Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INVOLVEMENT OF PP60(C-SRC) WITH 2 MAJOR SIGNALING PATHWAYS IN HUMAN BREAST-CANCER
Autore:
LUTTRELL DK; LEE A; LANSING TJ; CROSBY RM; JUNG KD; WILLARD D; LUTHER M; RODRIGUEZ M; BERMAN J; GILMER TM;
Indirizzi:
GLAXO RES INST,DEPT CELL BIOL,5 MOORE DR RES TRIANGLE PK NC 27709 GLAXO RES INST,DEPT BIOTECHNOL RES TRIANGLE PK NC 27709 GLAXO RES INST,DEPT MED CHEM RES TRIANGLE PK NC 27709
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 1, volume: 91, anno: 1994,
pagine: 83 - 87
SICI:
0027-8424(1994)91:1<83:IOPW2M>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; FACTOR-RECEPTOR GENE; C-SRC; MITOGENIC RESPONSIVENESS; CARBOXYL TERMINUS; TYROSINE KINASES; NEU ONCOGENE; EGF RECEPTOR; PP60C-SRC; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
D.K. Luttrell et al., "INVOLVEMENT OF PP60(C-SRC) WITH 2 MAJOR SIGNALING PATHWAYS IN HUMAN BREAST-CANCER", Proceedings of the National Academy of Sciences of the United Statesof America, 91(1), 1994, pp. 83-87

Abstract

The phosphotyrosine residues of receptor tyrosine kinases serve as unique binding sites for proteins involved in intracellular signaling, which contain SRC homology 2 (SH2) domains. Since overexpression or activation of the pp60c-src kinase has been reported in a number of humantumors, including primary human breast carcinomas, we examined the interactions of the SH2 and SH3 domains of human SRC with target proteins in human carcinoma cell lines. Glutathione S-transferase fusion proteins containing either the SH2, SH3, or the entire SH3/SH2 region of human SRC were used to affinity purify tyrosine-phosphorylated proteinsfrom human breast carcinoma cell lines. We show here that in human breast carcinoma cell lines, the SRC SH2 domain binds to activated epidermal growth factor receptor (EGFR) and p185HER2/neu. SRC SH2 binding to EGFR was also observed in a nontumorigenic cell line after hormone stimulation. Endogenous pp60c-src was found to tightly associate with tyrosine-phosphorylated EGFR. Association of the SRC SH2 with the EGFR was blocked by tyrosyl phosphopeptides containing the sequences surrounding tyrosine-530, the regulatory site in the SRC C terminus, or sequences surrounding the major sites of autophosphorylation in the EGFR. These results raise the possibility that association of pp60c-src withthese receptor tyrosine kinases is an integral part of the signaling events mediated by these receptors and may contribute to malignant transformation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 02:49:31