Androgen receptor abnormalities in castration-recurrent prostate cancer

References

• Bain DL, Heneghan AF, Connaghan-Jones KD, Miura MT. Nuclear receptor structure: implications for function. Annu. Rev. Physiol.69, 201–220 (2007).
   PubMed Web of Science ®Google Scholar
• Sonoda J, Pei L, Evans RM. Nuclear receptors: decoding metabolic disease. FEBS Lett.582(1), 2–9 (2008).
   PubMed Web of Science ®Google Scholar
• Lange CA, Gioeli D, Hammes SR, Marker PC. Integration of rapid signaling events with steroid hormone receptor action in breast and prostate cancer. Annu. Rev. Physiol.69, 171–199 (2007).
   PubMed Web of Science ®Google Scholar
• Dehm SM, Tindall DJ. Androgen receptor structural and functional elements: role and regulation in prostate cancer. Mol. Endocrinol.21(12), 2855–2863 (2007).
   PubMed Web of Science ®Google Scholar
• Jemal A, Siegel R, Ward E et al. Cancer statistics, 2008. CA Cancer J. Clin.58(2), 71–96 (2008).
   PubMed Web of Science ®Google Scholar
• Huggins C, Hodges CV. Studies on prostatic cancer: I. The effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate. 1941. J. Urol.168(1), 9–12 (2002).
   PubMed Web of Science ®Google Scholar
• Denmeade SR, Isaacs JT. A history of prostate cancer treatment. Nat. Rev. Cancer2(5), 389–396 (2002).
   PubMed Web of Science ®Google Scholar
• Culig Z, Bartsch G. Androgen axis in prostate cancer. J. Cell Biochem.99(2), 373–381 (2006).
   PubMed Web of Science ®Google Scholar
• Debes JD, Tindall DJ. Mechanisms of androgen-refractory prostate cancer. N. Engl. J. Med.351(15), 1488–1490 (2004).
   PubMed Web of Science ®Google Scholar
• Dehm SM, Tindall DJ. Regulation of androgen receptor signaling in prostate cancer. Expert Rev. Anticancer Ther.5(1), 63–74 (2005).
   PubMed Web of Science ®Google Scholar
• Culig Z, Bartsch G, Hobisch A. Antiandrogens in prostate cancer endocrine therapy. Curr. Cancer Drug Targets4(5), 455–461 (2004).
   PubMedGoogle Scholar
• Moul JW, Chodak G. Combination hormonal therapy: a reassessment within advanced prostate cancer. Prostate Cancer Prostatic Dis.7(Suppl. 1), S2–S7 (2004).
   Google Scholar
• Levinson A, Nagler EA, Lowe FC. Approach to management of clinically localized prostate cancer in patients with human immunodeficiency virus. Urology65(1), 91–94 (2005).
   PubMedGoogle Scholar
• Grossmann ME, Huang H, Tindall DJ. Androgen receptor signaling in androgen-refractory prostate cancer. J. Natl Cancer Inst.93(22), 1687–1697 (2001).
   PubMed Web of Science ®Google Scholar
• Scher HI, Sawyers CL. Biology of progressive, castration-resistant prostate cancer: directed therapies targeting the androgen-receptor signaling axis. J. Clin. Oncol.23(32), 8253–8261 (2005).
   PubMed Web of Science ®Google Scholar
• Feldman BJ, Feldman D. The development of androgen-independent prostate cancer. Nat. Rev. Cancer1(1), 34–45 (2001).
   PubMed Web of Science ®Google Scholar
• Gao H, Ouyang X, Banach-Petrosky WA, Shen MM, Abate-Shen C. Emergence of androgen independence at early stages of prostate cancer progression in Nkx3.1; Pten mice. Cancer Res.66(16), 7929–7933 (2006).
