Rapid increase in endothelial nitric oxide production by bradykinin is mediated by protein kinase A signaling pathway

2003 ◽  
Vol 306 (4) ◽  
pp. 981-987 ◽  
Author(s):  
Sung Won Bae ◽  
Hye Sue Kim ◽  
Young Nam Cha ◽  
Yoon Shin Park ◽  
Sangmee Ahn Jo ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Signaling Pathway ◽  
Nitric Oxide Production ◽  
Oxide Production ◽  
Endothelial Nitric Oxide ◽  
Kinase A

Methylmercury inhibits nitric oxide production mediated by Ca2+ overload and protein kinase A activation

Toxicology ◽  
2002 ◽  
Vol 176 (1-2) ◽  
pp. 113-122 ◽  
Author(s):  
Tsun-Cheng Kuo ◽  
Chin-Lien Huang ◽  
Shoei-Yn Lin-Shiau
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Nitric Oxide Production ◽  
Oxide Production ◽  
Kinase A

scholarly journals Altered nitric oxide production mediates matrix-specific PAK2 and NF-κB activation by flow

2013 ◽  
Vol 24 (3) ◽  
pp. 398-408 ◽  
Author(s):  
Arif Yurdagul ◽  
Jie Chen ◽  
Steven Daniel Funk ◽  
Patrick Albert ◽  
Christopher G. Kevil ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Shear Stress ◽  
Protein Kinase ◽  
Membrane Proteins ◽  
Basement Membrane ◽  
Protein Kinase A ◽  
Nitric Oxide Production ◽  
Oxide Production ◽  
Kinase A

Shear stress generated by distinct blood flow patterns modulates endothelial cell phenotype to spatially restrict atherosclerotic plaque development. Signaling through p21-activated kinase (PAK) mediates several of the deleterious effects of shear stress, including enhanced NF-κB activation and proinflammatory gene expression. Whereas shear stress activates PAK in endothelial cells on a fibronectin matrix, basement membrane proteins limit shear-induced PAK activation and inflammation through a protein kinase A–dependent pathway; however, the mechanisms underlying this regulation were unknown. We show that basement membrane proteins limit membrane recruitment of PAK2, the dominant isoform in endothelial cells, by blocking its interaction with the adaptor protein Nck. This uncoupling response requires protein kinase A–dependent nitric oxide production and subsequent PAK2 phosphorylation on Ser-20 in the Nck-binding domain. Of importance, shear stress does not stimulate nitric oxide production in endothelial cells on fibronectin, resulting in enhanced PAK activation, NF-κB phosphorylation, ICAM-1 expression, and monocyte adhesion. These data demonstrate that differential flow–induced nitric oxide production regulates matrix-specific PAK signaling and describe a novel mechanism of nitric oxide–dependent NF-κB inhibition.

LOW-INTENSITY ULTRASOUND INCREASES THE ENDOTHELIAL NITRIC OXIDE SYNTHASE (eNOS) EXPRESSION OF ENDOTHELIAL CELLS POSSIBLY VIA THE PHOSPHATIDYLINOSITOL 3-KINASE/AKT/PROTEIN KINASE A SIGNALING PATHWAY

2010 ◽  
Vol 22 (05) ◽  
pp. 367-376
Author(s):  
Shan-hui Hsu ◽  
Tsung-Bin Huang ◽  
Kuan-Pu Wang
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Ultrasound Exposure ◽  
Low Intensity ◽  
Low Intensity Ultrasound ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide ◽  
Kinase A

The stimulative effects and the associated mechanism of low-intensity ultrasound on endothelial cells were investigated in this study. Human umbilical cord endothelial cells (HUVECs) were exposed to 1 MHz pulsed ultrasound at 34 mW/cm2 for 10 min daily. The cell proliferation, nitric oxide release, intracellular calcium concentration, and endothelial nitric oxide synthase (eNOS) gene and protein expressions after ultrasound exposure were analyzed. It was found that ultrasound exposure did not change the cell proliferation, but it enhanced the release of nitric oxide and Ca2+ ions, and increased the eNOS activity. The induced phosphorylation of eNOS (Ser1177) by the ultrasound exposure was inhibited by the addition of N-[2-(p-bromocinnamylamino) ethyl]-5-isoquinoline sulfonamide (H89, a protein kinase A inhibitor), but not 2-(4-morpholino)-8-phenyl-4H-1-benzopyran-4-one hydrochloride (LY294002, a phosphoatidylinositol 3-kinase inhibitor). The induced phosphorylation of Akt (protein kinase B, Ser473) by the ultrasound exposure was inhibited by the addition of LY294002, but not by the presence of H89. The results also applied to bovine carotid artery endothelial cells (BAECs) exposed to ultrasound at a larger intensity (68 mW/cm2). The above experiments suggested that low-intensity ultrasound may promote eNOS activity of endothelial cells via the phosphatidylinositol 3-kinase/Akt/protein kinase A signaling pathway. This may have implications on the therapeutic effect of ultrasound in tissue repair.

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