Protein Kinase C Activates ATP-sensitive Potassium Channels in Rabbit Ventricular Myocytes.
- Author:
Nari KIM
1
;
Jae Boum YOUM
;
Hyun JOO
;
Hyungkyu KIM
;
Euiyong KIM
;
Jin HAN
Author Information
1. Mitochondrial Signaling Laboratory, Department of Physiology and Biophysics, College of Medicine, Cardiovascular & Metabolic Disease Center, Biohealth Products Research Center, Inje University, Busan 614-735, Korea. phyhanj@ijnc.inje.ac.kr
- Publication Type:Original Article
- Keywords:
KATP channel;
Patch-clamp electrophysiology;
Protein kinase C;
Phorbol 12, 13-didecanoate;
Bisindolylmaleimide
- MeSH:
Adenosine Triphosphate;
Ischemic Preconditioning;
KATP Channels*;
Muscle Cells*;
Okadaic Acid;
Patch-Clamp Techniques;
Protein Kinase C*;
Protein Kinases*;
Signal Transduction
- From:The Korean Journal of Physiology and Pharmacology
2005;9(4):187-193
- CountryRepublic of Korea
- Language:English
-
Abstract:
Several signal transduction pathways have been implicated in ischemic preconditioning induced by the activation of ATP-sensitive K+ (KATP) channels. We examined whether protein kinase C (PKC) modulated the activity of KATP channels by recording KATP channel currents in rabbit ventricular myocytes using patch-clamp technique and found that phorbol 12, 13-didecanoate (PDD) enhanced pinacidil-induced KATP channel activity in the cell-attached configuration; and this effect was prevented by bisindolylmaleimide (BIM). KATP channel activity was not increased by 4alpha-PDD. In excised inside-out patches, PKC stimulated KATP channels in the presence of 1 mM ATP, and this effect was abolished in the presence of BIM. Heat-inactivated PKC had no effect on channel activity. PKC-induced activation of KATP channels was reversed by PP2A, and this effect was not detected in the presence of okadaic acid. These results suggest that PKC activates KATP channels in rabbit ventricular myocytes.
