Flow-Mediated Signal Transduction in Endothelial Cells

1995 ◽  
pp. 46-61 ◽  
Author(s):  
Peter F. Davies
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells

Signal Transduction of Vascular Endothelial Cells

1995 ◽  
Vol 6 (2) ◽  
pp. 67-73
Author(s):  
Michihiko KUWANO ◽  
Hiroto IZUMI ◽  
Tadahisa SHONO ◽  
Sei-ichiro JIMI ◽  
Yukihiro WAKABAYASHI ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial

scholarly journals Melatonin and Microglia

2021 ◽  
Vol 22 (15) ◽  
pp. 8296
Author(s):  
Rüdiger Hardeland
Keyword(s):  
Oxidative Stress ◽  
Nitric Oxide ◽  
Signal Transduction ◽  
Endothelial Cells ◽  
Bacterial Infections ◽  
Melatonin Receptors ◽  
Sterile Inflammation ◽  
High Complexity ◽  
Anti Inflammatory ◽  
Multiple Signaling

Melatonin interacts in multiple ways with microglia, both directly and, via routes of crosstalk with astrocytes and neurons, indirectly. These effects of melatonin are of relevance in terms of antioxidative protection, not only concerning free-radical detoxification, but also in prevention of processes that cause, promote, or propagate oxidative stress and neurodegeneration, such as overexcitation, toxicological insults, viral and bacterial infections, and sterile inflammation of different grades. The immunological interplay in the CNS, with microglia playing a central role, is of high complexity and includes signaling toward endothelial cells and other leukocytes by cytokines, chemokines, nitric oxide, and eikosanoids. Melatonin interferes with these processes in multiple signaling routes and steps. In addition to canonical signal transduction by MT1 and MT2 melatonin receptors, secondary and tertiary signaling is of relevance and has to be considered, e.g., via the upregulation of sirtuins and the modulation of pro- and anti-inflammatory microRNAs. Many details concerning the modulation of macrophage functionality by melatonin are obviously also applicable to microglial cells. Of particular interest is the polarization toward M2 subtypes instead of M1, i.e., in favor of being anti-inflammatory at the expense of proinflammatory activities, which is well-documented in macrophages but also applies to microglia.

Heterogeneity of the signal transduction pathways for VEGF-induced MAPKs activation in human vascular endothelial cells

2001 ◽  
Vol 188 (2) ◽  
pp. 201-210 ◽  
Author(s):  
Rei Yashima ◽  
Mayumi Abe ◽  
Katsuhiro Tanaka ◽  
Hikaru Ueno ◽  
Kenya Shitara ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Signal Transduction Pathways ◽  
Vascular Endothelial

scholarly journals TNF-α Activates High-Mobility Group Box 1 - Toll-Like Receptor 4 Signaling Pathway in Human Aortic Endothelial Cells

2016 ◽  
Vol 38 (6) ◽  
pp. 2139-2151 ◽  
Author(s):  
Won Seok Yang ◽  
Nam Jeong Han ◽  
Jin Ju Kim ◽  
Mee Jeong Lee ◽  
Su-Kil Park
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
High Mobility ◽  
Neutralizing Antibody ◽  
High Mobility Group ◽  
Toll Like Receptor ◽  
Toll Like Receptor 4 ◽  
Aortic Endothelial Cells ◽  
Tnf Α ◽  
Human Aortic Endothelial Cells

