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Titolo:
Mutations at the boundary of the hinge and ligand binding domain of the androgen receptor confer increased transactivation function
Autore:
Buchanan, G; Yang, MO; Harris, JM; Nahm, HS; Han, GZ; Moore, N; Bentel, JM; Matusik, RJ; Horsfall, DJ; Marshall, VR; Greenberg, NM; Tilley, WD;
Indirizzi:
Flinders Univ S Australia, Med Ctr, Flinders Canc Ctr, Adelaide, SA 5042, Australia Flinders Univ S Australia Adelaide SA Australia 5042 , SA 5042, Australia Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia Univ Queensland Brisbane Qld Australia 4072 Brisbane, Qld 4072, Australia Baylor Coll Med, Dept Cell Biol, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ept Cell Biol, Houston, TX 77030 USA Baylor Coll Med, Dept Med, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Med, Dept Med, Houston, TX 77030 USA Vanderbilt Univ, Ctr Canc, Dept Cell Biol, Nashville, TN 37232 USA Vanderbilt Univ Nashville TN USA 37232 Cell Biol, Nashville, TN 37232 USA
Titolo Testata:
MOLECULAR ENDOCRINOLOGY
fascicolo: 1, volume: 15, anno: 2001,
pagine: 46 - 56
SICI:
0888-8809(200101)15:1<46:MATBOT>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDEPENDENT PROSTATE-CANCER; TRANSCRIPTIONAL COACTIVATOR; STEROID-RECEPTORS; CO-REPRESSOR; LNCAP CELLS; GENE; INTERACTS; PROTEIN; GRIP1; PROGESTERONE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Tilley, WD Flinders Univ S Australia, Med Ctr, Flinders Canc Ctr, Adelaide, SA 5042, Australia Flinders Univ S Australia Adelaide SA Australia 5042 Australia
Citazione:
G. Buchanan et al., "Mutations at the boundary of the hinge and ligand binding domain of the androgen receptor confer increased transactivation function", MOL ENDOCR, 15(1), 2001, pp. 46-56

Abstract

The androgen receptor (AR), a member of the steroid receptor superfamily of nuclear transcription factors, mediates androgen signaling in diverse target tissues. Here we report AR gene mutations identified in human prostate cancer and the autochthonous transgenic adenocarcinoma of the mouse prostate model that colocate to residues (668)QPIF(671) at the boundary of the hinge and ligand-binding domain, resulting in receptors that exhibit 2- to 4-fold increased activity compared with wildtype AR in response to dihydrotestosterone, estradiol, progesterone, adrenal androgens, and the AR antagonist, hydroxyflutamide, without an apparent effect on receptor levels, ligand binding kinetics, or DNA binding. The expression of these or similar variants could explain the emergence of hormone refractory disease in a subset of patients. Homology modeling indicates that amino acid residues (668)QPIF(671) form a ridge bordering a potential protein-protein interaction surface. The naturally occurring AR gene mutations reported in this study result in decreased hydrophobicity of this surface, suggesting that altered receptor-protein interaction mediates the precocious activity of the AR variants.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 17:40:49