   PubMed Web of Science ®Google Scholar
• Steinkamp MP, O’Mahony OA, Brogley M et al. Treatment-dependent androgen receptor mutations in prostate cancer exploit multiple mechanisms to evade therapy. Cancer Res.69(10), 4434–4442 (2009).
   PubMed Web of Science ®Google Scholar
• Chen G, Wang X, Zhang S et al. Androgen receptor mutants detected in recurrent prostate cancer exhibit diverse functional characteristics. Prostate63(4), 395–406 (2005).
   PubMed Web of Science ®Google Scholar
• Buchanan G, Irvine RA, Coetzee GA, Tilley WD. Contribution of the androgen receptor to prostate cancer predisposition and progression. Cancer Metastasis Rev.20(3–4), 207–223 (2001).
   PubMed Web of Science ®Google Scholar
• Locke JA, Guns ES, Lubik AA et al. Androgen levels increase by intratumoral de novo steroidogenesis during progression of castration-resistant prostate cancer. Cancer Res.68(15), 6407–6415 (2008).
   PubMed Web of Science ®Google Scholar
• Titus MA, Schell MJ, Lih FB, Tomer KB, Mohler JL. Testosterone and dihydrotestosterone tissue levels in recurrent prostate cancer. Clin. Cancer Res.11(13), 4653–4657 (2005).
   PubMed Web of Science ®Google Scholar
• Mohler JL, Gregory CW, Ford OH 3rd et al. The androgen axis in recurrent prostate cancer. Clin. Cancer Res.10(2), 440–448 (2004).
   PubMed Web of Science ®Google Scholar
• Mostaghel EA, Montgomery B, Nelson PS. Castration-resistant prostate cancer: targeting androgen metabolic pathways in recurrent disease. Urol. Oncol.27(3), 251–257 (2009).
   PubMed Web of Science ®Google Scholar
• Montgomery RB, Mostaghel EA, Vessella R et al. Maintenance of intratumoral androgens in metastatic prostate cancer: a mechanism for castration-resistant tumor growth. Cancer Res.68(11), 4447–4454 (2008).
   PubMed Web of Science ®Google Scholar
• Stanbrough M, Bubley GJ, Ross K et al. Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer. Cancer Res.66(5), 2815–2825 (2006).
   PubMed Web of Science ®Google Scholar
• Shen HC, Balk SP. Development of androgen receptor antagonists with promising activity in castration-resistant prostate cancer. Cancer Cell15(6), 461–463 (2009).
   PubMed Web of Science ®Google Scholar
• Attar RM, Takimoto CH, Gottardis MM. Castration-resistant prostate cancer: locking up the molecular escape routes. Clin. Cancer Res.15(10), 3251–3255 (2009).
   PubMed Web of Science ®Google Scholar
• Tindall DJ, Rittmaster RS. The rationale for inhibiting 5-reductase isoenzymes in the prevention and treatment of prostate cancer. J. Urol.179(4), 1235–1242 (2008).
   PubMed Web of Science ®Google Scholar
• Attard G, Reid AH, Olmos D, de Bono JS. Antitumor activity with CYP17 blockade indicates that castration-resistant prostate cancer frequently remains hormone driven. Cancer Res.69(12), 4937–4940 (2009).
   PubMed Web of Science ®Google Scholar
• Attard G, Reid AH, Yap TA et al. Phase I clinical trial of a selective inhibitor of CYP17, abiraterone acetate, confirms that castration-resistant prostate cancer commonly remains hormone driven. J. Clin. Oncol.26(28), 4563–4571 (2008).
   PubMed Web of Science ®Google Scholar
• Wilson JD. The role of 5-reduction in steroid hormone physiology. Reprod. Fertil. Dev.13(7–8), 673–678 (2001).
   PubMed Web of Science ®Google Scholar
• Andriole G, Bruchovsky N, Chung LW et al. Dihydrotestosterone and the prostate: the scientific rationale for 5-reductase inhibitors in the treatment of benign prostatic hyperplasia. J. Urol.172(4 Pt 1), 1399–1403 (2004).
