ANGIOTENSIN II DEPENDENT GENE REGULATION IN HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS INVOLVES VEGF-SIGNALING AND ANGIOGENESIS

2007 ◽  
Vol 77 (Suppl_1) ◽  
pp. 138-138
Author(s):  
Daniel Herr ◽  
Miriam Rodewald ◽  
Gerda Hack ◽  
Rolf Kreienberg ◽  
Christine Wulff
Keyword(s):  
Endothelial Cells ◽  
Gene Regulation ◽  
Angiotensin Ii ◽  
Umbilical Vein ◽  
Human Umbilical Vein ◽  
Vegf Signaling ◽  
Umbilical Vein Endothelial Cells

scholarly journals Angiotensin II degrades myeloid cell leukemia 1 in human umbilical vein endothelial cells

IUBMB Life ◽  
2017 ◽  
Vol 69 (5) ◽  
pp. 321-327
Author(s):  
Wenlong Zhang ◽  
Ruyan Yang ◽  
Yaorong Feng ◽  
Bin Hu ◽  
Jun Zhang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Angiotensin Ii ◽  
Umbilical Vein ◽  
Myeloid Cell ◽  
Cell Leukemia ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

Abstract 379: Silencing of Fxyd1 Uncouples Enos in Human Umbilical Vein Endothelial Cells

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
Owen Tang ◽  
Tom H Huang ◽  
Jianmei Li ◽  
Sarah Tandy ◽  
Gemma Figtree
Keyword(s):  
Endothelial Cells ◽  
Angiotensin Ii ◽  
Human Erythrocyte ◽  
Ex Vivo ◽  
Umbilical Vein ◽  
Heart Tissue ◽  
Enzyme Linked Immunosorbent Assay ◽  
Human Umbilical Vein ◽  
Enos Uncoupling ◽  
Umbilical Vein Endothelial Cells

Introduction/Aims: FXYD1 has been shown to be a master regulator of the sodium potassium pump activity in the caveolae of heart tissue, protecting the pump from glutathionylation and oxidative inhibition. However, very little is known about its expression and function in the endothelium, particularly in regard to its potential interaction with other caveolae proteins. Given the molecular mechanism of eNOS uncoupling is via glutathionylation, we examined whether FXYD1 was expressed in endothelial cells, and whether it had a functional partnership with eNOS. Methods: Co-immunoprecipitation was used to study the interaction of FXYD1 and eNOS. GSH antibody was used for immunodetection of eNOS glutathionylation. Silencing of FXYD1 using siRNA followed by DAF staining or spin trap were used to study the effects of FXYD1 on eNOS function. Enzyme-linked immunosorbent assay was also employed to quantify eNOS glutathionylation level in human erythrocyte samples post exposure to angiotensin II (0 to 500 nM) ex vivo. Results: FXYD1 co-immunoprecipitated with eNOS in human umbilical vein endothelial cells (HUVECs). Silencing of FXYD1 resulted in significantly increased eNOS glutathionylation, associated with significantly reduced NO bioavailability under baseline and acetylcholine stimulated conditions (1μM, 20mins). Furthermore, a dose-dependent increase in eNOS glutathionylation level was also observed in human erythrocyte exposed to angiotensin II. Discussion: Our findings demonstrated a novel functional partnership of FXYD1 with eNOS, protecting this vital enzyme from glutathionylation-mediated uncoupling. This has important implications for our understanding of ROS-signalling in the vasculature. Furthermore, FXYD1 expression/eNOS glutathionylation may serve as important biomarkers for oxidative stress.

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