Reactivation of the androgen receptor from murine preputial gland by thioredoxin or GSH

The androgen receptor from murine preputial gland was inactivated by density gradient centrifugation, affinity chromatography and isoelectric focusing. The hormone binding of the receptor could be partially restored (roughly 40%) by the thioredoxin-thioredoxinreductase system, by thioredoxin plus di...

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Veröffentlicht in:	Journal of steroid biochemistry 1989, Vol.32 (1), p.53-58
Hauptverfasser:	Wiegand, Manfred, Ofenloch-Hähnle, Beatus, Eisele, Karl
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Bacterial Proteins - pharmacology Biological and medical sciences Cell receptors Cell structures and functions Centrifugation, Density Gradient Chromatography, Affinity Cytosol - metabolism Fundamental and applied biological sciences. Psychology Glutathione - pharmacology Isoelectric Focusing Kinetics Male Mice Molecular and cellular biology Penis - metabolism Receptors, Androgen - drug effects Receptors, Androgen - isolation & purification Receptors, Androgen - metabolism Sebaceous Glands - metabolism Thioredoxins - pharmacology
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Beschreibung
Zusammenfassung:	The androgen receptor from murine preputial gland was inactivated by density gradient centrifugation, affinity chromatography and isoelectric focusing. The hormone binding of the receptor could be partially restored (roughly 40%) by the thioredoxin-thioredoxinreductase system, by thioredoxin plus dithiothreitol or by glutathione. Dithiothreitol, by itself, was unable to reactivate the androgen receptor. These findings show that the receptor inactivation is, at least partially, due to thiol group oxidation and removal of SH-reducing and/or -stabilizing substances from the receptor during purification.
ISSN:	0022-4731
DOI:	10.1016/0022-4731(89)90013-7