scholarly journals Marine Bromophenol Bis(2,3,6-Tribromo-4,5-Dihydroxybenzyl)ether Inhibits Angiogenesis in Human Umbilical Vein Endothelial Cells and Reduces Vasculogenic Mimicry in Human Lung Cancer A549 Cells

Marine Drugs ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. 641
Author(s):  
Songtao Dong ◽  
Zhongyuan Chen ◽  
Li Wang ◽  
Yankai Liu ◽  
Dimitrios Stagos ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Biological Activities ◽  
Umbilical Vein ◽  
Vasculogenic Mimicry ◽  
A549 Cells ◽  
Human Lung Cancer ◽  
Potential Candidate ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

Angiogenesis, including the growth of new capillary blood vessels from existing ones and the malignant tumors cells formed vasculogenic mimicry, is quite important for the tumor metastasis. Anti-angiogenesis is one of the significant therapies in tumor treatment, while the clinical angiogenesis inhibitors usually exhibit endothelial cells dysfunction and drug resistance. Bis(2,3,6-tribromo-4,5-dihydroxybenzyl)ether (BTDE), a marine algae-derived bromophenol compound, has shown various biological activities, however, its anti-angiogenesis function remains unknown. The present study illustrated that BTDE had anti-angiogenesis effect in vitro through inhibiting human umbilical vein endothelial cells migration, invasion, tube formation, and the activity of matrix metalloproteinases 9 (MMP9), and in vivo BTDE also blocked intersegmental vessel formation in zebrafish embryos. Moreover, BTDE inhibited the migration, invasion, and vasculogenic mimicry formation of lung cancer cell A549. All these results indicated that BTDE could be used as a potential candidate in anti-angiogenesis for the treatment of cancer.

Constructing heparin-modified pancreatic decellularized scaffold to improve its re-endothelialization

2018 ◽  
Vol 32 (8) ◽  
pp. 1063-1070 ◽  
Author(s):  
Liancheng Xu ◽  
Yibing Guo ◽  
Yan Huang ◽  
Yicheng Xiong ◽  
Yang Xu ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Therapeutic Option ◽  
Blue Staining ◽  
Potential Candidate ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Decellularized Scaffold

Pancreas transplantation is considered as a promising therapeutic option with the potential to cure diabetes. However, efficacy of current clinical transplantation is limited by the donor organ. With regard to creating a functional pancreas-tissue equivalent for transplantation, vascularization remains a large obstacle. To enhance the angiogenic properties of pancreatic decellularized scaffold, surface modification of the vasculature was used to promote endothelialization efficiency. In this study, an endothelialized pancreatic decellularized scaffold was obtained through heparin modification under mild conditions. The immobilization of heparin was performed through 1-ethyl-3–(3-dimethylaminopropyl)-carbodiimide and N-Hydroxysuccinimide. The morphology, ultra-structure and porosity of the heparinized scaffold were characterized by toluidine blue staining, scanning electron microscope and infrared spectrum. The adhesion, proliferation and angiogenesis of human umbilical vein endothelial cells on heparin-pancreatic decellularized scaffold were also researched in vitro. In vivo transplantation was also performed to observe the location of human umbilical vein endothelial cells and the formation of new blood vessel, which exhibited significant differences with pancreatic decellularized scaffold group (p<0.05). These findings indicated that the endothelialized heparin-pancreatic decellularized scaffold may be used to solve the problem of blood supply and to support the function of insulin-secreting cells better after in vivo transplantation, and therefore, would be a potential candidate for pancreatic tissue engineering.

scholarly journals Propolis Reduces Phosphatidylcholine-Specific Phospholipase C Activity and Increases Annexin a7 Level in Oxidized-LDL-Stimulated Human Umbilical Vein Endothelial Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-9
Author(s):  
Hongzhuan Xuan ◽  
Zhen Li ◽  
Jiying Wang ◽  
Kai Wang ◽  
Chongluo Fu ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Phospholipase C ◽  
Biological Activities ◽  
Umbilical Vein ◽  
Oxidized Ldl ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Brazilian Green Propolis ◽  
Chinese Propolis ◽  
Annexin A7

To understand the mechanisms underlying the regulating dyslipidemia action of Chinese propolis and Brazilian green propolis, we investigated their effects on phosphatidylcholine-specific phospholipase C (PC-PLC) activity and annexin a7 (ANXA7) level which play crucial roles in the control of the progress of atherosclerosis. Furthermore, active oxygen species (ROS) levels, nuclear factor-KappaB p65 (NF-κB p65), and mitochondrial membrane potential (MMP) were also investigated in oxidized-LDL- (ox-LDL-) stimulated human umbilical vein endothelial cells (HUVECs). Our data indicated that the treatment of both types of propolis 12.5 μg/mL significantly increased cell viability and attenuated apoptosis rate, increased ANXA7 level, and decreased PC-PLC activity. Both types of propolis also inhibited ROS generation as well as the subsequent MMP collapse, and NF-κB p65 activation induced by ox-LDL in HUVECs. Our results also indicated that Chinese propolis and Brazilian green propolis had similar biological activities and prevented ox-LDL induced cellular dysfunction in HUVECs.

scholarly journals CD39/NTPDase-1 expression and activity in human umbilical vein endothelial cells are differentially regulated by leaf extracts from Rubus caesius and Rubus idaeus

