scholarly journals Basic Fibroblast Growth Factor Stimulates the Competence Phase of Subcultured Endothelial Cells and the Progression Phase of Primary Cultured Smooth Muscle Cells from Rat Aorta.

1994 ◽  
Vol 17 (9) ◽  
pp. 1176-1181 ◽  
Author(s):  
Takeshi NAGAURA ◽  
Motonori OKABE ◽  
Shinjiro KOBAYASHI ◽  
Ikuko KIMURA ◽  
Masayasu KIMURA
Keyword(s):  
Endothelial Cells ◽  
Smooth Muscle ◽  
Growth Factor ◽  
Smooth Muscle Cells ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Muscle Cells ◽  
Rat Aorta ◽  
Fibroblast Growth ◽  
Cultured Smooth Muscle Cells

The chemotactic and mitogenic effects of platelet-derived growth factor-BB on rat aorta smooth muscle cells are inhibited by basic fibroblast growth factor

2000 ◽  
Vol 113 (16) ◽  
pp. 2855-2863
Author(s):  
A. Facchiano ◽  
F. De Marchis ◽  
E. Turchetti ◽  
F. Facchiano ◽  
M. Guglielmi ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Growth Factor ◽  
Smooth Muscle Cells ◽  
Fibroblast Growth Factor ◽  
Basic Fibroblast Growth Factor ◽  
Muscle Cells ◽  
Rat Aorta ◽  
Platelet Derived Growth Factor ◽  
Fibroblast Growth

In response to endovascular injury, platelet-derived growth factor-BB (PDGF-BB) and basic fibroblast growth factor (bFGF) are released locally and modulate vascular smooth muscle cells (SMC) proliferation and migration within the vascular wall. The aim of the present in vitro study was to determine how rat aorta SMC respond to the simultaneous exposure to PDGF-BB and bFGF. In a modified Boyden chamber assay bFGF exhibited a dose-dependent effect to inhibit the chemotactic action of PDGF-BB. A comparable result was observed in proliferation assays. In contrast, MIP-1 beta, epidermal growth factor (EGF), fibronectin and acidic FGF (aFGF) did not inhibit the chemotactic effect of PDGF-BB. Denatured bFGF did not exert an inhibitory effect and neutralizing antibodies either to bFGF or to bFGF-receptor abolished the inhibition observed in the presence of bFGF. The role played by PDGF receptor alpha (PDGF-Ralpha) was investigated in PDGF-Ralpha-dominant negative-transfected SMC, by selectively blocking PDGF-BB-binding to PDGF-Ralpha with neomycin, by neutralizing PDGF-Ralpha with a monoclonal antibody and by selectively stimulating PDGF-Ralpha with PDGF-AA; in all cases the effect of bFGF to inhibit PDGF-BB-directed SMC migration was abolished. These in vitro studies show that bFGF significantly inhibits PDGF-BB-induced SMC migration and proliferation and that this effect is mediated by both PDGF-Ralpha and bFGF receptor.

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