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Journal Article

Functional testosterone receptors in plasma membranes of T cells


Giese,  Günter
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;
Light Microscopy Facility, Max Planck Institute for Medical Research, Max Planck Society;

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Benten, W. P. M., Lieberherr, M., Giese, G., Wrehlke, C., Stamm, O., Sekeris, C. E., et al. (1999). Functional testosterone receptors in plasma membranes of T cells. The FASEB Journal, 13(1), 123-133. Retrieved from http://www.fasebj.org/cgi/content/abstract/13/1/123?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26andorexactfulltext%3Dand%26searchid%3D1%26FIRSTINDEX%3D0%26sortspec%3Drelevance%26volume%3D13%26firstpage%3D123%26resourcetype%3DHWCIT.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A385-A
T cells are considered to be unresponsive to testosterone due to the absence of androgen receptors (AR). Here, we demonstrate the testosterone responsiveness of murine splenic T cells in vitro as well as the presence of unconventional cell surface receptors for testosterone and classical intracellular AR. Binding sites for testosterone on the surface of both CD4(+) and CD8(+) subsets of T cells are directly revealed with the impeded ligand testosterone-BSA-FITC by confocal laser scanning microscopy (CLSM) and flow cytometry, respectively. Binding of the plasma membrane impermeable testosterone-BSA conjugate induces a rapid rise (<5 s) in [Ca2+]i of Fura-2-loaded T cells. This rise reflects influx of extracellular Ca2+ through non-voltage-gated and Ni2+-blockable Ca2+ channels of the plasma membrane. The testosterone-BSA-induced Ca2+ import is not affected by cyproterone, a blocker of the AR. In addition, AR are not detectable on the surface of intact T cells when using anti-AR antibodies directed against the amino and carboxy terminus of the AR, although T cells contain AR, as revealed by reverse transcription-polymerase chain reactions and Western blotting. AR can be visualized with the anti-AR antibodies in the cytoplasm of permeabilized T cells by using CLSM, though AR are not detectable in cytosol fractions when using the charcoal binding assay with 3H-R1881 as ligand. Cytoplasmic AR do not translocate to the nucleus of T cells in the presence of testosterone, in contrast to cytoplasmic AR in human cancer LNCaP cells. These findings suggest that the classical AR present in splenic T cells are not active in the genomic pathway. By contrast, the cell surface receptors for testosterone are in a functionally active state, enabling T cells a nongenomic response to testosterone.