Literature DB >> 20230007

Effect of anabolic-androgenic steroids and glucocorticoids on the kinetics of hAR and hGR nucleocytoplasmic translocation.

Amy B Cadwallader1, Douglas E Rollins, Carol S Lim.   

Abstract

Although the qualitative nucleocytoplasmic transport of nuclear hormone receptors (NHRs) has been studied, there is little documentation of the cellular kinetics of this transport. Here, translocation studies using the human androgen receptor (hAR) and the human glucocorticoid receptor (hGR) were performed to aid in identifying the mechanism by which anabolic-androgenic steroids (AAS) were activating hAR and potentially interacting with hGR and how glucocorticoid ligands were interacting with the hGR and hAR. The real-time analysis of EGFP-labeled hAR and hGR ligand-induced cytoplasm-to-nucleus translocation was performed using fluorescence microscopy to better understand the action of these NHRs in a physiologically relevant cell-based model. After transient transfection, the hAR and hGR individually translocate as expected (i.e., transport is ligand-induced and dose-dependent) in this model biological system. Testosterone (TEST) had the fastest translocation rate for the hAR of 0.0525 min(-1). The other endogenous steroids, androstenedione (ANE) and dihydrotestosterone (DHT), had considerably lower hAR transport rates. The rates of hAR transport for the exogenous steroids methyltrienelone (MET), nandrolone (NAN), and oxandrolone (OXA) are lower than that of testosterone and similar to those of the endogenous steroids ANE and DHT. The hGR transport rates for cortisol (COR) and dexamethasone (DEX) are also presented. The synthetic GC, DEX, had a more rapid translocation rate (0.1599 min(-1)) at the highest dose of 100 nM compared to the endogenous GC COR (0.0431 min(-1)). The data obtained agrees with the existing qualitative data and adds an important ligand-dependent kinetic component to hAR and hGR transport. These kinetic data can aid our understanding of NHR action and interaction with other regulatory proteins, and can be useful in the development of new therapies.

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Year:  2010        PMID: 20230007      PMCID: PMC2882525          DOI: 10.1021/mp900259w

Source DB:  PubMed          Journal:  Mol Pharm        ISSN: 1543-8384            Impact factor:   4.939


  47 in total

Review 1.  Subcellular steroid/nuclear receptor dynamics.

Authors:  M Kawata
Journal:  Arch Histol Cytol       Date:  2001-10

2.  The presence of both the amino- and carboxyl-terminal domains in the AR is essential for the completion of a transcriptionally active form with coactivators and intranuclear compartmentalization common to the steroid hormone receptors: a three-dimensional imaging study.

Authors:  Masayuki Saitoh; Ryoichi Takayanagi; Kiminobu Goto; Akiyoshi Fukamizu; Arihiro Tomura; Toshihiko Yanase; Hajime Nawata
Journal:  Mol Endocrinol       Date:  2002-04

3.  Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells.

Authors:  R K Tyagi; Y Lavrovsky; S C Ahn; C S Song; B Chatterjee; A K Roy
Journal:  Mol Endocrinol       Date:  2000-08

4.  Dynamic changes in subcellular localization of mineralocorticoid receptor in living cells: in comparison with glucocorticoid receptor using dual-color labeling with green fluorescent protein spectral variants.

Authors:  M Nishi; H Ogawa; T Ito; K I Matsuda; M Kawata
Journal:  Mol Endocrinol       Date:  2001-07

5.  Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces.

Authors:  J G Savory; G G Préfontaine; C Lamprecht; M Liao; R F Walther; Y A Lefebvre; R J Haché
Journal:  Mol Cell Biol       Date:  2001-02       Impact factor: 4.272

6.  Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor.

Authors:  V Georget; J M Lobaccaro; B Terouanne; P Mangeat; J C Nicolas; C Sultan
Journal:  Mol Cell Endocrinol       Date:  1997-04-25       Impact factor: 4.102

7.  Structure/function of the human glucocorticoid receptor: tyrosine 735 is important for transactivation.

Authors:  D W Ray; C S Suen; A Brass; J Soden; A White
Journal:  Mol Endocrinol       Date:  1999-11

8.  The subnuclear three-dimensional image analysis of androgen receptor fused to green fluorescence protein.

Authors:  A Tomura; K Goto; H Morinaga; M Nomura; T Okabe; T Yanase; R Takayanagi; H Nawata
Journal:  J Biol Chem       Date:  2001-05-21       Impact factor: 5.157

9.  Temporally distinct and ligand-specific recruitment of nuclear receptor-interacting peptides and cofactors to subnuclear domains containing the estrogen receptor.

Authors:  F Schaufele; C Y Chang; W Liu; J D Baxter; S K Nordeen; Y Wan; R N Day; D P McDonnell
Journal:  Mol Endocrinol       Date:  2000-12

10.  A glucocorticoid-responsive mutant androgen receptor exhibits unique ligand specificity: therapeutic implications for androgen-independent prostate cancer.

Authors:  Aruna V Krishnan; Xiao-Yan Zhao; Srilatha Swami; Lars Brive; Donna M Peehl; Kathryn R Ely; David Feldman
Journal:  Endocrinology       Date:  2002-05       Impact factor: 4.736

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  2 in total

Review 1.  The androgen receptor and its use in biological assays: looking toward effect-based testing and its applications.

Authors:  Amy B Cadwallader; Carol S Lim; Douglas E Rollins; Francesco Botrè
Journal:  J Anal Toxicol       Date:  2011-11       Impact factor: 3.367

2.  Role of androgens in dhea-induced rack1 expression and cytokine modulation in monocytes.

Authors:  Emanuela Corsini; Valentina Galbiati; Angela Papale; Elena Kummer; Antonella Pinto; Melania M Serafini; Antonio Guaita; Roberto Spezzano; Donatella Caruso; Marina Marinovich; Marco Racchi
Journal:  Immun Ageing       Date:  2016-05-29       Impact factor: 6.400

  2 in total

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