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Titolo:
PURIFICATION AND MOLECULAR-CLONING OF A SECRETED, FRIZZLED-RELATED ANTAGONIST OF WNT ACTION
Autore:
FINCH PW; HE X; KELLEY MJ; UREN A; SCHAUDIES RP; POPESCU NC; RUDIKOFF S; AARONSON SA; VARMUS HE; RUBIN JS;
Indirizzi:
NCI,CELLULAR & MOL BIOL LAB,MED SCI CTR 4255,BLDG 37,ROOM 1E24,37 CONVENT DR BETHESDA MD 20892 NCI,CELLULAR & MOL BIOL LAB,MED SCI CTR 4255 BETHESDA MD 20892 NCI,VARMUS LAB BETHESDA MD 20892 NCI,MED BRANCH BETHESDA MD 20892 NCI,EXPT CARCINOGENESIS LAB BETHESDA MD 20892 NCI,GENET LAB BETHESDA MD 20892 MT SINAI MED CTR,DERALD H RUTTENBERG CANC CTR NEW YORK NY 10029
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 13, volume: 94, anno: 1997,
pagine: 6770 - 6775
SICI:
0027-8424(1997)94:13<6770:PAMOAS>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPATOCYTE GROWTH-FACTOR; MAMMARY ONCOGENE INT-1; XENOPUS-EMBRYOS; EPITHELIAL-CELLS; DROSOPHILA; POLARITY; GENE; EXPRESSION; PROTOONCOGENE; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
P.W. Finch et al., "PURIFICATION AND MOLECULAR-CLONING OF A SECRETED, FRIZZLED-RELATED ANTAGONIST OF WNT ACTION", Proceedings of the National Academy of Sciences of the United Statesof America, 94(13), 1997, pp. 6770-6775

Abstract

Frizzled polypeptides are integral membrane proteins that recently were shown to function as receptors for Wnt signaling molecules, Were, me report the identification of a novel, secreted 36-kDa protein that contains a region homologous to a putative Wnt-binding domain of Frizzleds. This protein, called Frizzled-related, protein (FRP), was first identified as a heparin-binding polypeptide that copurified with hepatocyte growth factor/scatter factor in conditioned medium from a human embryonic lung fibroblast line, Degenerate oligonucleotides, based on the NH2-terminal sequence of the purified protein, were used to isolatecorresponding cDNA clones. These encoded a 313-amino acid polypeptide, containing a cysteine-rich domain of approximate to 110 residues that was 30-40% identical to the putative ligand-binding domain of Frizzled proteins, A 4.4-kb transcript of the FRP gene is present in many organs, both in the adult and during embryogenesis, and homologs of the gene are detectable in DNA from several vertebrate species, In biosynthetic studies, FRP was secreted but, like Wnts, tended to remain associated with cells, When coexpressed with several Wnt family members in early Xenopus embryos, FRP antagonized Wnt-dependent duplication of the embryonic dorsal asis. These results indicate that FRP may function as an inhibitor of Wnt action during development and in the adult.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:48:51