The Hsp90 inhibitor, 17‐AAG, prevents the ligand‐independent nuclear localization of androgen receptor in refractory prostate cancer cells

Saporita, Anthony J.; Ai, Junkui; Wang, Zhou

doi:10.1002/pros.20541

Cited by 77Prostate Cancer Treatment and ResearchHeat shock proteins researchProstate Cancer Diagnosis and Treatment

The Hsp90 inhibitor, 17‐AAG, prevents the ligand‐independent nuclear localization of androgen receptor in refractory prostate cancer cells

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Saporita, Anthony J., Ai, Junkui, Wang, Zhou·2007·The Prostate

DOI 10.1002/pros.20541PMC PMC2810394

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Abstract

BACKGROUND: Androgen receptor (AR) is the key molecule in androgen‐refractory prostate cancer. Despite androgen ablative conditions, AR remains active and is necessary for the growth of androgen‐refractory prostate cancer cells. Nuclear localization of AR is a prerequisite for its transcriptional activation. We examined AR localization in androgen‐dependent and androgen‐refractory prostate cancer cells. METHODS AND RESULTS: We demonstrate increased nuclear localization of a GFP‐tagged AR in the absence of hormone in androgen‐refractory C4‐2 cells compared to parental androgen‐sensitive human prostate cancer LNCaP cells. Analysis of AR mutants impaired in ligand‐binding indicates that the nuclear localization of AR in C4‐2 cells is truly androgen‐independent. The hsp90 inhibitor, 17‐allylamino‐17‐demethoxygeldanamycin (17‐AAG), inhibits basal PSA expression and disrupts the ligand‐independent nuclear localization of AR at doses much lower than required to inhibit androgen‐induced nuclear import. CONCLUSIONS: Hsp90 is a key regulator of ligand‐independent nuclear localization and activation of AR in androgen‐refractory prostate cancer cells. Prostate 67: 509–520, 2007. © 2007 Wiley‐Liss, Inc.

