Telmisartan attenuates hyperglycemia-aggravated VCAM-1 expression and monocytes adhesion in TNF[alpha]-stimulated endothelial cells by increasing GSK3[beta]-Ser9 phosphorylation

2017 ◽  
Author(s):  
Du-Hyong Cho ◽  
Sun-Ju Bae ◽  
Kee-Ho Song
Keyword(s):  
Endothelial Cells ◽  
Tnf Alpha

Induction of ICAM-1 by TNF-alpha, IL-1 beta, and LPS in human endothelial cells after downregulation of PKC

1992 ◽  
Vol 263 (4) ◽  
pp. C767-C772 ◽  
Author(s):  
C. L. Myers ◽  
S. J. Wertheimer ◽  
J. Schembri-King ◽  
T. Parks ◽  
R. W. Wallace
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Umbilical Vein ◽  
Interleukin 1 ◽  
Protein Kinase Inhibitors ◽  
Intercellular Adhesion Molecule ◽  
Tnf Alpha ◽  
Necrosis Factor Alpha ◽  
Western Blots ◽  
Mrna Induction

The intercellular adhesion molecule 1 (ICAM-1) is induced on endothelial cells by tumor necrosis factor-alpha (TNF-alpha), interleukin-1 beta (IL-1 beta), and lipopolysaccharide (LPS). We have reported the sensitivity of cytokine-induced ICAM-1 expression to protein kinase inhibitors, including inhibitors of protein kinase C (PKC) [C. L. Myers, S. N. Desai, J. Schembri-King, G. L. Letts, and R. W. Wallace. Am. J. Physiol. 262 (Cell Physiol. 31): C365-C373, 1992]. To directly investigate the role of PKC in ICAM-1 induction, we downregulated PKC by pretreatment of human umbilical vein endothelial cells with phorbol 12-myristate 13-acetate (PMA) and assessed ICAM-1 protein and mRNA induction elicited by subsequent exposure to inflammatory stimuli. PMA treatment results in ICAM-1 protein induction that declines to basal levels by 3 days. Western blots of endothelial cell lysates reveal a nearly complete loss of immunologically reactive PKC. Subsequent activation with cytokine or LPS leads to reinduction of ICAM-1 protein and mRNA; however, the cells no longer produced substantial amounts of ICAM-1 protein or mRNA in response to PMA stimulation. Cross desensitization is observed with phorbol dibutyrate, while 4 alpha-phorbol has no desensitizing effect. The data indicate that PKC activation, while capable of inducing ICAM-1 expression, is not essential for ICAM-1 induction by the inflammatory mediators TNF-alpha, IL-1 beta, or LPS.

scholarly journals Activation of AMP-Activated Protein Kinase by Adenine Alleviates TNF-Alpha-Induced Inflammation in Human Umbilical Vein Endothelial Cells

PLoS ONE ◽  
2015 ◽  
Vol 10 (11) ◽  
pp. e0142283 ◽  
Author(s):  
Yi-Fang Cheng ◽  
Guang-Huar Young ◽  
Jiun-Tsai Lin ◽  
Hyun-Hwa Jang ◽  
Chin-Chen Chen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Umbilical Vein ◽  
Tnf Alpha ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Amp Activated Protein Kinase

scholarly journals Caveolae/lipid raft modulates TNF‐alpha‐induced upregulation of cell adhesion molecules in human brain endothelial cells

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Sung Yong Eum ◽  
Ibolya E Andras ◽  
Yean Jung Choi ◽  
Bernhard Hennig ◽  
Michal Toborek
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Human Brain ◽  
Adhesion Molecules ◽  
Lipid Raft ◽  
Cell Adhesion Molecules ◽  
Tnf Alpha ◽  
Brain Endothelial Cells

scholarly journals Differential regulation by cytokines of constitutive and stimulated secretion of von Willebrand factor from endothelial cells

Blood ◽  
1990 ◽  
Vol 75 (3) ◽  
pp. 688-695 ◽  
Author(s):  
EM Paleolog ◽  
DC Crossman ◽  
JH McVey ◽  
JD Pearson
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Messenger Rna ◽  
Cell Injury ◽  
Interleukin 1 ◽  
Tnf Alpha ◽  
Detectable Effect ◽  
Dependent Manner ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract We examined the effect of cytokines on basal and agonist-stimulated release of von Willebrand factor (vWf) by human endothelial cells. Treatment of endothelial cells for up to 48 hours with human recombinant or purified interleukin 1 (IL-1) or human recombinant tumor necrosis factor-alpha (TNF-alpha) did not significantly affect constitutive secretion of vWf or intracellular levels of vWf, although basal prostacyclin (PGI2) production was markedly enhanced. In contrast, both IL-1 and TNF-alpha modulated vWf release in response to thrombin or phorbol ester. Pretreatment of endothelial cells for 2 hours with either cytokine enhanced by up to threefold the stimulatory effect of a subsequent 60-minute exposure to thrombin. Addition of cycloheximide (5 micrograms/mL) during the preincubation abolished this enhancement. Moreover, if the cytokine pretreatment time was extended to 24 hours, agonist-stimulated vWf release was significantly suppressed. Cytokine treatment for 2 or 24 hours had no detectable effect on levels of vWf messenger RNA. The effects of cytokines were not the result of contamination with bacterial lipopolysaccharide and were not attributable to endothelial cell injury. These results show that cytokines have little or no direct effect on vWf release from endothelial cells but can significantly modulate its acute release in response to other stimuli in a complex time- and dose-dependent manner.

