Protein Kinase C Activates ATP-sensitive Potassium Channels in Rabbit Ventricular Myocytes
The Korean Journal of Physiology and Pharmacology
;
: 187-193, 2005.
Article
in English
| WPRIM
| ID: wpr-727650
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Kinases
/
Protein Kinase C
/
Signal Transduction
/
Adenosine Triphosphate
/
Patch-Clamp Techniques
/
Okadaic Acid
/
Ischemic Preconditioning
/
Muscle Cells
/
KATP Channels
Type of study:
Diagnostic study
Language:
English
Journal:
The Korean Journal of Physiology and Pharmacology
Year:
2005
Type:
Article
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