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High concentrations of 17-AAG inhibit AR by affecting protein stability.
“Other groups have shown that high concentrations of 17-AAG inhibit AR by affecting protein stability (30)”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [30]
17-AAG and FK506 each can inhibit prostate cancer cell growth in culture.
“17-AAG and the immunophilin ligand FK506 each can inhibit prostate cancer cell growth in culture (21, 30).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [30]
The Results report that 17-AAG reduces androgen-receptor nuclear localization and PSA expression in cultured prostate cancer cells, not that it inhibits cell growth. The Discussion explicitly leaves open whether receptor localization is sufficient to drive growth. Searches for growth inhibition, proliferation, and FK506 found no passage establishing the claimed growth effect; the sentence’s other citation may address FK506. (LLM, conf=0.76)
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The development of androgen-independent prostate cancer.
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A New First Step in Activation of Steroid Receptors
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Background
Pharmacodynamic and clinical results from a phase 1/2 study of the HSP90 inhibitor onalespib in combination with abiraterone acetate in prostate cancer.
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Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
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Inhibition of Glycogen Synthase Kinase-3β Counteracts Ligand-Independent Activity of the Androgen Receptor in Castration Resistant Prostate Cancer
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Cytoplasmic localization of the androgen receptor is independent of calreticulin
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“This study suggested that Hsp90 plays a key role in ligand-independent nuclear localization and AR activity in castration-recurrent prostate cancer cells (Saporita et al., 2007).”
BackgroundSelf-citation
A novel androgen receptor antagonist JJ-450 inhibits enzalutamide-resistant mutant ARF876L nuclear import and function
Wu, Z.-Y., Wang, K., Yang, Z.-Y., Pascal, L. E., Nelson, J. B., Takubo, K., Wipf, P., & Wang, Z. (2019) · The Prostate · doi:10.1002/pros.23945 · Cited by 30
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Putting the brakes on continued androgen receptor signaling in castration-resistant prostate cancer
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“Preclinical observations suggested that CRPC might respond favorably to HSP90 inhibitor therapy (Saporita et al., 2007; Tsui et al., 2008; Solit et al., 2002).”
Development and Implementation of a High-Throughput High-Content Screening Assay to Identify Inhibitors of Androgen Receptor Nuclear Localization in Castration-Resistant Prostate Cancer Cells
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“35 As expected, 2GFP-AR was predominantly localized to the nuclei of C4-2 cells cultured in androgen-free media, and exposure to DHT further enhanced that nuclear distribution ( Fig.”
Self-citation
Hsp90 inhibitor 17-AAG inhibits progression of LuCaP35 xenograft prostate tumors to castration resistance
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Sex steroid receptors in skeletal differentiation and epithelial neoplasia: is tissue‐specific intervention possible?
Copland, J. A., Sheffield-Moore, M., Koldzic-Zivanovic, N., Gentry, S., Lamprou, G., Tzortzatou-Stathopoulou, F., Zoumpourlis, V. C., Urban, R., & Vlahopoulos, S. A. (2009) · Bioessays · doi:10.1002/bies.200800138 · Cited by 28 · see citing works
“Physical association with LBD that stabilizes helix 12 in a position favoring coactivators over corepressors, mimics agonist ligand.”
BackgroundInfluential
EAF2 regulates DNA repair through Ku70/Ku80 in the prostate
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Horizon scanning for novel therapeutics for the treatment of prostate cancer
Bianchini, D., Zivi, A., Sandhu, S. K., & Bono, J. S. D. (2010) · Annals of Oncology · doi:10.1093/annonc/mdq369 · Cited by 24 · see citing works
Hybrid Enzalutamide Derivatives with Histone Deacetylase Inhibitor Activity Decrease Heat Shock Protein 90 and Androgen Receptor Levels and Inhibit Viability in Enzalutamide-Resistant C4-2 Prostate Cancer Cells
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“In PCa cells, HSP90 inhibitors induce AR degradation and impair AR nuclear translocation while simultaneously reducing the levels of other oncogenic client proteins, such as p-AKT/AKT, EGFR and IGF-IR and survivin (He et al., 2013; Liu et al., 2015; Saporita et al., 2007; Solit et al., 2002).”
Background
High-Content Positional Biosensor Screening Assay for Compounds to Prevent or Disrupt Androgen Receptor and Transcriptional Intermediary Factor 2 Protein–Protein Interactions
Hua, Y., Tong, Y.-S., Strock, C., & Johnston, P. (2014) · Assay and drug development technologies · doi:10.1089/adt.2014.594 · Cited by 20 · see citing works
“6).(6,37) Exposure to DHT and biclautamide, but not to flutamide or 17-AAG, induced a concentration-dependent increase in the mean fluorescent intensity of AR-RFP in TIF2-GFP-positive nucleoli (Fig.”
Background
Identification of molecular candidates and interaction networks via integrative toxicogenomic analysis in a human cell line following low-dose exposure to the carcinogenic metals cadmium and nickel.
Kwon, J., Weon, J., Koedrith, P., Park, K.-S., Kim, I., & Seo, Y. (2013) · Oncology Report · doi:10.3892/or.2013.2587 · Cited by 20
“A number of these client proteins have been causally implicated in the pathogenesis of prostate cancer, including AR, HER2, AKT and RAF1 (54-56).”
Background
Conditional deletion of ELL2 induces murine prostate intraepithelial neoplasia
Pascal, L. E., Masoodi, K. Z., Liu, J., Qiu, X., Song, Q., Wang, Y.-J., Zang, Y.-C., Yang, T.-J., Wang, Y., Rigatti, L. H., et al. (2017) · Journal of Endocrinology · doi:10.1530/joe-17-0112 · Cited by 16 · see citing works
