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1 Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235; 2 Department of Internal Medicine, Jichi Medical School, Tochigi, Japan 329-0498; 3 Dallas Veterans Affairs Medical Center, Dallas 75216; 4 Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235; and 5 Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75235
Endothelin-1 (ET-1) activates
sodium/hydrogen exchanger 3 (NHE3) in opossum kidney clone P (OKP)
cells expressing ETB receptors. ET-1 (10
8 M)
caused a two- to threefold increase in apical membrane NHE3 (assessed
by surface biotinylation), in the absence of a change in total cellular
NHE3. A maximal effect was achieved within 15 min. The increase in
apical NHE3 was not blocked by cytochalasin D but was blocked by
latrunculin B, which also prevented the ET-1-induced increase in NHE3
activity. Endocytic internalization of NHE3, measured as protection of
biotinylated NHE3 from the membrane-impermeant, sulfhydryl-reducing
agent MesNa was minimal within 35 min and was not regulated by ET-1.
Exocytic insertion of NHE3, measured as the appearance of biotinylated
NHE3 after the blockade of reactive sites with sulfo-NHS-acetate, was
increased in response to ET-1. These studies demonstrate that ET-1
induces net trafficking of NHE3 to the apical membrane that is mediated
by enhanced exocytic insertion and is required for increased NHE3 activity.
sodium/hydrogen antiporter; sodium/hydrogen exchanger 3; opossum kidney clone 3; endothelin; membrane trafficking; proximal tubule
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