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

S. Zoppi, D. R. Allman, R. D. Gerard, M. J. McPhaul

Research output: Contribution to journalArticle

Abstract

The androgen receptor (AR) and closely related members of the steroid receptor family have proven difficult to obtain in native form in large quantities. 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 adenovirus that directs the expression of hAR under the control of a potent, constitutive promoter. Infection of eukaryotic cells with this recombinant virus leads to the synthesis of large quantities of the intact AR. In contrast to expression methods designed to direct the full-length AR in bacteria, yeast, and insect cells, AR expressed in mammalian cells using this adenoviral vector accumulates at high levels, retains many properties of the native AR, and is not rapidly proteolyzed. This method will prove useful for large-scale preparations of hAR for use in functional and structural studies.

Original languageEnglish (US)
Pages (from-to)321-328
Number of pages8
JournalJournal of Molecular Endocrinology
Volume27
Issue number3
DOIs
StatePublished - 2001

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Androgen Receptors
Eukaryotic Cells
Adenoviridae
Proteins
Steroid Receptors
Insects
Yeasts
human AR protein
Viruses
Bacteria
Infection

ASJC Scopus subject areas

  • Endocrinology

Cite this

Expression of the human androgen receptor in eukaryotic cells using a recombinant adenovirus vector yields high levels of the soluble, functional receptor protein. / Zoppi, S.; Allman, D. R.; Gerard, R. D.; McPhaul, M. J.

In: Journal of Molecular Endocrinology, Vol. 27, No. 3, 2001, p. 321-328.

Research output: Contribution to journalArticle

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