scholarly journals Concentration-Dependent Effects of N-3 Long-Chain Fatty Acids on Na,K-ATPase Activity in Human Endothelial Cells

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 128 ◽  
Author(s):  
Roberta Cazzola ◽  
Matteo Della Porta ◽  
Sara Castiglioni ◽  
Luciano Pinotti ◽  
Jeanette A.M. Maier ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Atpase Activity ◽  
Membrane Fluidity ◽  
Cell Function ◽  
Unsaturation Index ◽  
Linear Increase ◽  
Human Endothelial Cells ◽  
Epa And Dha ◽  
Low Concentrations ◽  
Vascular Protective Effect

N-3 eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) seem to prevent endothelial dysfunction, a crucial step in atherogenesis, by modulating the levels of vasoactive molecules and by influencing Na,K-ATPase activity of vascular myocytes. The activity of endothelial Na,K-ATPase controls the ionic homeostasis of the neighboring cells, as well as cell function. However, controversy exists with respect to the vascular protective effect of EPA and DHA. We argue that this dispute might be due to the use of different concentrations of EPA and DHA in different studies. Therefore, this study was designed to define an optimal concentration of EPA and DHA to investigate endothelial function. For this purpose, human endothelial cells were exposed for 24 h to different concentrations of DHA or EPA (0–20 μM) to study membrane fluidity, peroxidation potential and Na,K-ATPase activity. EPA and DHA were linearly incorporated and this incorporation was mirrored by the linear increase of unsaturation index, membrane fluidity, and peroxidation potential. Na,K-ATPase activity peaked at 3.75 μM of EPA and DHA and then gradually decreased. It is noteworthy that DHA effects were always more pronounced than EPA. Concluding, low concentrations of EPA and DHA minimize peroxidation sensitivity and optimize Na,K-ATPase activity.

Cholesterol and ω-3 fatty acids inhibit Na, K-ATPase activity in human endothelial cells

1999 ◽  
Vol 142 (2) ◽  
pp. 327-333 ◽  
Author(s):  
Vincent Mayol ◽  
Marie-Josée Duran ◽  
Alain Gerbi ◽  
Françoise Dignat-George ◽  
Samuel Lévy ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Endothelial Cells ◽  
Atpase Activity ◽  
Human Endothelial Cells

Effects of ouabain on proliferation of human endothelial cells correlate with Na+,K+-ATPase activity and intracellular ratio of Na+ and K+

2016 ◽  
Vol 81 (8) ◽  
pp. 876-883 ◽  
Author(s):  
A. M. Tverskoi ◽  
S. V. Sidorenko ◽  
E. A. Klimanova ◽  
O. A. Akimova ◽  
L. V. Smolyaninova ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Atpase Activity ◽  
Human Endothelial Cells

scholarly journals Exogenous tat protein activates human endothelial cells [see comments]

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2774-2780 ◽  
Author(s):  
FM Hofman ◽  
AD Wright ◽  
MM Dohadwala ◽  
F Wong-Staal ◽  
SM Walker
Keyword(s):  
Endothelial Cells ◽  
Leukocyte Adhesion ◽  
Protein A ◽  
Cell Permeability ◽  
Tat Protein ◽  
Human Endothelial Cells ◽  
Hiv Replication ◽  
Necrosis Factor Alpha ◽  
Low Concentrations ◽  
Infected Cells

Abstract tat protein, a human immunodeficiency virus (HIV) gene product that functions as a transactivator for HIV replication, is known to be secreted extracellularly by infected cells. To determine the potential role of tat in the dissemination of HIV into extravascular tissue, this protein was examined for its ability to activate human endothelial cells. The results show that tat does indeed stimulate endothelial cells. This is evidenced by their expression of the endothelial- leukocyte adhesion molecules, E-selectin, critical for the initial binding of leukocytes to the blood vessel wall, and their increased synthesis of interleukin-6 (IL-6), a cytokine known to enhance endothelial cell permeability. Furthermore, tat acts synergistically with low concentrations of tumor necrosis factor-alpha to enhance IL-6 secretion. These data suggest that extracellular tat protein secreted or released into the microenvironment may contribute significantly to the determination of specific sites of leukocyte binding to blood vessels, to transmigration into tissue, and to eventual dissemination of HIV-infected cells or free virions into tissue.

