scholarly journals Glossogyne tenuifolia Extract Increases Nitric Oxide Production in Human Umbilical Vein Endothelial Cells

2021 ◽  
Vol 14 (6) ◽  
pp. 577
Author(s):  
Chin-Feng Hsuan ◽  
Thung-Lip Lee ◽  
Wei-Kung Tseng ◽  
Chau-Chung Wu ◽  
Chi-Chang Chang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Western Blot ◽  
Umbilical Vein ◽  
No Production ◽  
Enos Expression ◽  
Human Umbilical Vein ◽  
Whole Plant ◽  
Umbilical Vein Endothelial Cells ◽  
Glossogyne Tenuifolia

The vascular nitric oxide (NO) system has a protective effect in atherosclerosis. NO is generated from the conversion of L-arginine to L-citrulline by the enzymatic action of endothelial NO synthase (eNOS). Compounds with the effect of enhancing eNOS expression are considered to be candidates for the prevention of atherosclerosis. In this study, extracts from the aerial, root, and whole plant of Glossogyne tenuifolia (GT) were obtained with ethanol, n-hexane, ethyl acetate (EA), and methanol extraction, respectively. The effects of these GT extracts on the synthesis of NO and the expression of eNOS in human umbilical vein endothelial cells (HUVECs) were investigated. NO production was determined as nitrite by colorimetry, following the Griess reaction. The treatment of HUVECs with EA extract from the root of GT and n-hexane, methanol, and ethanol extract from the aerial, root, and whole plant of GT increased NO production in a dose-dependent manner. When at a dose of 160 μg/mL, NO production increased from 0.9 to 18.4-fold. Among these extracts, the methanol extract from the root of GT (R/M GTE) exhibited the most potent effect on NO production (increased by 18.4-fold). Furthermore, using Western blot and RT–PCR analysis, treatment of HUVECs with the R/M GTE increased both eNOS protein and mRNA expression. In addition, Western blot analysis revealed that the R/M GTE increased eNOS phosphorylation at serine1177 as early as 15 min after treatment. The chemical composition for the main ingredients was also performed by HPLC analysis. In conclusion, the present study demonstrated that GT extracts increased NO production in HUVECs and that the R/M GTE increased NO production via increasing eNOS expression and activation by phosphorylation of eNOS at serine1177.

Abstract 43: A20 Plays as a Regulator in Tnfα-induced Injury of Human Umbilical Vein Endothelial Cells Through Tak1-dependent Pathway

2017 ◽  
Vol 121 (suppl_1) ◽  
Author(s):  
Lei Li ◽  
Jiafeng Lin ◽  
Maoping Chu ◽  
Kangting Ji ◽  
Lianpin Wu
Keyword(s):  
Endothelial Cells ◽  
P38 Mapk ◽  
Cell Apoptosis ◽  
Umbilical Vein ◽  
No Production ◽  
Enos Expression ◽  
Mapk Phosphorylation ◽  
Human Umbilical Vein ◽  
Over Expression ◽  
Umbilical Vein Endothelial Cells

A20, a negative regulator of nuclear factor κB signaling, has been shown to attenuate atherosclerotic events. Transforming growth factor beta-activated kinase 1 (TAK1) plays a critical role in TNFα-induced atherosclerosis via endothelial nitric oxide (NO) synthase (eNOS) uncoupling and NO reduction. Aims: In the study, we investigated the hypothesis that A20 protected endothelial cells induced by TNFα through modulating eNOS activity and TAK1 signalling. Human umbilical vein endothelial cells (HUVECs) were stimulated by TNFα. The impact of A20 on cell apoptosis, eNOS expression and NO production and related TAK1 pathway were detected. Both eNOS and NO production were remarkably reduced, TAK1and p38 MAPK phosphorylation, HUVECs apoptosis increased after TNFα stimulation for 2 hrs, all of which were effectively attenuated by A20 over-expression. Inhibition of A20 significantly activated TAK1, p38 MAPK phosphorylation, and cell apoptosis, but eNOS expression, NO production decreased. Furthermore, p38 MAPK expression was suppressed by A20 over-expression, but re-enhanced by inhibiting A20 or activation of TAK1. Furtherly, TNFα-induced suppression of eNOS and NO production were largely prevented by silencing p38 MAPK. Collectively, our results suggested that A20-mediated TAK1 inactivation suppresses p38 MAPK and regulated MAPK/eNOS pathway, which contributes to endothelial cell survival and function preservation.

