March 1993
Volume 34, Issue 3
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Articles  |   March 1993
Alteration of active Na-K transport on protein kinase C activation in cultured ciliary epithelium.
Author Affiliations
  • T Mito
    Department of Ophthalmology and Visual Sciences, Kentucky Lions Eye Research Institute, University of Louisville School of Medicine 40292.
  • N A Delamere
    Department of Ophthalmology and Visual Sciences, Kentucky Lions Eye Research Institute, University of Louisville School of Medicine 40292.
Investigative Ophthalmology & Visual Science March 1993, Vol.34, 539-546. doi:
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      T Mito, N A Delamere; Alteration of active Na-K transport on protein kinase C activation in cultured ciliary epithelium.. Invest. Ophthalmol. Vis. Sci. 1993;34(3):539-546.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

PURPOSE: Experiments were conducted to test whether protein kinase C activation causes changes in active sodium-potassium transport in an established SV-40 transformed line (ODM2) of cultured human nonpigmented ciliary epithelial cells. METHODS: Rubidium-86 (86Rb) uptake was measured and the data used to determine the rate of potassium entry into the cells. RESULTS: Protein kinase C activator, phorbol dibutyrate (PDBu), caused a stimulation of ouabain-sensitive 86Rb uptake. Inhibition of protein kinase C by 1-(5-isoquinolinylsulfonyl) 2-methylpiperazine (H-7), or down-regulation of protein kinase C activation by prolonged exposure of PDBu, decreased the PDBu response. These results suggest that protein kinase C plays a role in Na-K pump activation. The Na/H+ exchanger inhibitor, amiloride, also reduced the stimulation of the ouabain-sensitive 86Rb uptake by PDBu. 86Rb efflux was not altered by protein kinase C activation. At the same time that PDBu increased the ouabain-sensitive 86Rb uptake, it also decreased the ouabain-insensitive 86Rb uptake. The ouabain-insensitive 86Rb uptake component could be inhibited by bumetanide, suggesting that protein kinase C activation decreases the activity of a Na/K/2Cl cotransporter. CONCLUSIONS: These findings suggest that activation of protein kinase C may stimulate Na,K-ATPase activity mainly by a mechanism involving increased Na+ influx mediated by the Na+/H+ exchanger.

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