Regulating Effect of Tea Polyphenols on Endothelin, Intracellular Calcium Concentration, and Mitochondrial Membrane Potential in Vascular Endothelial Cells Injured by Angiotensin II

2014 ◽  
Vol 28 (4) ◽  
pp. 1016-1022 ◽  
Author(s):  
Minggao Li ◽  
Guixi Ma ◽  
Lei Han ◽  
Jing Li
Keyword(s):  
Endothelial Cells ◽  
Membrane Potential ◽  
Angiotensin Ii ◽  
Intracellular Calcium ◽  
Mitochondrial Membrane Potential ◽  
Mitochondrial Membrane ◽  
Calcium Concentration ◽  
Vascular Endothelial Cells ◽  
Tea Polyphenols ◽  
Vascular Endothelial

scholarly journals Glyoxal Damages Human Aortic Endothelial Cells by Perturbing the Glutathione, Mitochondrial Membrane Potential, and Mitogen-Activated Protein Kinase Pathways

2021 ◽  
Author(s):  
Ming-Zhang Xie ◽  
Chun Guo ◽  
Jia-Qi Dong. BA ◽  
Jie Zhang ◽  
Ke-Tao Sun ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Membrane Potential ◽  
Protein Kinase ◽  
Mitochondrial Membrane Potential ◽  
Mitochondrial Membrane ◽  
Mitogen Activated Protein Kinase ◽  
Aortic Endothelial Cells ◽  
Mitogen Activated Protein ◽  
Human Aortic Endothelial Cells ◽  
Quantitative Fluorescence

Abstract Background: Exposure to glyoxal, the smallest dialdehyde, is associated with several diseases; humans are routinely exposed to glyoxal because of its ubiquitous presence in foods and the environment. The aim of this study was to examine the damage caused by glyoxal in human aortic endothelial cells. Methods: Cell survival assays and quantitative fluorescence assays were performed to measure DNA damage; oxidative stress was detected by colorimetric assays and quantitative fluorescence, and the mitogen-activated protein kinase pathways were assessed using western blotting. Results: Exposure to glyoxal was found to be linked to abnormal glutathione activity, the collapse of mitochondrial membrane potential, and the activation of mitogen-activated protein kinase pathways. However, DNA damage and thioredoxin oxidation were not induced by dialdehydes. Conclusions: Intracellular glutathione, members of the mitogen-activated protein kinase pathways, and the mitochondrial membrane potential are all critical targets of glyoxal. These findings provide novel insights into the molecular mechanisms perturbed by glyoxal and may facilitate the development of new therapeutics and diagnostic markers for cardiovascular diseases.

scholarly journals Agonistic Autoantibodies to the Angiotensin II Type 1 Receptor Enhance ANGII Binding on Vascular Endothelial Cells

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Mark Cunningham ◽  
Jessica Faulkner ◽  
Lorena Amaral ◽  
Denise Cornelius ◽  
Robert Kramer ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Angiotensin Ii ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Agonistic Autoantibodies

Thrombin receptor 14-amino acid peptide binds to endothelial cells and stimulates calcium transients

1992 ◽  
Vol 263 (5) ◽  
pp. L595-L601 ◽  
Author(s):  
C. Tiruppathi ◽  
H. Lum ◽  
T. T. Andersen ◽  
J. W. Fenton ◽  
A. B. Malik
Keyword(s):  
Endothelial Cells ◽  
Intracellular Calcium ◽  
Vascular Endothelial Cells ◽  
Umbilical Vein ◽  
Calcium Transients ◽  
Cell Protein ◽  
Affinity Constant ◽  
Thrombin Receptor ◽  
Vascular Endothelial ◽  
Amino Terminal

We examined the binding characteristics of the recently described thrombin receptor amino-terminal peptide, SFLLRNPNDKYEPF (T. K. H. Vu, D. T. Hung, V. I. Wheaton, and S. R. Coughlin. Cell 64: 1057-1068, 1991), termed TRP-14, and its effect in activating intracellular calcium transients in pulmonary vascular endothelial cells. Binding of 125I-labeled TRP-14 was found to be saturable with a affinity constant of 2 microM and maximum binding of 41 pmol/mg of cell protein. The 125I-labeled TRP-14 also interacted with bovine pulmonary microvessel endothelial cells, human umbilical vein endothelial cells, and porcine pulmonary artery smooth muscle cells. Binding of 125I-labeled diisopropylphosphoryl (DIP)-alpha-thrombin, which is catalytically inactive but binds to thrombin receptors, was not inhibited by TRP-14 or vice versa, indicating that TRP-14 did not compete for the alpha-thrombin binding site(s) on the endothelial cell surface. TRP-14 (> 1 microM) increased the concentration of intracellular calcium ([Ca2+]i) in endothelial cells with kinetics similar to the increase in [Ca2+]i triggered by alpha-thrombin. In contrast, DIP-alpha-thrombin did not increase [Ca2+]i and also did not prevent the rise in [Ca2+]i induced by the subsequent challenge with either TRP-14 or alpha-thrombin. Because the generation of TRP-14 by the proteolytically active forms of thrombin stimulated a rise in endothelial [Ca2+]i, TRP-14 may be the agonist responsible for the activation of the alpha-thrombin receptor in pulmonary vascular endothelial cells.(ABSTRACT TRUNCATED AT 250 WORDS)

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