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1 Department of Physiology, Wayne State University School of Medicine, Detroit, MI, USA
2 Department of Internal Medicine, Wayne State University School of Medicine, Detroit, MI, USA
3 Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA
* To whom correspondence should be addressed. E-mail: dyingst{at}med.wayne.edu.
We present evidence that Na,K-ATPase in the rat proximal tubule is directly activated by angiotensin II (Ang II) much faster than previously observed. Specifically, we show that a twominute exposure to 0.1 and 1 nM Ang II slowed the rate of intracellular sodium accumulation in response to an increase in extracellular sodium added in the presence of gramicidin D. From these data we show that Ang II directly stimulates Na,K-ATPase activity at rate-limiting
concentrations of intracellular sodium. Under these same conditions exposing proximal tubules to Ang II altered the amount of 32P incorporated into multiple phosphopeptides generated from a tryptic digest of the 
-subunit of Na,K-ATPase. Na,K-ATPase was isolated from whole cell lysates by means of an ouabain-affinity column and then separated into its individual subunits by
SDS PAGE. Na,K-ATPase bound to the column in its E2 conformation and was eluted by altering its conformation to E1 using Na+ATP. Na,K-ATPase isolated from cells treated with Ang II eluted more easily from the ouabain-affinity column than Na,K-ATPase isolated from control cells, suggesting that Ang II decreased the affinity of Na,K-ATPase for ouabain. Thus, Ang II rapidly stimulated the activity of Na,K-ATPase in two minutes or less by a mechanism that could involve changes in phosphorylation and conformation of Na,K-ATPase. We suggest
that the physiological role for rapid direct activation of Na,K-ATPase is greater control of intracellular sodium during sodium reabsorption.
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