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Journal of Clinical Endocrinology & Metabolism, Vol 80, 2993-2996, Copyright © 1995 by Endocrine Society
ARTICLES |
T Okabe, M Haji, R Takayanagi, M Adachi, K Imasaki, F Kurimoto, T Watanabe and H Nawata
Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Although evidence indicates that dehydroepiandrosterone (DHEA) exerts direct physiological effects, its mechanism of action remains unknown. DHEA binding sites were examined using a whole-cell binding assay in a human T lymphoid cell line, PEER, revealing that a single class of high- affinity binding sites for DHEA (dissociation constant = 7.4 +/- 0.53 nmol/L, mean +/- SE, n = 4) was greatly increased when treated with DHEA, phorbol-12-myristate-13-acetate, and the Ca2+ ionophore A23187. Bound [3H]DHEA was displaced sensitively by DHEA and secondarily by dihydrotestosterone, but not effectively by other steroids, including DHEA sulfate. These results not only indicate the existence of a DHEA receptor, but also suggest that T cells become susceptible to regulation by DHEA during the process of signal-induced activation.
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