scholarly journals The stimulation of arginine transport by TNFα in human endothelial cells depends on NF-κB activation

2004 ◽  
Vol 1664 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Rossana Visigalli ◽  
Ovidio Bussolati ◽  
Roberto Sala ◽  
Amelia Barilli ◽  
Bianca Maria Rotoli ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Human Endothelial Cells ◽  
Arginine Transport ◽  
Stimulation Of

scholarly journals Platelet-derived growth factor does not stimulate prostacyclin synthesis by cultured endothelial cells

Blood ◽  
1986 ◽  
Vol 67 (1) ◽  
pp. 131-134
Author(s):  
KS Callahan ◽  
A Schorer ◽  
JM Harlan
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Umbilical Vein ◽  
Platelet Derived Growth Factor ◽  
Human Endothelial Cells ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Prostacyclin Synthesis ◽  
Release Product ◽  
Stimulation Of

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.

Histamine stimulation of prostaglandin and HETE synthesis in human endothelial cells

1988 ◽  
Vol 255 (2) ◽  
pp. C214-C225 ◽  
Author(s):  
G. E. Revtyak ◽  
M. J. Hughes ◽  
A. R. Johnson ◽  
W. B. Campbell
Keyword(s):  
Endothelial Cells ◽  
Arachidonic Acid ◽  
Umbilical Artery ◽  
Epoxyeicosatrienoic Acids ◽  
Human Endothelial Cells ◽  
Intact Cells ◽  
Histamine Stimulation ◽  
Human Umbilical Artery ◽  
A Minor ◽  
Stimulation Of

Endothelial cells (EC) cultured from human umbilical artery (UA) and vein (UV) metabolized [14C]arachidonic acid to prostaglandins (PGs), monohydroxyeicosatetraenoic acids (HETEs), and epoxyeicosatrienoic acids (EETs). Major radioactive products were identified as 6-keto-PGF1 alpha, PGE2, PGF2 alpha, 12-hydroxy heptadecatrienoic acid, 15-HETE, and 11-HETE. In addition, extracts from UV ECs contained 12-HETE, 5-HETE, 14,15-EET, and 5,6-EET as minor products, whereas extracts from UA ECs contained only 12-HETE as a minor product. UA ECs also produced metabolites comigrating with 14,15-EET, 11,12-EET, 8,9-EET, and 5,6-EET. Histamine increased the release of [14C]PGs and [14C]HETEs from [14C]arachidonic acid-labeled ECs. Indomethacin, aspirin, and nordihydroguauretic acid completely inhibited synthesis of both [14C]PGs and [14C]HETEs from exogenous [14C]arachidonic acid in these cells. Microsomes metabolized [14C]arachidonic acid to the same [14C]PGs and [14C]HETEs as intact cells. Pretreatment of microsomes with indomethacin completely inhibited formation of these products. These data indicate that UA ECs and UV ECs metabolize endogenous and exogenous arachidonic acid to both PGs and HETEs. Also 15-HETE and 11-HETE appear to be synthesized by a microsomal enzyme with the properties of cyclooxygenase.

Regulation of arginine transport and metabolism by Protein Kinase Cα in endothelial cells: stimulation of CAT2 transporters and arginase activity

2010 ◽  
Vol 49 (2) ◽  
pp. 260-270 ◽  
Author(s):  
Rossana Visigalli ◽  
Amelia Barilli ◽  
Alessandro Parolari ◽  
Roberto Sala ◽  
Bianca Maria Rotoli ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Arginase Activity ◽  
Arginine Transport ◽  
Protein Kinase Cα ◽  
Stimulation Of

scholarly journals Platelet-derived growth factor does not stimulate prostacyclin synthesis by cultured endothelial cells

Blood ◽  
1986 ◽  
Vol 67 (1) ◽  
pp. 131-134 ◽  
Author(s):  
KS Callahan ◽  
A Schorer ◽  
JM Harlan
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Umbilical Vein ◽  
Platelet Derived Growth Factor ◽  
Human Endothelial Cells ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Prostacyclin Synthesis ◽  
Release Product ◽  
Stimulation Of

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.

Sign in / Sign up

Export Citation Format

Share Document