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Dehydroepiandrosterone Activates Mutant Androgen Receptors Expressed in the Androgen-Dependent Human Prostate Cancer Xenograft CWR22 and LNCaP Cells

Laboratories for Reproductive Biology Departments of Pediatrics (J.-A.T., K.G.H., C.W.G., D.-Y.Z., M.S., E.M.W., F.S.F.), Biochemistry and Biophysics (E.M.W.), Surgery (Y.S., J.L.M.), and Pathology (J.L.M.) and The Lineberger Comprehensive Cancer Center (E.M.W., F.S.F., J.L.M.) School of Medicine The University of North Carolina Chapel Hill, North Carolina 27599 Department of Urology and Medicine (P.G., R.dW.) University of California Davis Medical Center Sacramento, California 95817 Department of Medicine (S.E.H.) The University of Texas Health Science Center San Antonio, Texas 78284-7756 Department of Pathology (T.G.P.) School of Medicine Case Western Reserve University Cleveland, Ohio 44160

An androgen receptor (AR) gene mutation identified in the androgen-dependent human prostate cancer xenograft, CWR22, changed codon 874 in the ligand-binding domain (exon H) from CAT for histidine to TAT for tyrosine and abolished a restriction site for the endonuclease SfaNI. SfaNI digestion of AR exon H DNA from normal but not from prostate cancer tissue indicated H874Y is a somatic mutation that occurred before the initial tumor transplant. CWR22, an epithelial cell tumor, expresses a 9.6-kb AR mRNA similar in size to the AR mRNA in human benign prostatic hyperplasia. AR protein is present in cell nuclei by immunostaining as in other androgen-responsive tissues. Transcriptional activity of recombinant H874Y transiently expressed in CV1 cells in the presence of testosterone or dihydrotestosterone was similar to that of wild type AR. With dihydrotestosterone at a near physiological concentration (0.01 nM), H874Y and wild type AR induced 2-fold greater luciferase activity than did the LNCaP mutant AR T877A. The adrenal androgen, dehydroepiandrosterone (10 and 100 nM) with H874Y stimulated a 3- to 8-fold greater response than with wild type AR and at 100 nM the response was similar with the LNCaP mutant. H874Y, like the LNCaP cell mutant, was more responsive to estradiol and progesterone than was wild type AR. The antiandrogen hydroxyflutamide (10 nM) had greater agonist activity (4- to 7-fold) with both mutant ARs than with wild type AR. AR mutations that alter ligand specificity may influence tumor progression subsequent to androgen withdrawal by making the AR more responsive to adrenal androgens or antiandrogens.

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