Microdialysis as a window on interstitial reactive oxygen species in human tissues?A commentary on “Antioxidant supplementation enhances the exercise-induced increase in mitochondrial uncoupling protein 3 and endothelial nitric oxide synthase mRNA content in human skeletal muscle,” by Hellsten et al.

2007 ◽  
Vol 43 (3) ◽  
pp. 351-352 ◽  
Author(s):  
Malcolm J. Jackson
Keyword(s):  
Endothelial Nitric Oxide Synthase ◽  
Uncoupling Protein ◽  
Oxygen Species ◽  
Mitochondrial Uncoupling ◽  
Mitochondrial Uncoupling Protein ◽  
Uncoupling Protein 3 ◽  
Mrna Content ◽  
Exercise Induced ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

scholarly journals p32-Dependent p38 MAPK Activation by Arginase II Downregulation Contributes to Endothelial Nitric Oxide Synthase Activation in HUVECs

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 392 ◽  
Author(s):  
Bon-Hyeock Koo ◽  
Moo-Ho Won ◽  
Young-Myeong Kim ◽  
Sungwoo Ryoo
Keyword(s):  
Nitric Oxide ◽  
Signaling Pathway ◽  
P38 Mapk ◽  
Endothelial Nitric Oxide Synthase ◽  
Oxygen Species ◽  
Mapk Activation ◽  
Enos Phosphorylation ◽  
Arginase Ii ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Arginase II reciprocally regulates endothelial nitric oxide synthase (eNOS) through a p32-dependent Ca2+ control. We investigated the signaling pathway of arginase II-dependent eNOS phosphorylation. Western blot analysis was applied for examining protein activation and [Ca2+]c was analyzed by microscopic and FACS analyses. Nitric oxide (NO) and reactive oxygen species (ROS) productions were measured using specific fluorescent dyes under microscopy. NO signaling pathway was tested by measuring vascular tension. Following arginase II downregulation by chemical inhibition or gene knockout (KO, ArgII−/−), increased eNOS phosphorylation at Ser1177 and decreased phosphorylation at Thr495 was depend on p38 MAPK activation, which induced by CaMKII activation through p32-dependent increase in [Ca2+]c. The protein amount of p32 negatively regulated p38 MAPK activation. p38 MAPK contributed to Akt-induced eNOS phosphorylation at Ser1177 that resulted in accelerated NO production and reduced reactive oxygen species production in aortic endothelia. In vascular tension assay, p38 MAPK inhibitor decreased acetylcholine-induced vasorelaxation responses and increased phenylephrine-dependent vasoconstrictive responses. In ApoE−/− mice fed a high cholesterol diet, arginase II inhibition restored p32/CaMKII/p38 MAPK/Akt/eNOS signaling cascade that was attenuated by p38 MAPK inhibition. Here, we demonstrated a novel signaling pathway contributing to understanding of the relationship between arginase II, endothelial dysfunction, and atherogenesis.

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