Salidroside Inhibits Endogenous Hydrogen Peroxide Induced Cytotoxicity of Endothelial Cells

2013 ◽  
Vol 750-752 ◽  
pp. 1529-1532 ◽  
Author(s):  
Xing Yu Zhao ◽  
Lian Hai Jin ◽  
Dong Jun Wang ◽  
Bin Xu ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Glucose Oxidase ◽  
Flow Cytometric Analysis ◽  
Steady States ◽  
Protective Effects ◽  
Human Endothelial Cells ◽  
Flow Cytometric ◽  
Dose Dependent ◽  
Mtt Assays

To explore the protective effects of salidroside against endogenous hydrogen peroxide (H2O2) -induced cytotoxicity in human endothelial cells (EVC-304). EVC-304 cells were incubated in the presence or absence of low steady states of H2O2 (34μM) generated by glucose oxidase (GOX) with or without salidroside. MTT assays were performed, together with flow cytometric analysis using propidium (PI) label. The results indicated that salidroside could attenuate H2O2 induced cytotoxicity in EVC-304 cells in a dose-dependent pattern. Furthermore, flow cytometric analysis revealed that salidroside could also inhibited the G2/M arrest induced by endogenous hydrogen. The present study demonstrates that salidroside could inhibit endogenous hydrogen peroxide induced cytotoxicity of endothelial cells .

Protective effects of peoniflorin against hydrogen peroxide-induced oxidative stress in human umbilical vein endothelial cells

2011 ◽  
Vol 89 (6) ◽  
pp. 445-453 ◽  
Author(s):  
Tao Chen ◽  
Zai-pei Guo ◽  
Xiao-yan Jiao ◽  
Yu-hong Zhang ◽  
Jing-yi Li ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Oxidative Damage ◽  
Umbilical Vein ◽  
Flow Cytometric Analysis ◽  
Vascular Diseases ◽  
Protective Effects ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

Peoniflorin (PF), extracted from the root of Paeonia lactiflora Pall., has been reported to have anti-inflammation and antioxidant effects in several animal models. Herein, we investigated the protective effects of PF against hydrogen peroxide (H2O2)-induced oxidative damage in human umbilical vein endothelial cells (HUVECs). HUVECs were treated by H2O2 (240 µmol/L) with or without PF. PF significantly increased the percent cell viability of HUVECs injured by H2O2 using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) assay. By flow cytometric analysis, PF markedly attenuated H2O2-induced apoptosis and intracellular reactive oxygen species production. In addition, PF also displayed a dose-dependent reduction of lactate dehydrogenase leakage, malondialdehyde formation, and caspase-3 proteolytic activities in H2O2-treated cells, which was accompanied with a restoration of the activities of endogenous antioxidants, including total superoxide dismutase and glutathione peroxidase. Finally, Western blot data revealed that H2O2 upregulated phosphorylation of extracellular signal-regulated kinase 1/2 in HUVECs, which was almost completely reversed by PF. Taken together, our data provide the first evidence that PF has a protective ability against oxidative damage in HUVECs. PF may be a candidate medicine for the treatment of vascular diseases associated with oxidative stress.

Ibuprofen protects human endothelial cell prostaglandin H synthase from hydrogen peroxide

1996 ◽  
Vol 271 (6) ◽  
pp. C1879-C1886 ◽  
Author(s):  
D. A. Wessels ◽  
S. L. Hempel
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Arachidonic Acid ◽  
Endothelial Cell ◽  
Arachidonic Acid Release ◽  
Human Endothelial Cells ◽  
Prostaglandin H Synthase ◽  
Cyclooxygenase Activity ◽  
Acid Release ◽  
Prostaglandin H

Human endothelial cells exposed to H2O2 demonstrate decreased prostacyclin (PGI2) synthesis due to decreased prostaglandin H synthase (PGH synthase) activity. We tested the hypothesis that PGH synthase activity could be protected from H2O2 by a reversible nonsteroidal anti-inflammatory drug. Experiments demonstrate that ibuprofen if present during H2O2 exposure, protects endothelial cell PGH synthase against the decrease in prostaglandin formation caused by H2O2. Additional studies demonstrated that decreasing arachidonic acid release from cell phospholipids during H2O2 exposure did not protect PGI2 synthesis following H2O2 exposure. In other experiments, ibuprofen did not chelate Fe2+ in a conformation that inhibited the reactivity of Fe2+. In addition, ibuprofen did not scavenge HO. However, we demonstrate that ibuprofen significantly protects purified PGH synthase cyclooxygenase activity from the effects of H2O2. The results confirm the hypothesis. These findings suggest that ibuprofen displaces oxidant species from the cyclooxygenase site of PGH synthase, thereby preventing oxidation of the functional groups important for PGH synthase activity.

scholarly journals Attachment of cultured human endothelial cells is promoted by specific association with S protein (vitronectin) as well as with the ternary S protein-thrombin-antithrombin III complex

Blood ◽  
1988 ◽  
Vol 71 (6) ◽  
pp. 1581-1589 ◽  
Author(s):  
KT Preissner ◽  
E Anders ◽  
J Grulich-Henn ◽  
G Muller-Berghaus
Keyword(s):  
Endothelial Cells ◽  
Antithrombin Iii ◽  
Cell Attachment ◽  
Umbilical Vein ◽  
Cell Types ◽  
Human Endothelial Cells ◽  
S Protein ◽  
Major Vessel ◽  
Specific Association ◽  
Dose Dependent

