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Research Article Free access | 10.1172/JCI119279

20-Hydroxyeicosa-tetraenoic acid (20 HETE) activates protein kinase C. Role in regulation of rat renal Na+,K+-ATPase.

S Nowicki, S L Chen, O Aizman, X J Cheng, D Li, C Nowicki, A Nairn, P Greengard, and A Aperia

Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Department of Women and Child Health, Karolinska Institute, Stockholm, Sweden.

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Published March 15, 1997 - More info

Published in Volume 99, Issue 6 on March 15, 1997
J Clin Invest. 1997;99(6):1224–1230. https://doi.org/10.1172/JCI119279.
© 1997 The American Society for Clinical Investigation
Published March 15, 1997 - Version history
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Abstract

It is well documented that the activity of Na+,K+-ATPase can be inhibited by the arachidonic acid metabolite, 20-hydroxyeicosa-tetraenoic acid (20 HETE). Evidence is presented here that this effect is mediated by protein kinase C (PKC). PKC inhibitors abolished 20 HETE inhibition of rat Na+,K+-ATPase in renal tubular cells. 20 HETE caused translocation of PKC alpha from cytoplasm to membrane in COS cells. It also inhibited Na+,K+-ATPase activity in COS cells transfected with rat wild-type renal Na+,K+-ATPase alpha1 subunit, but not in cells transfected with Na+,K+-ATPase alpha1, where the PKC phosphorylation site, serine 23, had been mutated to alanine. PKC-induced phosphorylation of rat renal Na+,K+-ATPase, as well as of histone was strongly enhanced by 20 HETE at the physiologic calcium concentration of 1.3 microM, but not at the calcium concentration of 200 microM. The results indicate that phospholipase A2-arachidonic acid-20 HETE pathway can exert important biological effects via activation of PKC and that this effect may occur in the absence of a rise in intracellular calcium.

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