scholarly journals The CXCL2/IL8/CXCR2 Pathway Is Relevant for Brain Tumor Malignancy and Endothelial Cell Function

2021 ◽  
Vol 22 (5) ◽  
pp. 2634
Author(s):  
Ruth Urbantat ◽  
Anne Blank ◽  
Irina Kremenetskaia ◽  
Peter Vajkoczy ◽  
Güliz Acker ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Function ◽  
The Cancer Genome Atlas ◽  
Human Endothelial Cells ◽  
In Vitro Proliferation ◽  
Endothelial Cell Function ◽  
Human Gbm ◽  
And Migration ◽  
The Impact

We aimed to evaluate the angiogenic capacity of CXCL2 and IL8 effecting human endothelial cells to clarify their potential role in glioblastoma (GBM) angiogenesis. Human GBM samples and controls were stained for proangiogenic factors. Survival curves and molecule correlations were obtained from the TCGA (The Cancer Genome Atlas) database. Moreover, proliferative, migratory and angiogenic activity of peripheral (HUVEC) and brain specific (HBMEC) primary human endothelial cells were investigated including blockage of CXCR2 signaling with SB225502. Gene expression analyses of angiogenic molecules from endothelial cells were performed. Overexpression of VEGF and CXCL2 was observed in GBM patients and associated with a survival disadvantage. Molecules of the VEGF pathway correlated but no relation for CXCR1/2 and CXCL2/IL8 was found. Interestingly, receptors of endothelial cells were not induced by addition of proangiogenic factors in vitro. Proliferation and migration of HUVEC were increased by VEGF, CXCL2 as well as IL8. Their sprouting was enhanced through VEGF and CXCL2, while IL8 showed no effect. In contrast, brain endothelial cells reacted to all proangiogenic molecules. Additionally, treatment with a CXCR2 antagonist led to reduced chemokinesis and sprouting of endothelial cells. We demonstrate the impact of CXCR2 signaling on endothelial cells supporting an impact of this pathway in angiogenesis of glioblastoma.

Thrombin induces Contraction And increased 51-Cr Release from Cultured Human Endothelial Cells

1979 ◽  
Author(s):  
K.S. Galdal ◽  
S.A. Evensen
Keyword(s):  
Endothelial Cells ◽  
Calf Serum ◽  
Linear Increase ◽  
Foetal Calf Serum ◽  
Human Endothelial Cells ◽  
Trypan Blue Exclusion ◽  
Trypan Blue Exclusion Test ◽  
Release Assay

Injury to human endothelial cells(EC) in primary culture was evaluated by a 51-Cr release assay, phase contrast microscopy and the trypan blue exclusion test. Normal integrity of EC, was maintained and 51-Cr release showed a slow linear increase during 24h incubation with either RPMI 1640 supplemented with 20% foetal calf serum, glutamine and antibiotics(SCM) or normal human serum(NHS). Thrombin in a concentration as low as 0.1 IU/ml induced obvious contraction of EC incubated in SCM, but the cells remained fixed to the bottom of the wells. Cell contraction was maximal after 15min and disappeared within 4h. 51-Cr release increased 2-3 fold within a few minutes and remained increased during an incubation period of 4h. The injurious effect of thrombin was inhibited in SCM containing hirudin(l.7 u/ml) or in NHS. ADP(10-5 M), endotoxin (0.1mg/ml) and 5 vasoactive agents adrenalin 5.5 10-5, noradrenalin 5.9 10-5 M, histamine 9.10-4 M, bradykinin 7.5 10-7 M and serotonin 10-5 M) did not cause cellular injury. Cultured human EC are injured by thrombin. The other tested agents do not appear to induce direct injury in vitro, but may interact with cellular elements in the blood to produce the endothelial injury previously observed in vivo.

scholarly journals Exogenous tat protein activates human endothelial cells [see comments]