   PubMed Web of Science ®Google Scholar
• Zhou ZX, Lane MV, Kemppainen JA, French FS, Wilson EM. Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability. Mol. Endocrinol.9(2), 208–218 (1995).
   PubMed Web of Science ®Google Scholar
• Wright AS, Thomas LN, Douglas RC, Lazier CB, Rittmaster RS. Relative potency of testosterone and dihydrotestosterone in preventing atrophy and apoptosis in the prostate of the castrated rat. J. Clin. Invest.98(11), 2558–2563 (1996).
   PubMed Web of Science ®Google Scholar
• Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev.18(3), 306–360 (1997).
   PubMed Web of Science ®Google Scholar
• Smith DF, Toft DO. Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions. Mol. Endocrinol.22(10), 2229–2240 (2008).
   PubMed Web of Science ®Google Scholar
• Elbi C, Walker DA, Romero G et al. Molecular chaperones function as steroid receptor nuclear mobility factors. Proc. Natl Acad. Sci. USA101(9), 2876–2881 (2004).
   PubMed Web of Science ®Google Scholar
• Heemers HV, Tindall DJ. Androgen receptor (AR) coregulators: a diversity of functions converging on and regulating the AR transcriptional complex. Endocr. Rev.28(7), 778–808 (2007).
   PubMed Web of Science ®Google Scholar
• Agoulnik IU, Weigel NL. Coactivator selective regulation of androgen receptor activity. Steroids74(8), 669–674 (2009).
   PubMed Web of Science ®Google Scholar
• Edwards J, Bartlett JM. The androgen receptor and signal-transduction pathways in hormone-refractory prostate cancer. Part 1: modifications to the androgen receptor. BJU Int.95(9), 1320–1326 (2005).
   PubMed Web of Science ®Google Scholar
• Mahajan NP, Liu Y, Majumder S et al. Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation. Proc. Natl Acad. Sci. USA104(20), 8438–8443 (2007).
   PubMed Web of Science ®Google Scholar
• Guo Z, Dai B, Jiang T et al. Regulation of androgen receptor activity by tyrosine phosphorylation. Cancer Cell10(4), 309–319 (2006).
   PubMed Web of Science ®Google Scholar
• Cardozo T, Pagano M. The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol.5(9), 739–751 (2004).
   PubMed Web of Science ®Google Scholar
• Ravid T, Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol.9(9), 679–690 (2008).
   PubMed Web of Science ®Google Scholar
• Lin HK, Yeh S, Kang HY, Chang C. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc. Natl Acad. Sci. USA98(13), 7200–7205 (2001).
   PubMed Web of Science ®Google Scholar
• Taneja SS, Ha S, Swenson NK et al. Cell-specific regulation of androgen receptor phosphorylation in vivo. J. Biol. Chem.280(49), 40916–40924 (2005).
   PubMed Web of Science ®Google Scholar
• Xin L, Teitell MA, Lawson DA, Kwon A, Mellinghoff IK, Witte ON. Progression of prostate cancer by synergy of AKT with genotropic and nongenotropic actions of the androgen receptor. Proc. Natl Acad. Sci. USA103(20), 7789–7794 (2006).
   PubMed Web of Science ®Google Scholar
• Lin HK, Wang L, Hu YC, Altuwaijri S, Chang C. Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J.21(15), 4037–4048 (2002).
   PubMed Web of Science ®Google Scholar
• Xu K, Shimelis H, Linn DE et al. Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination. Cancer Cell15(4), 270–282 (2009).
   PubMedGoogle Scholar
• Heemers HV, Tindall DJ. Unraveling the complexities of androgen receptor signaling in prostate cancer cells. Cancer Cell15(4), 245–247 (2009).
