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Last Updated: Jun 23, 2026

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

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Published on: November 11, 2022

Primary Culture of Adult Rat Heart Myocytes

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Published on: June 16, 2009

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

Area of Science:

Cardiovascular Physiology
Molecular Cardiology
Ion Channel Regulation

Background:

Complex modulation of voltage-gated Ca2+ currents involves interplay between Ca2+ channels and Ca2+-binding proteins.
K+ channel interacting protein 2 (KChIP2) is a Ca2+-binding protein known to regulate K(V)4.2 channels.

Purpose of the Study:

To investigate the hypothesis that KChIP2 directly regulates the cardiac L-type Ca2+ current (ICa,L).

Main Methods:

Electrophysiological recordings in KChIP2 knockout and wild-type myocytes.
Transfected cell line experiments to isolate Ca2+ channel current.
Biochemical analysis to determine protein interactions.

Main Results:

ICa,L density was reduced by 28% in KChIP2 knockout myocytes compared to wild-type.
KChIP2 directly affects Ca2+ channel current, independent of Ca2+ binding.
KChIP2 interacts with the N-terminal inhibitory module of the Ca(V)1.2 alpha(1C) subunit, augmenting ICa,L density without altering protein expression or trafficking.

Conclusions:

KChIP2 directly augments cardiac ICa,L by impeding the N-terminal inhibitory module of Ca(V)1.2.
KChIP2 acts as a multimodal regulator of cardiac ionic currents, influencing K(V), Na(V), and Ca2+ channels.