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Investigative Ophthalmology & Visual Science, Vol 34, 539-546, Copyright © 1993 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

Alteration of active Na-K transport on protein kinase C activation in cultured ciliary epithelium

T Mito and NA Delamere
Department of Ophthalmology and Visual Sciences, Kentucky Lions Eye Research Institute, University of Louisville School of Medicine 40292.

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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