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Am J Physiol Cell Physiol 276: C938-C945, 1999;
0363-6143/99 $5.00
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Vol. 276, Issue 4, C938-C945, April 1999

ETB receptor activation leads to activation and phosphorylation of NHE3

Y. Peng1, O. W. Moe1,2, T.-S. Chu1, P. A. Preisig1, M. Yanagisawa3,4, and R. J. Alpern1

Departments of 1 Internal Medicine and 3 Molecular Genetics and 4 Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, 75235; and 2 Veterans Affairs Medial Center, Dallas, Texas 75216

In OKP cells expressing ETB endothelin receptors, activation of Na+/H+ antiporter activity by endothelin-1 (ET-1) was resistant to low concentrations of ethylisopropyl amiloride, indicating regulation of Na+/H+ exchanger isoform 3 (NHE3). ET-1 increased NHE3 phosphorylation in cells expressing ETB receptors but not in cells expressing ETA receptors. Receptor specificity was not due to demonstrable differences in receptor-specific activation of tyrosine phosphorylation pathways or inhibition of adenylyl cyclase. Phosphorylation was associated with a decrease in mobility on SDS-PAGE, which was reversed by treating immunoprecipitated NHE3 with alkaline phosphatase. Phosphorylation was first seen at 5 min and was maximal at 15-30 min. Phosphorylation was maximal with 10-9 M ET-1. Phosphorylation occurred on threonine and serine residues at multiple sites. In summary, ET-1 induces NHE3 phosphorylation in OKP cells on multiple threonine and serine residues. ETB receptor specificity, time course, and concentration dependence are all similar between ET-1-induced increases in NHE3 activity and phosphorylation, suggesting that phosphorylation plays a key role in activation.

sodium/hydrogen antiporter; adenylyl cyclase; tyrosine kinases; endothelin; OKP cells


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