scholarly journals Role of CaMKII in hydrogen peroxide activation of ERK1/2, p38 MAPK, HSP27 and actin reorganization in endothelial cells

FEBS Letters ◽  
2004 ◽  
Vol 572 (1-3) ◽  
pp. 307-313 ◽  
Author(s):  
Andrew Nguyen ◽  
Peng Chen ◽  
Hua Cai
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
P38 Mapk ◽  
Actin Reorganization ◽  
Peroxide Activation

Involvement of Ca2+ in the H2O2-induced increase in endothelial permeability

1996 ◽  
Vol 270 (6) ◽  
pp. L973-L978 ◽  
Author(s):  
A. Siflinger-Birnboim ◽  
H. Lum ◽  
P. J. Del Vecchio ◽  
A. B. Malik
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Endothelial Cell ◽  
Binding Sites ◽  
Endothelial Permeability ◽  
Extracellular Medium ◽  
Critical Determinant ◽  
Cell Monolayers ◽  
Sensitive Membrane

We studied the role of Ca2+ in mediating the hydrogen peroxide (H2O2)-induced increase in endothelial permeability to 125I-labeled albumin using bovine pulmonary microvessel endothelial cells (BMVEC). Changes in cytosolic-free Ca2+ ([Ca2+]i) were monitored in BMVEC monolayers loaded with the Ca(2+)-sensitive membrane permeant fluorescent dye fura 2-AM. H2O2 (100 microM) produced a rise in [Ca2+]i within 10 s that was reduced by the addition of EGTA to the medium. Uptake of 45Ca2+ from the extracellular medium increased in the presence of H2O2 (100 microM) compared with control monolayers, suggesting that the H2O2-induced rise in [Ca2+]i is partly the result of extracellular Ca2+ influx. The effects of [Ca2+]i on endothelial permeability were addressed by pretreatment of BMVEC monolayers with BAPTA-AM (3-5 microM), a membrane permeant Ca2+ chelator, before the H2O2 exposure. BAPTA-AM produced an approximately 50% decrease in the H2O2-induced increase in endothelial permeability compared with endothelial cell monolayers exposed to H2O2 alone. The increase in endothelial permeability was independent of Ca2+ influx, since LaCl3 (0-100 microM), which displaces Ca2+ from binding sites on the cell surface, did not modify the permeability response. These results indicate that the rise in [Ca2+]i produced by H2O2 is a critical determinant of the increase in endothelial permeability.

Cytosolic phospholipase A2-α is an early apoptotic activator in PEDF-induced endothelial cell apoptosis

2009 ◽  
Vol 296 (2) ◽  
pp. C273-C284 ◽  
Author(s):  
Tsung-Chuan Ho ◽  
Show-Li Chen ◽  
Yuh-Cheng Yang ◽  
Tzu-Hsiu Lo ◽  
Jui-Wen Hsieh ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
P38 Mapk ◽  
Cell Apoptosis ◽  
Nuclear Translocation ◽  
Mitogen Activated Protein Kinase ◽  
Endothelial Cell Apoptosis ◽  
P53 Expression ◽  
Ppar Γ

Pigment epithelium-derived factor (PEDF) is an intrinsic antiangiogenic factor and a potential therapeutic agent. Previously, we discovered the mechanism of PEDF-induced apoptosis of human umbilical vein endothelial cells (HUVECs) as sequential induction/activation of p38 mitogen-activated protein kinase (MAPK), peroxisome proliferator-activated receptor gamma (PPAR-γ), and p53. In the present study, we investigated the signaling role of cytosolic calcium-dependent phospholipase A2-α (cPLA2-α) to bridge p38 MAPK and PPAR-γ activation. PEDF induced cPLA2-α activation in HUVECs and in endothelial cells in chemical burn-induced vessels on mouse cornea. The cPLA2-α activation is evident from the phosphorylation and nuclear translocation of cPLA2-α as well as arachidonic acid release and the cleavage of PED6, a synthetic PLA2 substrate. Such activation can be abolished by p38 MAPK inhibitor. The PEDF-induced PPAR-γ activation, p53 expression, caspase-3 activity, and apoptosis can be abolished by both cPLA2 inhibitor and small interfering RNA targeting cPLA2-α. Our observation not only establishes the signaling role of cPLA2-α but also for the first time demonstrates the sequential activation of p38 MAPK, cPLA2-α, PPAR-γ, and p53 as the mechanism of PEDF-induced endothelial cell apoptosis.

Role of p38 MAPK in ICAM-1 Expression of Vascular Endothelial Cells Induced by Lipopolysaccharide

Shock ◽  
2002 ◽  
Vol 17 (5) ◽  
pp. 433-438 ◽  
Author(s):  
Wensheng Yan ◽  
Keseng Zhao ◽  
Yong Jiang ◽  
Qiaobing Huang ◽  
Jingzhen Wang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
P38 Mapk ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial

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.

scholarly journals p38 MAPK Regulates Induction of HSPs in Human Esophageal Microvascular Endothelial Cells (HEMEC) in Response to Acidic pH Stress: Role of PI3/Akt

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
parvaneh rafiee ◽  
Monica Theriot ◽  
Victoria Nelson ◽  
Scott Horowitz ◽  
Aaron Rogaczewski ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
P38 Mapk ◽  
Microvascular Endothelial Cells ◽  
Acidic Ph ◽  
Ph Stress ◽  
Microvascular Endothelial

scholarly journals The Antioxidant Machinery of Young and Senescent Human Umbilical Vein Endothelial Cells and Their Microvesicles

2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Guillermo Bodega ◽  
Matilde Alique ◽  
Lourdes Bohórquez ◽  
Sergio Ciordia ◽  
María C. Mena ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Endothelial Cells ◽  
Superoxide Anion ◽  
Umbilical Vein ◽  
Redox Status ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Ros Scavengers ◽  
Antioxidant Machinery

We examine the antioxidant role of young and senescent human umbilical vein endothelial cells (HUVECs) and their microvesicles (MVs). Proteomic and Western blot studies have shown young HUVECs to have a complete and well-developed antioxidant system. Their MVs also contain antioxidant molecules, though of a smaller and more specific range, specialized in the degradation of hydrogen peroxide and the superoxide anion via the thioredoxin-peroxiredoxin system. Senescence was shown to be associated with a large increase in the size of the antioxidant machinery in both HUVECs and their MVs. These responses might help HUVECs and their MVs deal with the more oxidising conditions found in older cells. Functional analysis confirmed the antioxidant machinery of the MVs to be active and to increase in size with senescence. No glutathione or nonpeptide antioxidant (ascorbic acid and vitamin E) activity was detected in the MVs. Endothelial cells and MVs seem to adapt to higher ROS concentrations in senescence by increasing their antioxidant machinery, although this is not enough to recover completely from the senescence-induced ROS increase. Moreover, MVs could be involved in the regulation of the blood plasma redox status by functioning as ROS scavengers.

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