scholarly journals Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells. Essential role for a herbimycin-sensitive kinase.

1996 ◽  
Vol 98 (11) ◽  
pp. 2623-2631 ◽  
Author(s):  
M Takahashi ◽  
B C Berk
Keyword(s):  
Endothelial Cells ◽  
Shear Stress ◽  
Protein Kinase ◽  
Essential Role ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Eosinophil adhesion under flow conditions activates mechanosensitive signaling pathways in human endothelial cells

2005 ◽  
Vol 202 (6) ◽  
pp. 865-876 ◽  
Author(s):  
Susan L. Cuvelier ◽  
Smitha Paul ◽  
Neda Shariat ◽  
Pina Colarusso ◽  
Kamala D. Patel
Keyword(s):  
Endothelial Cells ◽  
Shear Stress ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Leukocyte Adhesion ◽  
Focal Adhesions ◽  
Mitogen Activated Protein Kinase ◽  
Flow Conditions ◽  
Endothelial Cell Surface ◽  
Mitogen Activated Protein

Leukocyte transmigration can be affected by shear stress; however, the mechanisms by which shear stress modulates transmigration are unknown. We found that adhesion of eosinophils or an eosinophilic cell line to intereukin 4–stimulated endothelial cells led to a shear-dependent increase in endothelial cell intracellular calcium and increased phosphorylation of extracellular signal-regulated kinase (ERK) 2, but not c-Jun NH2-terminal kinase or p38 mitogen-activated protein kinase. Latex beads coated with antibodies were used to characterize the role of specific endothelial cell surface molecules in initiating signaling under shear conditions. We found that ligation of either vascular cell adhesion molecule–1 or E-selectin, but not major histocompatibility complex class I, induced a shear-dependent increase in ERK2 phosphorylation in cytokine-stimulated endothelial cells. Disassembly of the actin cytoskeleton with latrunculin A prevented ERK2 phosphorylation after adhesion under flow conditions, supporting a role for the cytoskeleton in mechanosensing. Rapid phosphorylation of focal adhesion kinase and paxillin occurred under identical conditions, suggesting that focal adhesions were also involved in mechanotransduction. Finally, we found that Rho-associated protein kinase and calpain were both critical in the subsequent transendothelial migration of eosinophils under flow conditions. These data suggest that ligation of leukocyte adhesion molecules under flow conditions leads to mechanotransduction in endothelial cells, which can regulate subsequent leukocyte trafficking.

scholarly journals Fluid Shear Stress Stimulates Big Mitogen-activated Protein Kinase 1 (BMK1) Activity in Endothelial Cells

1999 ◽  
Vol 274 (1) ◽  
pp. 143-150 ◽  
Author(s):  
Chen Yan ◽  
Masafumi Takahashi ◽  
Masanori Okuda ◽  
Jiing-Dwan Lee ◽  
Bradford C. Berk
Keyword(s):  
Endothelial Cells ◽  
Shear Stress ◽  
Protein Kinase ◽  
Fluid Shear Stress ◽  
Mitogen Activated Protein Kinase ◽  
Fluid Shear ◽  
Mitogen Activated Protein

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.

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