Structure-function relationship of basic fibroblast growth factor: site-directed mutagenesis of a putative heparin-binding and receptor-binding region.
Biochem Biophys Res Commun
; 185(3): 1098-107, 1992 Jun 30.
Article
en En
| MEDLINE
| ID: mdl-1378264
Basic residues Arg-118, Lys-119, Lys-128, and Arg-129 within a putative heparin-binding and receptor-binding region of the 155-amino acid form of basic fibroblast growth factor (bFGF) have been changed to neutral glutamine residues by site-directed mutagenesis of the human bFGF cDNA. The bFGF mutant (M6B-bFGF) was expressed in E. coli and purified to homogeneity. When compared to wild type bFGF, M6B-bFGF showed in cultured endothelial cells a similar receptor-binding capacity and mitogenic activity, but a reduced affinity for heparin-like low affinity binding sites, a reduced chemotactic activity, and a reduced capacity to induce the production of urokinase-type plasminogen activator. In vivo, M6B-bFGF lacked a significant angiogenic activity. Modifications of both the primary and the tertiary structure of bFGF appear to be responsible for the modified biological properties of M6B-bFGF, thus confirming the possibility to dissociate at the structural level some of the biological activities exerted by bFGF on endothelial cells.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Heparina
/
Factor 2 de Crecimiento de Fibroblastos
/
Mutagénesis Sitio-Dirigida
/
Receptores de Superficie Celular
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1992
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Estados Unidos