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. 1996 Sep 15;495(Pt 3):681–688. doi: 10.1113/jphysiol.1996.sp021625

Protein kinase C inhibition of cloned inward rectifier (HRK1/KIR2.3) K+ channels expressed in Xenopus oocytes.

P Henry 1, W L Pearson 1, C G Nichols 1
PMCID: PMC1160774  PMID: 8887775

Abstract

1. The effect of protein kinase activators on cloned inward rectifier channels expressed in Xenopus oocytes was examined using a two-electrode voltage clamp. PKA activators caused no change in KIR1.1, KIR2.1, or KIR2.3 current. The PKC activators phorbol 12-myristate 14-acetate (PMA) and phorbol 12, 13-dibutyrate (PDBu) inhibited KIR2.3 currents, but not KIR2.1 or KIR1.1 current. This inhibition was blocked by staurosporine. An inactive phorbol ester, 4 alpha-phorbol 12, 13-didecanoate (4 alpha-PDD), had no effect on KIR2.3. 2. Upon changing solution from 2 to 98 microM K+, KIR2.3 but not KIR1.1 or KIR2.1 currents typically 'ran down' over 5 min to 60-80% of maximum amplitude. Rundown occurred even if PMA was applied before changing to high [K+] solution, indicating that rundown was independent of PKC activity. Rundown was evoked by substituting NMG+ for Na+, showing that it results from low [Na+] and not from high [K+]. 3. These results suggest that KIR2.3, but not KIR1.1 or KIR2.1, is subject to regulation, both by PKC activation and as a consequence of low [Na+]o. The difference in secondary regulation may account for specific responses to PKC stimulation of tissues expressing otherwise nearly identical KIR channels.

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Selected References

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