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Titolo:
SUBCELLULAR-LOCALIZATION AND BIOLOGICAL-ACTIVITY OF MR-18,000 BASIC FIBROBLAST GROWTH-FACTOR - SITE-DIRECTED MUTAGENESIS OF A PUTATIVE NUCLEAR TRANSLOCATION SEQUENCE
Autore:
PRESTA M; GUALANDRIS A; URBINATI C; RUSNATI M; COLTRINI D; ISACCHI A; CACCIA P; BERGONZONI L;
Indirizzi:
UNIV BRESCIA,SCH MED,DEPT BIOMED SCI,VIA VALSABBINA 19 I-25123 BRESCIA ITALY UNIV BRESCIA,SCH MED,DEPT BIOMED SCI & BIOTECHNOL,GEN PATHOL & IMMUNOL UNIT I-25123 BRESCIA ITALY FARMITALIA CARLO ERBA SPA,DEPT BIOTECHNOL I-20014 NERVIANO ITALY
Titolo Testata:
Growth factors
fascicolo: 4, volume: 9, anno: 1993,
pagine: 269 - 278
SICI:
0897-7194(1993)9:4<269:SABOMB>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
AORTIC ENDOTHELIAL-CELLS; PLASMINOGEN-ACTIVATOR PRODUCTION; PROTEIN-KINASE-C; HEPARIN-BINDING; MITOGENIC ACTIVITY; RECEPTOR-BINDING; POINT MUTATION; DNA-SYNTHESIS; BFGF; FGF;
Keywords:
FIBROBLAST GROWTH FACTOR; NUCLEUS; PLASMINOGEN ACTIVATOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M. Presta et al., "SUBCELLULAR-LOCALIZATION AND BIOLOGICAL-ACTIVITY OF MR-18,000 BASIC FIBROBLAST GROWTH-FACTOR - SITE-DIRECTED MUTAGENESIS OF A PUTATIVE NUCLEAR TRANSLOCATION SEQUENCE", Growth factors, 9(4), 1993, pp. 269-278

Abstract

Residues 27-31 (Lys-Asp-Pro-Lys-Arg) of the 155-amino acid form of basic fibroblast growth factor (bGF) are in good agreement with a consensus sequence for nuclear translocation. To evaluate the role of this sequence in mediating the intracellular localization and biological activity of bFGF, basic residues Lys-27, Lys-30, and Arg-31 were changed to neutral glutamine residues by site-directed mutagenesis of the human bFGF cDNA. The bFGF mutant (M1Q-bFGF) was expressed in eukaryotic cells and in prokaryotic cells, from which it was purified to homogeneity. Transient expression of bFGF cDNA and of M1Q-bFGF cDNA in simian COS-1 cells followed by immunolocalization and by subcellular fractionation indicated that both molecules localize in the nucleus, as well as in the cytoplasm of transfected cells, and interact with nuclear chromatin and with eukaryote DNA in a similar manner. Prokaryotic expression of M1Q-bFGF cDNA yields a polypeptide endowed with a receptor-binding capacity and mitogenic activity similar to that exerted by wild-typebFGF. However, recombinant M1Q-bFGF showed a drastically reduced capacity to induce the production of urokinase-type plasminogen activator (uPA) in endothelial cells. The uPA-inducing activity of M1Q-bFGF was fully restored by the presence of soluble heparin in the culture medium. In conclusion, the sequence bFGF(27-31) does not appear to represent a nuclear translocation and/or retention sequence for bFGF. However,neutralization of its basic residues seems to modify the tertiary structure of the growth factor, thus affecting some of its biological properties.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 02:21:26