Abstract The interaction of the multifunctional S protein (vitronectin) with cultured human endothelial cells of macrovascular and microvascular origin was investigated. Purified S protein, coated on polystyrene Petri dishes, induced dose-dependent and time-dependent attachment and spreading of human umbilical vein endothelial cells (HUVECs) as well as human omental tissue microvascular endothelial cells (HOTMECs) at 37 degrees C. Not only isolated S protein, but also the ternary S protein- thrombin-antithrombin III (STAT) complex promoted attachment of approximately 90% of the cells within 2 hours at an S protein concentration of 0.13 mumol/L. Inhibition of attachment in these experiments was achieved by the addition of the cell-attachment pentapeptide Gly-Arg-Gly-Asp-Ser and by monospecific antibodies against S protein, whereas nonrelated peptides or antibodies against fibronectin, fibrinogen, or von Willebrand factor (vWF) were ineffective. Direct binding of S protein to HUVECs and HOTMECs was studied with cells in suspension at a density of 1 x 10(6) cells/mL and was maximal after 120 minutes. S protein bound to both cell types in a dose-dependent fashion with an estimated dissociation constant Kd = 0.2 mumol/L. At a 200-fold to 500-fold molar excess of unlabeled S protein, greater than 80% of bound radiolabeled S protein was displaceable, whereas binding was reduced to 30% to 50% by addition of the pentapeptide, the STAT complex, or by physiologic concentrations of fibrinogen or vWF as well as Fab fragments of anti(human S protein)IgG, but not by Fab rabbit IgG. These findings present evidence for the specific association of S protein with endothelial cells ultimately leading to attachment and spreading of cells. Moreover, a novel function for the ternary STAT complex, which induced endothelial cell attachment and spreading virtually identical to free S protein, is described. These data further suggest a possible role for S protein during coagulation as major vessel wall-related adhesive protein at sites of vascular injury.

scholarly journals GLP-1 promotes angiogenesis in human endothelial cells in a dose-dependent manner, through the Akt, Src and PKC pathways

Metabolism ◽  
2013 ◽  
Vol 62 (9) ◽  
pp. 1279-1286 ◽  
Author(s):  
Konstantinos N. Aronis ◽  
John P. Chamberland ◽  
Christos S. Mantzoros
Keyword(s):  
Endothelial Cells ◽  
Dependent Manner ◽  
Human Endothelial Cells ◽  
Dose Dependent

scholarly journals Synthesis of 8-epi-prostaglandin F2α by human endothelial cells: role of prostaglandin H2 synthase

1999 ◽  
Vol 344 (3) ◽  
pp. 747-754 ◽  
Author(s):  
Michael T. WATKINS ◽  
George M. PATTON ◽  
Hiram M. SOLER ◽  
Hassan ALBADAWI ◽  
Donald E. HUMPHRIES ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Umbilical Artery ◽  
Prostaglandin F2α ◽  
Human Endothelial Cells ◽  
Microcarrier Beads ◽  
A Cell ◽  
Superoxide Scavenger ◽  
Negative Cell Line

The experiments described in this paper were designed to determine the mechanism underlying the increase in 8-isoprostaglandin F2α (8-epi-PGF2α) production by cultured human endothelial cells during reoxygenation following hypoxia. Human umbilical artery endothelial cells were grown on microcarrier beads and exposed to sequential periods of normoxia, hypoxia, and reoxygenation. The amount of 8-epi-PGF2α in the medium was determined by ELISA. The production of 8-epi-PGF2α decreased by greater than 90% during hypoxia. Upon reoxygenation 8-epi-PGF2α production increased linearly for 90 min reaching nearly 3 times normoxic levels. When added to the medium during reoxygenation, neither superoxide dismutase nor Tiron, a cell-permeable superoxide scavenger, inhibited 8-epi-PGF2α production. However, 8-epi-PGF2α production was inhibited by catalase. The production of 8-epi-PGF2α was also inhibited by indomethacin and aspirin. Exogenous hydrogen peroxide stimulated 8-epi-PGF2α production by normoxic cells, and aspirin inhibited the hydrogen peroxide-mediated increase in 8-epi-PGF2α production. These results indicate that the reactive oxygen species responsible for 8-epi-PGF2α synthesis during reoxygenation is hydrogen peroxide and that in endothelial cells 8-epi-PGF2α synthesis is mediated by prostaglandin H2 synthase (PGHS). To verify the role of PGHS in 8-epi-PGF2α synthesis, human PGHS-1 was expressed in COS-7 cells, a PGHS negative cell line that does not synthesize 8-epi-PGF2α. In the presence of exogenous arachidonic acid the COS-7 cells expressing human PGHS-1 produced substantial amounts of PGE2 and 8-epi-PGF2α. These data indicate that human PGHS-1 can support the synthesis of 8-epi-PGF2α and that 8-epi-PGF2α synthesis by cultured human endothelial cells during reoxygenation is dependent on the activity of PGHS-1.

Cyclooxygenase-2 mediates hydrogen peroxide-induced wound repair in human endothelial cells

2009 ◽  
Vol 46 (10) ◽  
pp. 1428-1436 ◽  
Author(s):  
Sonia Eligini ◽  
Izaskun Arenaz ◽  
Silvia S. Barbieri ◽  
Maurizio L. Faleri ◽  
Mauro Crisci ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Wound Repair ◽  
Cyclooxygenase 2 ◽  
Human Endothelial Cells
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