Expression of the human androgen receptor in eukaryotic cells using a recombinant adenovirus vector yields high levels of the soluble, functional receptor protein

The androgen receptor (AR) and closely related members of the steroid recep tor family have proven difficult to obtain in native form in large quantiti es. In the case of the human AR (hAR), high-level expression in prokaryotic or non-mammalian cells leads to the synthesis of a high proportion of non- binding, insoluble, or degraded forms of the receptor protein. To circumvent these difficulties, we have constructed a recombinant adenovi rus that directs the expression of hAR under the control of a potent, const itutive promoter. Infection of eukaryotic cells with this recombinant virus leads to the synthesis of large quantities of the intact AR. In contrast t o expression methods designed to direct the full-length AR in bacteria, yea st, and insect cells, AR expressed in mammalian cells using this adenoviral vector accumulates at high levels, retains many properties of the native A R, and is not rapidly proteolyzed. This method will prove useful for large- scale preparations of hAR for use in functional and structural studies.