scholarly journals Stable expression of human platelet-derived growth factor B chain by bovine aortic endothelial cells. Matrix association and selective proteolytic cleavage by thrombin

1994 ◽  
Vol 269 (26) ◽  
pp. 17734-17740
Author(s):  
A.A. Soyombo ◽  
P.E. DiCorleto
Blood ◽  
1986 ◽  
Vol 67 (1) ◽  
pp. 131-134
Author(s):  
KS Callahan ◽  
A Schorer ◽  
JM Harlan

We examined the effect of highly purified platelet-derived growth factor (PDGF) on prostacyclin (PGI2) release by cultured human umbilical vein and bovine aortic endothelial cells. PDGF tested at concentrations equal to or exceeding those observed in serum did not increase endothelial cell PGI2 synthesis as measured by radioimmunoassay of its metabolite, 6-keto-PGF1 alpha. In contrast, cells incubated with 20% human whole blood serum (WBS) demonstrated significantly increased PGI2 production (fivefold stimulation). Addition of anti-PDGF antibody to the 20% WBS did not attenuate the increased synthesis of PGI2. Incubation with 20% plasma-derived serum (PDS) that was deficient in PDGF produced stimulation of PGI2 release similar to 20% WBS. These results demonstrate that PDGF does not cause increased PGI2 synthesis in cultured human endothelial cells of human or bovine origin, and further suggest that the stimulation observed with serum is not due to a platelet-release product.


Blood ◽  
1986 ◽  
Vol 67 (1) ◽  
pp. 131-134 ◽  
Author(s):  
KS Callahan ◽  
A Schorer ◽  
JM Harlan

Abstract We examined the effect of highly purified platelet-derived growth factor (PDGF) on prostacyclin (PGI2) release by cultured human umbilical vein and bovine aortic endothelial cells. PDGF tested at concentrations equal to or exceeding those observed in serum did not increase endothelial cell PGI2 synthesis as measured by radioimmunoassay of its metabolite, 6-keto-PGF1 alpha. In contrast, cells incubated with 20% human whole blood serum (WBS) demonstrated significantly increased PGI2 production (fivefold stimulation). Addition of anti-PDGF antibody to the 20% WBS did not attenuate the increased synthesis of PGI2. Incubation with 20% plasma-derived serum (PDS) that was deficient in PDGF produced stimulation of PGI2 release similar to 20% WBS. These results demonstrate that PDGF does not cause increased PGI2 synthesis in cultured human endothelial cells of human or bovine origin, and further suggest that the stimulation observed with serum is not due to a platelet-release product.


1999 ◽  
Vol 85 (12) ◽  
pp. 1132-1138 ◽  
Author(s):  
M. Angeles Castilla ◽  
Maria Victoria Alvarez Arroyo ◽  
Esther Aceituno ◽  
Paloma Aragoncillo ◽  
Francisco R. González-Pacheco ◽  
...  

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