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Papers In Press, published online ahead of print April 4, 2002
Department of Internal Medicine, University of Iowa, Iowa City, IA 52246
Corresponding Author: joseph-dillon{at}uiowa.edu
The adrenal steroid dehydroepiandrosterone (DHEA) has no known cellular receptor or unifying mechanism of action, despite evidence suggesting beneficial vascular effects in humans. Based on previous data from our laboratory, we hypothesized that DHEA binds to specific cell-surface receptors to activate intracellular G-proteins and endothelial nitric oxide synthase (eNOS). We now pharmacologically characterize a putative plasma membrane DHEA receptor and define its associated G-proteins. The [3H]DHEA binding to isolated plasma membranes from bovine aortic endothelial cells was of high affinity (Kd = 48.7 pM) and saturable (Bmax = 500 fmol/mg protein). Structurally related steroids failed to compete with DHEA for binding. The putative DHEA receptor was functionally coupled to G-proteins, since guanosine-5’-O-(3-thio) triphosphate (GTP
J. Biol. Chem, 10.1074/jbc.M200491200
Submitted on January 16, 2002
Revised on March 29, 2002
Accepted on April 3, 2002
Dehydroepiandrosterone activates endothelial cell nitric oxide synthase by a specific plasma membrane receptor coupled to G
i2,3
S) inhibited [3H]DHEA binding to plasma membranes by 69%, and DHEA increased [35S]GTPS binding by 157%. DHEA stimulated [35S]GTPS binding to G
i2 and Gi3, but not to Gi1 or Go. Pretreatment of plasma membranes with antibody to Gi2 or Gi3, but not to Gi1, inhibited the DHEA-activation of eNOS. Thus, DHEA receptors are expressed on endothelial cell plasma membranes and are coupled to eNOS activity through Gi2 and Gi3. These novel findings should allow us to isolate the putative receptor and reevaluate the physiological role of DHEA activity.
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