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Titolo:
ACTIVITY OF WNT-1 AS A TRANSMEMBRANE PROTEIN
Autore:
PARKIN NT; KITAJEWSKI J; VARMUS HE;
Indirizzi:
AVIRON,1450 ROLLINS RD BURLINGAME CA 94010 UNIV CALIF SAN FRANCISCO,DEPT MICROBIOL & IMMUNOL SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143 COLUMBIA UNIV COLL PHYS & SURG,CTR REPROD SCI,DEPT PATHOL NEW YORK NY10032
Titolo Testata:
Genes & development
fascicolo: 11, volume: 7, anno: 1993,
pagine: 2181 - 2193
SICI:
0890-9369(1993)7:11<2181:AOWAAT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR PRECURSOR; MAMMARY ONCOGENE INT-1; EPITHELIAL-CELL LINE; DROSOPHILA EMBRYO; XENOPUS EMBRYOS; KIT LIGAND; SIGNAL TRANSDUCTION; WINGLESS PROTEIN; EXPRESSION; GENE;
Keywords:
WNT-1; TRANSMEMBRANE PROTEIN; TRANSFORMATION; MAMMARY ONCOGENE; CD4; CD8;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
70
Recensione:
Indirizzi per estratti:
Citazione:
N.T. Parkin et al., "ACTIVITY OF WNT-1 AS A TRANSMEMBRANE PROTEIN", Genes & development, 7(11), 1993, pp. 2181-2193

Abstract

The product of the Wnt-1 proto-oncogene is a cysteine-rich glycoprotein that plays a crucial role in the development of the vertebrate central nervous system. Wnt-1 protein is secreted but remains associated with the cell surface and extracellular matrix. The function of Wnt-1 in several different biological settings can be carried out by cells that receive the Wnt signal from adjacent cells. Ectopic expression of Wnt-1 in certain mammary gland cell lines, such as C57MG, causes morphological transformation; C57MG cells can also be transformed by a paracrine mechanism when mixed with other cell types secreting Wnt-1 protein. To ask whether Wnt-1 protein can function while bound to the cell of origin, a variety of cell types were programmed to produce chimeric proteins containing the complete sequence of mature Wnt-1 protein fused to part or all of the transmembrane protein CD4 or CD8. The chimeraswere found at the cell surface of transfected cells and did not appear to be proteolytically processed. In autocrine and paracrine transformation assays with C57MG cells and in an axis induction assay in Xenopus laevis embryos, the Wnt-1/CD4 or CD8 fusions retained significant activity, as did a secreted chimera containing the CD8 extracellular domain but lacking the transmembrane domain. However, a chimera lacking a spacer between the Wnt-1 and the transmembrane domains was weakly active and only in autocrine transformation. These results show that tethering Wnt-1 to the cell surface still allows Wnt-1-mediated cell-to-cell signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/10/20 alle ore 03:34:07