scholarly journals Role of Rutin on Nitric Oxide Synthesis in Human Umbilical Vein Endothelial Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Azizah Ugusman ◽  
Zaiton Zakaria ◽  
Kien Hui Chua ◽  
Nor Anita Megat Mohd Nordin ◽  
Zaleha Abdullah Mahdy
Keyword(s):  
Oxidative Stress ◽  
Nitric Oxide ◽  
Endothelial Cells ◽  
Umbilical Vein ◽  
Enos Gene ◽  
No Production ◽  
Protective Effects ◽  
Human Umbilical Vein ◽  
Gene And Protein Expression ◽  
Umbilical Vein Endothelial Cells

Nitric oxide (NO), produced by endothelial nitric oxide synthase (eNOS), is a major antiatherogenic factor in the blood vessel. Oxidative stress plays an important role in the pathogenesis of various cardiovascular diseases, including atherosclerosis. Decreased availability of endothelial NO promotes the progression of endothelial dysfunction and atherosclerosis. Rutin is a flavonoid with multiple cardiovascular protective effects. This study aimed to investigate the effects of rutin on eNOS and NO production in cultured human umbilical vein endothelial cells (HUVEC). HUVEC were divided into four groups: control; oxidative stress induction with 180 μM H2O2; treatment with 300 μM rutin; and concomitant induction with rutin and H2O2for 24 hours. HUVEC treated with rutin produced higher amount of NO compared to control (P<0.01). In the oxidative stress-induced HUVEC, rutin successfully induced cells’ NO production (P<0.01). Rutin promoted NO production in HUVEC by inducing eNOS gene expression (P<0.05), eNOS protein synthesis (P<0.01), and eNOS activity (P<0.05). Treatment with rutin also led to increased gene and protein expression of basic fibroblast growth factor (bFGF) in HUVEC. Therefore, upregulation of eNOS expression by rutin may be mediated by bFGF. The results showed that rutin may improve endothelial function by augmenting NO production in human endothelial cells.

scholarly journals Interleukin-6 Impairs the Insulin Signaling Pathway, Promoting Production of Nitric Oxide in Human Umbilical Vein Endothelial Cells

2007 ◽  
Vol 27 (6) ◽  
pp. 2372-2383 ◽  
Author(s):  
Francesco Andreozzi ◽  
Emanuela Laratta ◽  
Cristina Procopio ◽  
Marta Letizia Hribal ◽  
Angela Sciacqua ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Interleukin 6 ◽  
Umbilical Vein ◽  
Inhibitory Effect ◽  
Pi3 Kinase ◽  
No Production ◽  
Human Umbilical Vein ◽  
Impaired Insulin ◽  
Umbilical Vein Endothelial Cells

ABSTRACT Interleukin 6 (IL-6) is an independent predictor of type 2 diabetes and cardiovascular disease and is correlated with insulin resistance. Insulin stimulates nitric oxide (NO) production through the IRS-1/PI3-kinase/Akt/eNOS pathway (where IRS-1 is insulin receptor substrate 1, PI3-kinase is phosphatidylinositol 3-kinase, and eNOS is endothelial NO synthase). We asked if IL-6 affects insulin vasodilator action both in human umbilical vein endothelial cells (HUVEC) and in the aortas of C57BL/6J mice and whether this inhibitory effect was caused by increased Ser phosphorylation of IRS-1. We observed that IL-6 increased IRS-1 phosphorylation at Ser312 and Ser616; these effects were paralleled by increased Jun N-terminal protein kinase (JNK) and extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylation and reversed by JNK and ERK1/2 inhibition. In addition, IL-6 treatment resulted in impaired IRS-1 phosphorylation at Tyr612, a site essential for engaging PI3-kinase. Furthermore, IL-6 treatment reduced insulin-stimulated phosphorylation of eNOS at the stimulatory Ser1177 site and impaired insulin-stimulated eNOS dephosphorylation at the inhibitory Thr495 site. Insulin-stimulated eNOS activation and NO production were also inhibited by IL-6; these effects were reversed by inhibition of JNK and ERK1/2. Treatment of C57BL/6J mice with IL-6 resulted in impaired insulin-dependent activation of the Akt/eNOS pathway in the aorta as a result of JNK and ERK1/2 activation. Our data suggest that IL-6 impairs the vasodilator effects of insulin that are mediated by the IRS-1/PI3-kinase/Akt/eNOS pathway through activation of JNK and ERK1/2.