Background/Aims: Toll-like receptor 4 (TLR4) interacts with endogenous substances as well as lipopolysaccharide. We explored whether TLR4 is implicated in tumor necrosis factor-α (TNF-α) signal transduction in human aortic endothelial cells. Methods: The pathway was evaluated by transfection of siRNAs, immunoprecipitation and Western blot analysis. Results: TNF-α activated spleen tyrosine kinase (Syk) within 10 min, which led to endothelin-1 (ET-1) production. TLR4 was also rapidly activated by TNF-α stimulation, as shown by recruitment of interleukin-1 receptor-associated kinase 1 to TLR4 and its adaptor molecule, myeloid differentiation factor 88 (MyD88). siRNA depletion of TLR4 markedly attenuated TNF-α-induced Syk activation and ET-1 production. TLR4 inhibitor (CLI-095), TLR4-neutralizing antibody and siRNA depletion of MyD88 also attenuated TNF-α-induced Syk activation. Syk was co-immunoprecipitated with TLR4, and TNF-α activated Syk bound to TLR4. High-mobility group box 1 (HMGB1) was rapidly released and associated with TLR4 after TNF-α stimulation with a peak at 5 min, which was prevented by N-acetylcysteine, an antioxidant. Glycyrrhizin (HMGB1 inhibitor), HMGB1-neutralizing antibody and siRNA depletion of HMGB1 all suppressed TNF-α-induced Syk activation and ET-1 production. Conclusion: Upon TNF-α stimulation, TLR4 is activated by HMGB1 that is immediately released after the generation of reactive oxygen species, and plays a crucial role in the signal transduction.

Signal Transduction Pathways in Endothelial Cells

2015 ◽  
pp. 99-116
Author(s):  
Una S. Ryan ◽  
Marilyn K. Glassberg ◽  
Anthony Johns
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Signal Transduction Pathways

Abstract 2390: Serotonin signal transduction in human endothelial cells

2010 ◽  
Author(s):  
Ali Zamani ◽  
Anshu Roy ◽  
Ling Zhai ◽  
Rangbao Li ◽  
Zhican Qu
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Human Endothelial Cells

scholarly journals Calcium/calmodulin transduces thrombin-stimulated secretion: studies in intact and minimally permeabilized human umbilical vein endothelial cells.

1992 ◽  
Vol 118 (6) ◽  
pp. 1501-1510 ◽  
Author(s):  
K A Birch ◽  
J S Pober ◽  
G B Zavoico ◽  
A R Means ◽  
B M Ewenstein
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Phorbol Esters ◽  
Umbilical Vein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Inhibitory Peptide ◽  
Permeabilized Cells ◽  
Calmodulin Binding ◽  
Umbilical Vein Endothelial Cells

Thrombin stimulates cultured endothelial cells (EC) to secrete stored von Willebrand factor (vWF), but the signal transduction pathways are poorly defined. Thrombin is known to elevate the concentration of intracellular calcium ([Ca2+]i) and to activate protein kinase C (PKC) in EC. Since both calcium ionophores and phorbol esters release vWF, both second messenger pathways have been postulated to participate in vWF secretion in response to naturally occurring agonists. We find that in intact human EC, vWF secretion stimulated by either thrombin or by a thrombin receptor activating peptide, TR(42-55), can be correlated with agonist-induced elevations of [Ca2+]i. Further evidence implicating calcium in the signal transduction pathway is suggested by the finding that MAPTAM, a cell-permeant calcium chelator, in combination with the extracellular calcium chelator EGTA, can inhibit thrombin-stimulated secretion. In contrast, the observation that staurosporine (a pharmacological inhibitor of PKC) blocks phorbol ester- but not thrombin-stimulated secretion provides evidence against PKC-mediated signal transduction. To examine further the signal transduction pathway initiated by thrombin, we developed novel conditions for minimal permeabilization of EC with saponin (4-8 micrograms/ml for 5-15 min at 37 degrees C) which allow the introduction of small extracellular molecules without the loss of large intracellular proteins and which retain thrombin-stimulated secretion. These minimally permeabilized cells secrete vWF in response to exogenous calcium, and EGTA blocks thrombin-induced secretion. Moreover, in these cells, thrombin-stimulated secretion is blocked by a calmodulin-binding inhibitory peptide but not by a PKC inhibitory peptide. Taken together, these findings demonstrate that thrombin-stimulated vWF secretion is transduced by a rise in [Ca2+]i and provide the first evidence for the role of calmodulin in this process.

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