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17-ABAG, a novel geldanamycin derivative, inhibits LNCaP-cell proliferation through heat shock protein 90 inhibition
Lin, Z.-Y., Peng, R., Li, Z.-Y., Wang, Y., Lu, C.-H., Shen, Y.-M., Wang, J., & Shi, G.-W. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2239 · Cited by 16
“Previous studies have demonstrated that in prostate cancer, Hsp90 regulates the nuclear localization and activation of ARs (5,32,33), which have a key role in prostate carcinogenesis and progression (34,35).”
A Novel Mechanism for Cross-Adaptation between Heat and Altitude Acclimation: The Role of Heat Shock Protein 90
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“Hsp90 inhibition by 17-AAG may influence the N/C interaction via the LBD, because Hsp90 can bind to the LBD (8).”
BackgroundInfluentialSelf-citation
Tumor suppressor REIC/DKK-3 and co-chaperone SGTA: Their interaction and roles in the androgen sensitivity
Ochiai, K., Morimatsu, M., Kato, Y., Ishiguro-Oonuma, T., Udagawa, C., Rungsuriyawiboon, O., Azakami, D., Michishita, M., Ariyoshi, Y., Ueki, H., et al. (2015) · OncoTarget · doi:10.18632/oncotarget.6488 · Cited by 12
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Method
Capillarisin blocks prostate‐specific antigen expression on activation of androgen receptor in prostate carcinoma cells
Tsui, K.-H., Chang, Y.-L., Feng, T.-H., Hou, C.-P., Lin, Y.-H., Yang, P.-S., Lee, B.-W., & Juang, H. (2018) · The Prostate · doi:10.1002/pros.23463 · Cited by 11 · see citing works
Reconfiguring the AR-TIF2 Protein–Protein Interaction HCS Assay in Prostate Cancer Cells and Characterizing the Hits from a LOPAC Screen
Fancher, A. T., Hua, Y., Camarco, D. P., Close, D. A., Strock, C. J., & Johnston, P. A. (2016) · Assay and drug development technologies · doi:10.1089/adt.2016.741 · Cited by 11 · see citing works
“The AR-GFP nuclear localization HCS assay was designed to identify compounds that altered the sub-cellular distribution and/or expression of AR-GFP.47 eThe % inhibition data for the AR-TIF2 PPI LOPAC hits in the Dex-induced GR nuclear translocation assay were extracted by querying our HTS database.”
N-terminal domain of the androgen receptor contains a region that can promote cytoplasmic localization
Dar, J. A., Eisermann, K., Masoodi, K. Z., Ai, J., Wang, D., Severance, T. S., Sampath-Kumar, S. D., & Wang, Z. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.09.013 · Cited by 10 · see citing works
Self-citation
Perspectives on designs of antiandrogens for prostate cancer
Estébanez‐Perpiñá, E., Jouravel, N., & Fletterick, R. J. (2007) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2.10.1341 · Cited by 12 · see citing works
“With androgens still available for AR activation, more efficient use of active AR might be achieved in cancer cells through overexpression of co-activators [61] , DNA amplification [63] , delayed AR degradation [64] or localization of AR in the nucleus [65] .”
Background
Heat shock protein 90 is associated with hyperplasia and neoplastic transformation of canine prostatic epithelial cells.
Palmieri, C., Mancini, M., Benazzi, C., & Salda, L. D. (2014) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2014.01.006 · Cited by 10 · see citing works
“Saporita et al. (2007) have demonstrated that a geldanamycin derivative, 17-AAG, can prevent the ligand-independent nuclear localization of AR in C4-2 cells, a model for androgen-refractory prostate cancer cells, partially restoring androgen-dependent regulation of AR and thus potentially providing…”
Background
The Role of Foxa Proteins in the Regulation of Androgen Receptor Activity
DeGraff, D., Yu, X.-P., Sun, Q., Mirosevich, J., Jin, R., Wang, Y., Gupta, A., Nandana, S., Case, T., Paul, M., et al. (2009) · Springer eBooks · doi:10.1007/978-0-387-69179-4_25 · Cited by 9 · see citing works
“While the nuclear translocation of AR is normally ligand dependent, androgen-insensitive prostate cancer cells display high levels of nuclear AR even in the absence of androgen ( Saporita et al. 2007 ).”
Background
High-Content Screening Campaign to Identify Compounds That Inhibit or Disrupt Androgen Receptor-Transcriptional Intermediary Factor 2 Protein-Protein Interactions for the Treatment of Prostate Cancer
Fancher, A. T., Hua, Y., Camarco, D. P., Close, D. A., Strock, C., & Johnston, P. (2018) · Assay and drug development technologies · doi:10.1089/adt.2018.858 · Cited by 8 · see citing works
Androgen metabolism in castration-resistant prostate cancer
Koltai, T., Reshkin, S. J., Baltazar, F., & Fliegel, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-90528-2.00003-5
Chemical and biological evaluation of the Plumbago Zeylanica plant against prostate cancer. A unified approach combining molecular docking, dynamic simulations, pharmacophore modeling, DFT and ADMET studies
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NXP800 Activates the Unfolded Protein Response, Altering AR and E2F Function to Impact Castration-Resistant Prostate Cancer Growth
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Background
RETRACTED: Horizon scanning for novel therapeutics for the treatment of prostate cancer
Bianchini, D., Zivi, A., Sandhu, S. K., & Bono, J. S. D. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2010.514261 · Cited by 6 · see citing works
Retracted
Insights from AR Gene Mutations
Buchanan, G., Need, E. F., Bianco‐Miotto, T., Greenberg, N. M., Scher, H. I., Centenera, M. M., Butler, L. M., Robins, D. M., & Tilley, W. D. (2009) · Springer eBooks · doi:10.1007/978-0-387-69179-4_10 · Cited by 4 · see citing works
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“Both testosterone and DHT bind to the cytoplasmic AR, which in its inactive state is complexed with molecular chaper-ones—most notably heat shock protein 90 (Hsp90), heat shock protein 70 (Hsp70), and Prostaglandin E Synthase 3 (p23) [83].”
Growth arrest and DNA‐damage‐inducible 45 beta (GADD45&bgr;) deletion suppresses testosterone‐induced prostate hyperplasia in mice
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“8 [00 ; 14] [15 ; 49] [50 ; 64] [65 ; 74] [75 ; 84] [85 ; ++] Total”

