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Titolo:
MULTIPLE ISOFORMS OF THE ESTROGEN-RECEPTOR IN ENDOMETRIAL CANCER
Autore:
MARSIGLIANTE S; MUSCELLA A; CIARDO V; PUDDEFOOT JR; LEO G; VINSON GP; STORELLI C;
Indirizzi:
UNIV LECCE,DIPARTIMENTO BIOL,FISIOL LAB,VIA PROV MONTERONI I-73100 LECCE ITALY UNIV LONDON QUEEN MARY & WESTFIELD COLL,FAC BASIC MED SCI,DEPT BIOCHEM LONDON E1 4NS ENGLAND OSPED V FAZZI,ANAL CLIN LAB LECCE ITALY
Titolo Testata:
Journal of molecular endocrinology
fascicolo: 3, volume: 14, anno: 1995,
pagine: 365 - 374
SICI:
0952-5041(1995)14:3<365:MIOTEI>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ESTROGEN-RECEPTOR; HUMAN-BREAST-CANCER; PROGESTERONE RECEPTORS; IMMUNOHISTOCHEMICAL EVALUATION; ESTRADIOL RECEPTORS; STEROID-RECEPTORS; CYTOSOL ESTROGEN; HORMONE BINDING; CARCINOMA; SAMPLES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
S. Marsigliante et al., "MULTIPLE ISOFORMS OF THE ESTROGEN-RECEPTOR IN ENDOMETRIAL CANCER", Journal of molecular endocrinology, 14(3), 1995, pp. 365-374

Abstract

We evaluated the presence and variability of oestrogen receptor (ER) isoforms in endometrial cancer by using [H-3]oestradiol-labelled ERs and the H222 monoclonal antibody obtained from the Abbott enzyme immunoassay kit. Using isoelectric focusing (IEF), endometrial ER was shown to be composed of four different species, with pI values of 6.1, 6.3, 6.6 and 6.8, indistinguishable from the isoforms found in normal rat uterus, and human breast and larynx carcinomas. The isoforms at pI 6.3,6.6 and 6.8, all sedimenting at 4S by sucrose gradient fractionation,showed, on two-dimensional SDS electrophoresis, relative masses of 50, 70 and 65 kDa respectively, equal to the masses previously found in breast cancer. These isoforms did not alter their pi values during IEFfractionation performed in a linear gradient of urea, while the pi 6.1, sedimenting at 8S, generated a new isoform at about 9 mol/l urea with pi 7.2 and a relative mass of 65 kDa. The urea-dissociated isoform (pi 7.2) was able approximately to double the antibody binding with respect to the non-dissociated oligomer, which suggested that some epitopes are 'masked', i.e. not accessible to the antibodies when ER is present in its complexed form. The evidence thus suggested that the oligomer at pi 6.1 contained a single 65 kDa ER form which, as a monomer, focused at pI 7.2. The variability in the ER isoform profile found in endometrial cancer was similar to the variability previously reported in breast and larynx carcinomas. The balance between these isoforms could be a dynamic parameter involved in the functionality of this receptor and consequently in cell transformation.

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Documento generato il 18/09/20 alle ore 19:51:27