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Titolo:
Heat shock protein 90 and the nuclear transport of progesterone receptor
Autore:
Haverinen, M; Passinen, S; Syvala, H; Pasanen, S; Manninen, T; Tuohimaa, P; Ylikomi, T;
Indirizzi:
Univ Tampere, Grad Sch Biosci, Dept Cell Biol, Tampere 33014, Finland UnivTampere Tampere Finland 33014 ept Cell Biol, Tampere 33014, Finland Univ Tampere, Sch Med, Dept Anat, Tampere 33014, Finland Univ Tampere Tampere Finland 33014 ed, Dept Anat, Tampere 33014, Finland Tampere Univ Hosp, Dept Clin Chem, Tampere 33521, Finland Tampere Univ Hosp Tampere Finland 33521 lin Chem, Tampere 33521, Finland
Titolo Testata:
CELL STRESS & CHAPERONES
fascicolo: 3, volume: 6, anno: 2001,
pagine: 256 - 262
SICI:
1355-8145(200107)6:3<256:HSP9AT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND-BINDING DOMAIN; LARGE TUMOR-ANTIGEN; GLUCOCORTICOID RECEPTOR; STEROID-RECEPTORS; ESTROGEN-RECEPTOR; DNA-BINDING; IN-VIVO; MONOCLONAL-ANTIBODIES; MAMMALIAN-CELLS; CHICKEN OVIDUCT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Ylikomi, T Univ Tampere, Grad Sch Biosci, Dept Cell Biol, Tampere 33014, Finland Univ Tampere Tampere Finland 33014 ol, Tampere 33014, Finland
Citazione:
M. Haverinen et al., "Heat shock protein 90 and the nuclear transport of progesterone receptor", CELL STR CH, 6(3), 2001, pp. 256-262

Abstract

Steroid receptors exist as large oligomeric complexes in hypotonic cell extracts. In the present work, we studied the nuclear transport of the 2 major components of the oligomeric complex, the receptor itself and the heat shock protein 90 (Hsp90), by using different in vitro transport systems: digitonin permeabilized cells and purified nuclei. We demonstrate that the stabilized oligomeric complex of progesterone receptor (PR) cannot be transported into the nucleus and that unliganded PR salt dissociated from Hsp90 is transported into the nucleus. When nonstabilized PR oligomer was introduced into the nuclear transport system, the complex dissociated and the PR but not the Hsp90 was transported into the nucleus. If PR exists as an oligomeric form after synthesis, as suggested by the experiments with reticulocyte lysate, the present results suggest that the complex is short-lived and is dissociated before or during nuclear transport. Thus, the role of Hsp90 in PR action is likely to reside in the Hsp90-assisted chaperoning process of PR preceding nuclear transport of the receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:04:15