Authors: Saporita, A. J., Ai, J., & Wang, Z.
Affiliations: Northwestern University (US)
Corresponding author: Wang, Zhou
ORCID: Wang, Zhou
Venue: The Prostate
Publisher: Wiley
Published: 2007-01-12
Volume: 67
Issue: 5
Pages: 509-520
ISSN: 0270-4137 (ISSN-L)
1097-0045
DOI: 10.1002/pros.20541
PMC: PMC2810394
OpenAlex: W2081963757
Cited by: 77
References: 0
Citations by year: 2026: 1 · 2025: 3 · 2023: 2 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 6 · 2014: 8 · 2013: 8 · 2012: 3
FWCI: 5.76
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The Prostate (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
Robert H. Lurie Comprehensive Cancer Center
National Cancer Institute (R01CA108675, P50CA090386, T32 CA80621, T32CA080621, 1P50 CA90386)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK051193, 5 R01 DK51993)
Topics: Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Diagnosis and Treatment
Keywords: androgen receptor, HSP90, 17-AAG, geldanamycin, androgen-refractory prostate cancer, nuclear import, prostate-specific antigen, C4-2 cells, LNCaP cells, Hsp90 inhibitors
MeSH terms: Cell Nucleus, Humans, Ligands, Male, Neoplasms, Hormone-Dependent, Prostatic Neoplasms, Receptors, Androgen, RNA, Neoplasm, Transcription, Genetic, Transfection, Blotting, Northern, Blotting, Western, Benzoquinones, Prostate-Specific Antigen, HSP90 Heat-Shock Proteins, Cell Line, Tumor, Lactams, Macrocyclic

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The Hsp90 inhibitor, 17‐AAG, prevents the ligand‐independent nuclear localization of androgen receptor in refractory prostate cancer cells

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