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Am J Physiol Renal Physiol (February 19, 2002). doi:10.1152/ajprenal.00226.2001
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Articles in PresS, published online ahead of print February 19, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00226.2001
Submitted on July 20, 2001
Accepted on February 13, 2002

Stimulation of the Protein Kinase C pathway mediates endocytosis of the human nongastric H+,K+-ATPase ATP1AL1

Juergen Reinhardt1*, Markus Kosch2, Markus Lerner1, Helga Bertram1, Dieter Lemke1, and Hans Oberleithner1

1 Institute of Physiology, University of Muenster, Muenster, NRW, Germany
2 Department of Internal Medicine, University of Muenster, Muenster, NRW, Germany

* To whom correspondence should be addressed. E-mail: Reinhard{at}uni-muenster.de.

The human nongastric H+,K+-ATPase, ATP1AL1, shown to reabsorb K+ in exchange to H+ or Na+ ions, is localized in the luminal plasma membrane of renal epithelial cells. It is presumed that renal H+,K+-ATPases can be regulated by endocytosis. However, little is known about the molecular mechanisms which control plasma membrane expression of renal H+,K+-ATPase. In our study activation of PKC using phorbol-esters (PMA) leads to clathrin dependent internalization and intracellular accumulation of the ion pump in stable-transfected MDCK cells. Functional inactivation of the H+,K+-ATPase by PKC activation is shown by intracellular pH measurements. Proton extrusion capacity of ATP1AL1 transfected cells is drastically reduced after PMA incubation and could be prevented with the PKC blocker bisindolylmalenimide. Ion pump internalization and inactivation is specifically mediated by the PKC pathway whereas activation of the Protein Kinase A (PKA) pathway has no influence. Our results show that the nongastric H+,K+-ATPase is a specific target for the PKC pathway. Therefore PKC mediated phosphorylation is a potential regulatory mechanism for apical nongastric H+,K+-ATPase plasma membrane expression.




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