   PubMedGoogle Scholar
• Cheng J, Bawa T, Lee P, Gong L, Yeh ET. Role of desumoylation in the development of prostate cancer. Neoplasia8(8), 667–676 (2006).
   PubMed Web of Science ®Google Scholar
• Wu F, Mo YY. Ubiquitin-like protein modifications in prostate and breast cancer. Front. Biosci.12, 700–711 (2007).
   PubMedGoogle Scholar
• Hay RT. SUMO-specific proteases: a twist in the tail. Trends Cell Biol.17(8), 370–376 (2007).
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay D, Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci.32(6), 286–295 (2007).
   PubMed Web of Science ®Google Scholar
• Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Janne OA. Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J. Biol. Chem.274(27), 19441–19446 (1999).
   PubMedGoogle Scholar
• Poukka H, Karvonen U, Janne OA, Palvimo JJ. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl Acad. Sci. USA97(26), 14145–14150 (2000).
   PubMed Web of Science ®Google Scholar
• Callewaert L, Verrijdt G, Haelens A, Claessens F. Differential effect of small ubiquitin-like modifier (SUMO)-ylation of the androgen receptor in the control of cooperativity on selective versus canonical response elements. Mol. Endocrinol.18(6), 1438–1449 (2004).
   PubMedGoogle Scholar
• Kaikkonen S, Jaaskelainen T, Karvonen U et al. SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells. Mol. Endocrinol.23(3), 292–307 (2009).
   PubMedGoogle Scholar
• Bergerat JP, Ceraline J. Pleiotropic functional properties of androgen receptor mutants in prostate cancer. Hum. Mutat.30(2), 145–157 (2009).
   PubMed Web of Science ®Google Scholar
• Tepper CG, Boucher DL, Ryan PE et al. Characterization of a novel androgen receptor mutation in a relapsed CWR22 prostate cancer xenograft and cell line. Cancer Res.62(22), 6606–6614 (2002).
   PubMed Web of Science ®Google Scholar
• Libertini SJ, Tepper CG, Rodriguez V, Asmuth DM, Kung HJ, Mudryj M. Evidence for calpain-mediated androgen receptor cleavage as a mechanism for androgen independence. Cancer Res.67(19), 9001–9005 (2007).
   PubMed Web of Science ®Google Scholar
• Dehm SM, Schmidt LJ, Heemers HV, Vessella RL, Tindall DJ. Splicing of a novel androgen receptor exon generates a constitutively active androgen receptor that mediates prostate cancer therapy resistance. Cancer Res.68(13), 5469–5477 (2008).
   PubMed Web of Science ®Google Scholar
• Hu R, Dunn TA, Wei S et al. Ligand-independent androgen receptor variants derived from splicing of cryptic exons signify hormone-refractory prostate cancer. Cancer Res.69(1), 16–22 (2009).
   PubMed Web of Science ®Google Scholar
• Guo Z, Yang X, Sun F et al. A novel androgen receptor splice variant is up-regulated during prostate cancer progression and promotes androgen depletion-resistant growth. Cancer Res.69(6), 2305–2313 (2009).
   PubMed Web of Science ®Google Scholar
• Lapouge G, Marcias G, Erdmann E et al. Specific properties of a C-terminal truncated androgen receptor detected in hormone refractory prostate cancer. Adv. Exp. Med. Biol.617, 529–534 (2008).
   PubMedGoogle Scholar
• Dehm SM, Regan KM, Schmidt LJ, Tindall DJ. Selective role of an NH2-terminal WxxLF motif for aberrant androgen receptor activation in androgen depletion independent prostate cancer cells. Cancer Res.67(20), 10067–10077 (2007).
   PubMed Web of Science ®Google Scholar
• Dehm SM, Tindall DJ. Ligand-independent androgen receptor activity is activation function-2-independent and resistant to antiandrogens in androgen refractory prostate cancer cells. J. Biol. Chem.281(38), 27882–27893 (2006).
   PubMed Web of Science ®Google Scholar