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Endocrinology Vol. 140, No. 2 660-666
Copyright © 1999 by The Endocrine Society

ARTICLES

Rapid Action of 17ß-Estradiol on Kainate-Induced Currents in Hippocampal Neurons Lacking Intracellular Estrogen Receptors1

Qin Gu, Kenneth S. Korach and Robert L. Moss

Department of Physiology, University of Texas Southwestern Medical Center (Q.G., R.L.M.), Dallas, Texas 75235; Laboratories for Reproductive Biology, University of North Carolina (K.S.K.), Chapel Hill, North Carolina 27599

Address all correspondence and requests for reprints to: Dr. Robert L. Moss, Department of Physiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9049. E-mail: rmoss{at}mednet.swmed.edu

17ß-Estradiol can potentiate kainate-induced currents in isolated hippocampal CA1 neurons. The action of estrogen was rapid in onset, steroid and stereospecific, and reversible. The potentiation could be mimicked by 8-bromo-cAMP, an activator of protein kinase A. As the hippocampus expresses both isoforms of the intracellular estrogen receptor (ER{alpha} and ERß), the role of ERs in the rapid action of 17ß-estradiol remains elusive. Here we report that the rapid action of 17ß-estradiol is independent from the classical ER activation in the modulation of membrane excitability. Under whole cell voltage clamp recording configuration, 17ß-estradiol-induced potentiation was observed in both wild-type and the ER{alpha} gene knockout mice. The perfusion or incubation of ICI 182,780, which blocks both ER{alpha} and ERß, did not affect estrogen potentiation in either group. Further study showed that adenosine 3',5'-cyclic-monophosphothioate Rp-isomer, a specific inhibitor of protein kinase A, completely blocked the potentiation observed with the application of 17ß-estradiol in ER{alpha} gene knockout mice. Our results provide evidence that a distinct estrogen-binding site exists, which appears to be coupled to {alpha}-amino-3-hydroxyl-5-methyl-4-isoxazole proprionic acid/kainate receptors by a cAMP-dependent phosphorylation process.




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