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
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
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人碱性成纤维细胞生长因子 (bFGF) 的生物活性合成片段：鉴定内皮细胞中参与 bFGF 促有丝分裂活性的两个包含 Asp-Gly-Arg 的结构域
DOI：
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发表时间：
1991
影响因子：
5.6
通讯作者：
G. Ragnotti
中科院分区：
文献类型：
--
作者：
M. Presta;M. Rusnati;C. Urbinati;A. Sommer;G. Ragnotti
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 mito‐genic 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.
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DOI：
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发表时间：
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期刊：
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DOI：
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发表时间：
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期刊：
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DOI：
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发表时间：
1988-07
期刊：
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影响因子：
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