scholarly journals Estradiol-17β Stimulates Specific Receptor and Endogenous Nitric Oxide-Dependent Dynamic Endothelial Protein S-Nitrosylation: Analysis of Endothelial Nitrosyl-Proteome

Endocrinology ◽  
2010 ◽  
Vol 151 (8) ◽  
pp. 3874-3887 ◽  
Author(s):  
Hong-hai Zhang ◽  
Lin Feng ◽  
Itamar Livnat ◽  
Jeong-Kyu Hoh ◽  
Jae-Yoon Shim ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Umbilical Vein ◽  
Cell Structure ◽  
Protein S ◽  
No Production ◽  
Two Dimensional ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Estradiol 17Β

Covalent adduction of a nitrosyl group to cysteines [S-nitrosylation (S-NO)] is emerging as a key route for nitric oxide (NO) to directly modulate protein functions. Here, we studied the effects of estrogens on endothelial protein S-NO and analyzed the nitrosyl-proteomes by biotin/CyDye switch technique combined with two-dimensional fluorescence difference gel electrophoresis and identified nitrosoproteins by matrix-assisted laser desorption/ionization-time of flight mass spectrometry. Estradiol-17β (E2) rapidly stimulated protein S-NO in human umbilical vein endothelial cells, maximizing within 10- to 30-min post-E2 (10 nm) exposure. E2-BSA also rapidly stimulated protein S-NO. Both E2 and E2-BSA-induced protein S-NO was blocked by ICI 182,780 and N-nitro-l-arginine-methylester. Human umbilical vein endothelial cells expressed estrogen receptor (ER)α and ERβ; both seemed to be required for E2 stimulation of protein S-NO because: 1) neither ERα or ERβ agonist alone, but their combination, stimulated protein S-NO; and 2) either ERα or ERβ antagonist blocked E2-induced protein S-NO. Numerous nitrosoproteins (spots) were observed on two-dimensional fluorescence difference gel. One hundred spots of interest were picked up; 58 were identified and, of which 15 were novel nitrosoproteins, 28 were up-regulated, 11 were decreased, and the rest were unchanged by E2. Pathway analysis suggested that nitrosoproteins are involved in regulating various endothelial functions, including apoptosis, cell structure and metabolism, redox homeostasis, etc. Thus, estrogens stimulate dynamic endothelial protein S-NO via mechanisms linked to specific ERs possibly on the plasma membrane and endogenous NO. These findings signify a critical next step for the understanding of the biological targets of enhanced NO production by estrogens.

scholarly journals Cilostazol Induces eNOS and TM Expression via Activation with Sirtuin 1/Krüppel-like Factor 2 Pathway in Endothelial Cells

2021 ◽  
Vol 22 (19) ◽  
pp. 10287
Author(s):  
Chih-Hsien Wu ◽  
Yi-Lin Chiu ◽  
Chung-Yueh Hsieh ◽  
Guo-Shiang Tsung ◽  
Lian-Shan Wu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Endothelial Nitric Oxide Synthase ◽  
Umbilical Vein ◽  
Sirtuin 1 ◽  
No Production ◽  
Beneficial Effects ◽  
Umbilical Vein Endothelial Cells ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Cilostazol was suggested to be beneficial to retard in-stent atherosclerosis and prevent stent thrombosis. However, the mechanisms responsible for the beneficial effects of cilostazol are not fully understood. In this study, we attempted to verify the mechanism of the antithrombotic effect of cilostazol. Human umbilical vein endothelial cells (HUVECs) were cultured with various concentrations of cilostazol to verify its impact on endothelial cells. KLF2, silent information regulator transcript-1 (SIRT1), endothelial nitric oxide synthase (eNOS), and endothelial thrombomodulin (TM) expression levels were examined. We found cilostazol significantly activated KLF2 expression and KLF2-related endothelial function, including eNOS activation, Nitric oxide (NO) production, and TM secretion. The activation was regulated by SIRT1, which was also stimulated by cilostazol. These findings suggest that cilostazol may be capable of an antithrombotic and vasculoprotective effect in endothelial cells.

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