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Titolo:
Identification and characterization of membrane estrogen receptor from MCF7 estrogen-target cells
Autore:
Powell, CE; Soto, AM; Sonnenschein, C;
Indirizzi:
Tufts Univ, Sch Med, Dept Anat & Cellular Biol, Boston, MA 02111 USA TuftsUniv Boston MA USA 02111 Anat & Cellular Biol, Boston, MA 02111 USA
Titolo Testata:
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 2-3, volume: 77, anno: 2001,
pagine: 97 - 108
SICI:
0960-0760(200105)77:2-3<97:IACOME>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-BREAST-CANCER; PITUITARY-TUMOR CELLS; S-49 LYMPHOMA-CELLS; PLASMA-MEMBRANE; GLUCOCORTICOID RECEPTOR; GROWTH-REGULATION; NEGATIVE CONTROL; ESTROCOLYONE-I; BINDING-SITES; RAT PITUITARY;
Keywords:
membrane estrogen receptor; cell proliferation; MCF7 cells; growth inhibitors; cell division; growth inhibition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Sonnenschein, C Tufts Univ, Sch Med, Dept Anat & Cellular Biol, 136 Harrison Ave, Boston, MA 02111 USA Tufts Univ 136 Harrison Ave Boston MA USA 02111 02111 USA
Citazione:
C.E. Powell et al., "Identification and characterization of membrane estrogen receptor from MCF7 estrogen-target cells", J STEROID B, 77(2-3), 2001, pp. 97-108

Abstract

Estrogens control the proliferation of estrogen-target cells through a receptor mediated pathway. We have recently presented evidence that estradiol cancels the proliferative inhibition exerted by albumin on estrogen-target cells (indirect-negative hypothesis). We postulate that this mechanism requires the presence of a membrane estrogen receptor (mER)-membrane albumin receptor complex. Confirmation for mER alpha in MCF7 cells is now made using both the C542 monoclonal and ER-21 polyclonal antibodies (Ab)s specific forER alpha. Western blot analysis of purified membrane proteins with ER alpha Abs revealed multiple high M, mERs (92 k. 110 k, and 130 k M,), as well as a 67 k M, mER; immunoreactive proteins were competed by inclusion of 500-fold molar excess C542 peptide. Ligand blot analysis of similar extracts with estradiol-peroxidase identified several potential mERs as well; two of these proteins were also recognized by C542 and ER-21 Abs (110 and 67 k M,). Fluorescence. confocal and electron microscopy of MCF7 cells fixed in 2.0%paraformaldehyde/0.1% glutaraldehyde identified specific mER I sites by immunocytochemistry. Specific binding of H-3-17 beta -estradiol was reduced by a 200-fold molar excess of unlabeled 17 beta -estradiol, but not by testosterone and progesterone. These results suggest that the ER on the plasma membrane of MCF7 cells is similar, but not identical to its intracellular counterpart. We propose that the observed mER actively participates in the estrogen-mediated proliferation of MCF7 cells. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 03:47:59