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1 Department of Human Physiology, University of California, School of Medicine, Davis, CA, USA
2 USDA-ARS Western Human Nutrition Research Center, Davis, CA, USA
* To whom correspondence should be addressed. E-mail: shpetersen{at}ucdavis.edu.
In this report, we describe the cloning, cellular localization, and functional characteristics of NHE1 (paNHE1) from red blood cells of the winter flounder, Pseudopleuronectes americanus. The paNHE1 protein localizes primarily to the marginal band, and exhibits 74% similarity to the trout 
NHE, and 65% to the human (h)NHE1. Functionally, paNHE1 shares characteristics of both NHE and hNHE1 in that it is activated both by manipulations which increase cAMP, and by cell shrinkage, respectively. In accordance, the paNHE1 protein exhibits both protein kinase A consensus sites as in NHE, and a region of high homology to that required for shrinkage-dependent activation of hNHE1. After shrinkage-dependent activation of paNHE1 and resulting activation of a Cl-/HCO3- exchanger, their parallel operation results in net uptake of NaCl and osmotically obliged water. Activation of paNHE1 by cAMP is at least additive to that elicited by osmotic shrinkage, suggesting that these stimuli regulate paNHE1 by distinct mechanisms. Finally, exposure to the serine/threonine phosphatase inhibitor calyculin A potently activates paNHE1, and this activation is also additive to that induced by shrinkage or cAMP.
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