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Biologically active synthetic fragments of human basic fibroblast growth factor (bFGF): identification of two Asp-Gly-Arg-containing domains involved in the mitogenic activity of bFGF in endothelial cells.

PRESTA, Marco;RUSNATI, Marco;URBINATI, Chiara Eva;
1991-01-01
1991
MIUR (compresi PRIN FIRB,FISR)
LS1_1 Molecular biology and interactions
JOURNAL OF CELLULAR PHYSIOLOGY
sì
2-s2.0-0025788065
WOS:A1991GU23700021
Esperti anonimi
Inglese
Internazionale
149
3
512
524
12
1660485
Synthetic peptides derived from the amino acid sequence of human basic fibroblast growth factor (bFGF) have been assayed for the capacity to exert bFGF agonist and antagonist activities in cultured endothelial cells. bFGF fragments A and C, which correspond to the sequences bFGF (38-61) and bFGF (82-101), induce a limited but statistically significant increase in cell number when administered to cultures of fetal bovine aortic endothelial GM 7373 cells and adult bovine aortic endothelial cells. The two peptides also exert a partial antagonist activity when GM 7373 cells are stimulated to proliferate by bFGF, but they do not affect cell proliferation induced by serum, epidermal growth factor (EGF), phorbol ester (TPA), or 1,2-diacylglycerol (diC8). Moreover, antibodies raised against peptides A and C specifically quench the mitogenic activity of bFGF. Peptides A and C contain the amino acid sequence Asp-Gly-Arg (DGR), which is the inverse of the cell adhesion signal sequence RGD recognized by integrins. DGR- and RGD-containing tetra- and heptapeptides inhibit the mitogenic activity exerted by bFGF and by the two active bFGF fragments. They do not affect cell proliferation induced by acidic FGF, EGF, serum, TPA, and diC8. However, neither peptides A and C, their corresponding antibodies, nor DGR-and RGD-containing peptides inhibit the binding of 125I-bFGF to its low and high affinity binding sites. The data suggest that amino acid residues 38-61 and 82-101, both containing a core DGR sequence, represent two "activation" domains of bFGF. Both domains are involved in the modulation of the mitogenic activity of bFGF without interacting directly with the bFGF receptor.
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; Amino Acid Sequence; Animals; Cattle; Cell Division; Cell Line; Transformed; Cell Membrane; Endothelium; Vascular; Fibroblast Growth Factor 2; Humans; Isoquinolines; Kinetics; Models; Biological; Molecular Sequence Data; Peptide Fragments; Peptides; Piperazines; Protein Kinase Inhibitors; Receptors; Cell Surface; Fibroblast Growth Factor; Recombinant Proteins
Ateneo di appartenenza
http://dx.doi.org/10.1002/jcp.1041490322
5
info:eu-repo/semantics/article
262
Presta, Marco; Rusnati, Marco; Urbinati, Chiara Eva; A., Sommer; G., Ragnotti
1 Contributo su Rivista::1.1 Articolo in rivista
none
1.1 Articolo in rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11379/31115
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