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1 Department of Human Physiology, School of Medicine, University of California-Davis, and 2 United States Department of Agriculture-Agricultural Research Service Western Human Nutrition Research Center, Davis, California 95616
In this report, we
describe the cloning, cellular localization, and functional
characteristics of Na+/H+ exchanger 1 (NHE1)
from red blood cells of the winter flounder Pseudopleuronectes
americanus (paNHE1). The paNHE1 protein localizes primarily to the
marginal band and exhibits a 74% similarity to the trout
-NHE, and
65% to the human NHE1 (hNHE1). Functionally, paNHE1 shares
characteristics of both
-NHE and hNHE1 in that it is activated both
by manipulations that 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
/HCO
sodium-proton antiport; red blood cells;
-Na+/H+ exchanger; protein kinase A; protein kinase C; protein phosphatases
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