Sprouty Proteins Inhibit Fibroblast Growth Factor 2-induced Endothelial Nitric Oxide Synthase Activation via the PI3K-Akt Pathway in Placental Artery Endothelial Cells.

2010 ◽  
Vol 83 (Suppl_1) ◽  
pp. 191-191
Author(s):  
Lin Feng ◽  
Wu-xiang Liao ◽  
Jing Zheng ◽  
Dong-bao Chen
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Endothelial Nitric Oxide Synthase ◽  
Fibroblast Growth Factor 2 ◽  
Akt Pathway ◽  
Fibroblast Growth ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

scholarly journals Hepatocyte growth factor activates endothelial nitric oxide synthase by Ca2+- and phosphoinositide 3-kinase/Akt-dependent phosphorylation in aortic endothelial cells

2003 ◽  
Vol 374 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Kennedy MAKONDO ◽  
Kazuhiro KIMURA ◽  
Naoki KITAMURA ◽  
Takanori KITAMURA ◽  
Daisuke YAMAJI ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Growth Factor ◽  
Endothelial Nitric Oxide Synthase ◽  
Aortic Endothelial Cells ◽  
Enos Activity ◽  
Phosphoinositide 3 Kinase ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Hepatocyte Growth

Hepatocyte growth factor (HGF) causes endothelium-dependent vasodilation, but its relation to endothelial nitric oxide synthase (eNOS) activity remains to be elucidated. Treatment of bovine aortic endothelial cells with HGF increased eNOS activity within minutes, accompanied by an increase of activity-related site-specific phosphorylation of eNOS. The phosphorylation was completely abolished by pretreatment of the cells with a phosphoinositide 3-kinase (PI3K) inhibitor (wortmannin) and by transfection of dominant-negative Akt, and the enzyme activity was inhibited by wortmannin. In addition, eNOS activity and phosphorylation were abolished by pretreatment of the cells with an intracellular Ca2+-chelator, bis-(o-aminophenoxy)ethane-N,N,N′,N′-tetra-acetic acid tetrakis(acetoxymethyl ester) (BAPTA/AM), with a suppression of Akt phosphorylation. These results suggest that HGF stimulates eNOS activity by a PI3K/Akt-dependent phosphorylation in a Ca2+-sensitive manner in vascular endothelial cells.

scholarly journals Endothelial nitric oxide synthase is dynamically expressed during bone marrow stem cell differentiation into endothelial cells

2007 ◽  
Vol 293 (3) ◽  
pp. H1760-H1765 ◽  
Author(s):  
Zhenguo Liu ◽  
Yuehua Jiang ◽  
Hong Hao ◽  
Kalpna Gupta ◽  
Jian Xu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Stem Cell ◽  
Growth Factor ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Stem Cell Differentiation ◽  
Enos Expression ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

This study was designed to investigate the developmental expression of endothelial nitric oxide synthase (eNOS) during stem cell differentiation into endothelial cells and to examine the functional status of the newly differentiated endothelial cells. Mouse adult multipotent progenitor cells (MAPCs) were used as the source of stem cells and were induced to differentiate into endothelial cells with vascular endothelial growth factor (VEGF) in serum-free medium. Expression of eNOS in the cells during differentiation was evaluated with real-time PCR, nitric oxide synthase (NOS) activity, and Western blot analysis. It was found that eNOS, but no other NOS, was present in undifferentiated MAPCs. eNOS expression disappeared in the cells immediately after induction of differentiation. However, eNOS expression reoccurred at day 7 during differentiation. Increasing eNOS mRNA, protein content, and activity were observed in the cells at days 14 and 21 during differentiation. The differentiated endothelial cells formed dense capillary networks on growth factor-reduced Matrigel. VEGF-stimulated phosphorylation of extracellular signal-regulated kinase (ERK)-1 and ERK-2 occurred in these cells, which was inhibited by NOS inhibitor NG-nitro-l-arginine methyl ester. In conclusion, these data demonstrate that eNOS is present in MAPCs and is dynamically expressed during the differentiation of MAPCs into endothelial cells in vitro.

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