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2774-2780 ◽  
Author(s):  
FM Hofman ◽  
AD Wright ◽  
MM Dohadwala ◽  
F Wong-Staal ◽  
SM Walker
Keyword(s):  
Endothelial Cells ◽  
Leukocyte Adhesion ◽  
Protein A ◽  
Cell Permeability ◽  
Tat Protein ◽  
Human Endothelial Cells ◽  
Hiv Replication ◽  
Necrosis Factor Alpha ◽  
Low Concentrations ◽  
Infected Cells

tat protein, a human immunodeficiency virus (HIV) gene product that functions as a transactivator for HIV replication, is known to be secreted extracellularly by infected cells. To determine the potential role of tat in the dissemination of HIV into extravascular tissue, this protein was examined for its ability to activate human endothelial cells. The results show that tat does indeed stimulate endothelial cells. This is evidenced by their expression of the endothelial- leukocyte adhesion molecules, E-selectin, critical for the initial binding of leukocytes to the blood vessel wall, and their increased synthesis of interleukin-6 (IL-6), a cytokine known to enhance endothelial cell permeability. Furthermore, tat acts synergistically with low concentrations of tumor necrosis factor-alpha to enhance IL-6 secretion. These data suggest that extracellular tat protein secreted or released into the microenvironment may contribute significantly to the determination of specific sites of leukocyte binding to blood vessels, to transmigration into tissue, and to eventual dissemination of HIV-infected cells or free virions into tissue.

scholarly journals Injury of Endothelial Cells in Culture Induced by Low Density Lipoproteins

1977 ◽  
Author(s):  
T. Henriksen ◽  
S.A. Evensen ◽  
B. Carlander
Keyword(s):  
Endothelial Cells ◽  
Morphological Changes ◽  
Low Density Lipoproteins ◽  
Culture Vessel ◽  
Low Density ◽  
Human Endothelial Cells ◽  
Injurious Effect ◽  
Low Concentrations ◽  
Release Assay ◽  
Normal Human

The effect of low density lipoproteins on human endothelial cells in primary culture was investigated. The effect was evaluated by use of a Cr-release assay and phase contrast microscopy. When the cells were exposed to low density lipoproteins(LDL, d=l.019-1.063g/ml)suspended in RPMI 1640 the endothelial cells underwent extensive morphological changes and detached from the bottom of the culture vessel. Addition of lipoprotein-poor serum (d>1.21 g/ml) prevented the injurious effect of the LDL fraction at low concentrations, and to a lesser extent as the LDL concentration was raised. Unfractionated serum from hyperlipoproteinemic patients(type IIa) did not appear to injure endothelial cells. Addition of the LDL fraction, however, had a more pronounced effect on the cells when added to hyper-lipoproteinemic serum than to normal human serum. Thus, LDL as obtained by ultracentrifugation may have an injurious effect on cultured human endothelial cells. Secondly, hyperlipoproteinemic serum appears to contain factors which augment the effect of the added LDL fraction.

Hyperoxia reduces plasma membrane fluidity: a mechanism for endothelial cell dysfunction

1986 ◽  
Vol 60 (3) ◽  
pp. 826-835 ◽  
Author(s):  
E. R. Block ◽  
J. M. Patel ◽  
K. J. Angelides ◽  
N. P. Sheridan ◽  
L. C. Garg
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Pulmonary Artery ◽  
Atpase Activity ◽  
Membrane Fluidity ◽  
Atp Content ◽  
Aortic Endothelial Cells ◽  
Plasma Membrane Fluidity ◽  
High O2 ◽  
Aortic Endothelial

To evaluate the relative contributions of three possible mechanisms that can be advanced to explain the observation that hyperoxia decreases serotonin uptake by endothelial cells, we examined the effect of high O2 tensions on Na+-K+-ATPase activity, ATP content, and plasma membrane fluidity in cultured endothelial cells. Confluent monolayers of pulmonary artery and aortic endothelial cells were exposed to 95% O2 (hyperoxia) or 20% O2 (controls) in 5% CO2 at 1 ATA for 4–42 h. Exposure to high O2 tensions had no effect on Na+-K+-ATPase activity or ATP content in pulmonary artery or aortic endothelial cells in culture. However, hyperoxia decreased the fluidity of the plasma membrane of pulmonary artery and aortic endothelial cells in culture, and the time course for the decrease in fluidity parallels that of the hyperoxic inhibition of serotonin transport. These results indicate that hyperoxia decreases fluidity in the hydrophobic core of the plasma membranes of cultured endothelial cells. Such decreases in plasma membrane fluidity may be responsible for hyperoxia-induced alterations in membrane function including decreases in transmembrane transport of amines.

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