scholarly journals TNF-alpha inhibits pregnancy-adapted Ca2+ signaling in uterine artery endothelial cells

2019 ◽  
Vol 488 ◽  
pp. 14-24 ◽  
Author(s):  
Amanda C. Ampey ◽  
Derek S. Boeldt ◽  
Luca Clemente ◽  
Mary A. Grummer ◽  
FuXian Yi ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Uterine Artery ◽  
Tnf Alpha

scholarly journals Tumor necrosis factor alpha induces endothelial galactosyl transferase activity and verocytotoxin receptors. Role of specific tumor necrosis factor receptors and protein kinase C

Blood ◽  
1995 ◽  
Vol 85 (3) ◽  
pp. 734-743 ◽  
Author(s):  
NC van de Kar ◽  
T Kooistra ◽  
M Vermeer ◽  
W Lesslauer ◽  
LA Monnens ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Synthesis ◽  
Protein Kinase ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tnf Alpha ◽  
Transferase Activity ◽  
Necrosis Factor Alpha ◽  
Galactosyl Transferase ◽  
Necrosis Factor

Infections with verocytotoxin (VT) producing Escherichia coli have been strongly implicated in the epidemic form of hemolytic uremic syndrome (HUS). Endothelial damage plays a central role in the pathogenesis of HUS. In vitro studies have shown that VT can damage endothelial cells after interaction with its cellular receptor globotriaosylceramide (GbOse3cer). Cytokines, such as tumor necrosis factor alpha (TNF alpha) and interleukin-1 (IL-1) can potentiate the toxic effect of VT by inducing a protein-synthesis dependent increase in VT receptors on endothelial cells. In this study, the mechanisms underlying the increase in endothelial VT receptors induced by TNF alpha were studied in more detail. To investigate which proteins were involved in this induction, endothelial cells were incubated with and without TNF alpha in the presence of 14C-galactose or 14C-glucose. Thin-layer chromatography (TLC) analysis of the glycolipid extracts of these cells demonstrated a markedly enhanced incorporation of 14C-galactose in GbOse3cer and other galactose-containing glycolipids, suggesting that TNF alpha enhanced galactosyl-transferase activity. To examine the role of the two recently cloned TNF-receptors (TNFR-p75 and TNFR-p55) in the TNF alpha-induced increase in GbOse3cer in human endothelial cells, cells were incubated with TNF alpha, the TNFR-p55 selective R32W-S86T- TNF alpha-mutant, or the TNFR-p75 selective D143N-A145R-TNF alpha- mutant. The effect of TNF alpha activation, determined by binding- experiments with 125I-VT-1, could be largely, but not completely mimicked by R32W-S86T-TNF alpha. Although incubation of cells with D143N-A145R-TNF alpha did not show an increase in VT-1 binding, the monoclonal antibody utr-1, which prevents binding to TNFR-p75, decreased the TNF alpha-induced VT-1 binding. Activation of protein kinase C (PKC) by phorbol ester increases the expression of VT-1 receptors; this effect was prevented by the PKC inhibitor Ro31–8220 and by homologous desensitization by pretreatment with phorbol ester. In contrast, the presence of the protein kinase inhibitor Ro31–8220 or desensitization of PKC activity reduced the TNF alpha-induced increase in VT-1 receptors maximally by 50% and 24%, respectively. Comparable reductions in overall protein synthesis and the synthesis of E-selectin and plasminogen activator inhibitor-1 (PAI-1) were observed. This suggests an effect on general protein synthesis rather than a specific effect of PKC in the signal transduction pathway, by which TNF alpha induces VT-1 receptors. Our results indicate that TNF alpha can increase the VT-1 receptors on endothelial cells by inducing galactosyl- transferase activity, that this action of TNF alpha mainly occurs via the TNFR-p55; and that PKC activation increases expression of VT-1 receptors by a separate mechanism that acts additively to the TNF alpha- induced increase in VT-1 receptors.

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