2014 ◽  
Vol 19 (3) ◽  
Author(s):  
Dominika Dudzinska ◽  
Boguslawa Luzak ◽  
Magdalena Boncler ◽  
Joanna Rywaniak ◽  
Dorota Sosnowska ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Biological Activities ◽  
Umbilical Vein ◽  
Surface Membrane ◽  
Rubus Idaeus ◽  
Leaf Extracts ◽  
Membrane Expression ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells ◽  
Expression And Activity

AbstractMany experimental studies have demonstrated the favorable biological activities of plants belonging to the genus Rubus, but little is known of the role of Rubus leaf extracts in the modulation of the surface membrane expression and activity of endothelial apyrase. The aim of this study was to assess the influence of 1–15 μg/ml Rubus extracts on CD39 expression and enzymatic activity, and on the activation (ICAM-1 expression) and viability of human umbilical vein endothelial cells (HUVEC). The polyphenolic contents and antioxidative capacities of extracts from dewberry (R. caesius L.) and raspberry (R. idaeus L.) leaves were also investigated. The techniques applied were flow cytometry (endothelial surface membrane expression of ICAM-1 and CD39), malachite green assay (CD39 activity), HPLC-DAD (quantitative analysis of polyphenolic extract), ABTS, DPPH and FRAP spectrometric assays (antioxidant capacity), and the MTT test (cell viability). Significantly increased CD39 expressions and significantly decreased ATPDase activities were found in the cells treated with 15 μg/ml of either extract compared to the results for the controls. Neither of the extracts affected cell proliferation, but both significantly augmented endothelial cell ICAM-1 expression. The overall antioxidant capacities of the examined extracts remained relatively high and corresponded well to the determined total polyphenol contents. Overall, the results indicate that under in vitro conditions dewberry and raspberry leaf extracts have unfavorable impact on endothelial cells.

scholarly journals Jolkinolide A and Jolkinolide B Inhibit Proliferation of A549 Cells and Activity of Human Umbilical Vein Endothelial Cells

2017 ◽  
Vol 23 ◽  
pp. 223-237 ◽  
Author(s):  
Lei Shen ◽  
Shan-Qiang Zhang ◽  
Lei Liu ◽  
Yu Sun ◽  
Yu-Xuan Wu ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
A549 Cells ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

scholarly journals Berberine Protects Human Umbilical Vein Endothelial Cells against LPS-Induced Apoptosis by Blocking JNK-Mediated Signaling

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Junping Guo ◽  
Lijun Wang ◽  
Linyao Wang ◽  
Senmi Qian ◽  
Dayong Zhang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Molecular Mechanisms ◽  
Umbilical Vein ◽  
Specific Inhibitor ◽  
Cell Counting ◽  
Potential Candidate ◽  
Sod Activity ◽  
Human Umbilical Vein ◽  
Induced Apoptosis ◽  
Umbilical Vein Endothelial Cells

Endothelial dysfunction is a critical factor during the initiation of atherosclerosis. Berberine has a beneficial effect on endothelial function; however, the underlying mechanisms remain unclear. In this study, we investigated the effects of berberine on lipopolysaccharide- (LPS-) induced apoptosis in human umbilical vein endothelial cells (HUVECs) and the molecular mechanisms mediating the effect. The effects of berberine on LPS-induced cell apoptosis and viability were measured with 5-ethynyl-2′-deoxyuridine staining, flow cytometry, and Cell Counting Kit-8 assays. The expression and/or activation of proapoptotic and antiapoptotic proteins or signaling pathways, including caspase-3, poly(ADP-ribose) polymerase, myeloid cell leukemia-1 (MCL-1), p38 mitogen-activated protein kinase, C-Jun N-terminal kinase (JNK), and extracellular signal-regulated kinase, were determined with western blotting. The malondialdehyde levels, superoxide dismutase (SOD) activity, and production of proinflammatory cytokines were measured with enzyme-linked immunosorbent assays. The results demonstrated that berberine pretreatment protected HUVECs from LPS-induced apoptosis, attenuated LPS-induced injury, inhibited LPS-induced JNK phosphorylation, increased MCL-1 expression and SOD activity, and decreased proinflammatory cytokine production. The effects of berberine on LPS-treated HUVECs were prevented by SP600125, a JNK-specific inhibitor. Thus, berberine might be a potential candidate in the treatment of endothelial cell injury-related vascular diseases.

scholarly journals Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1481-1484 ◽  
Author(s):  
I Maruyama ◽  
PW Majerus
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Cancer Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Protein S ◽  
Lung Cancer Cells ◽  
Human Lung Cancer ◽  
Umbilical Vein Endothelial Cells

Abstract We investigated the effect of protein C on the endocytosis of thrombin- thrombomodulin complexes. We previously showed that exposure of umbilical vein endothelial cells to thrombin stimulated the internalization and degradation of thrombin. A similar internalization was stimulated by a monoclonal antithrombomodulin antibody. We have repeated these studies in the presence of protein C and found that endocytosis of 125I-thrombin-thrombomodulin complexes, but not 125I- antithrombomodulin-thrombomodulin complexes, is inhibited. Activated protein C did not inhibit endocytosis of thrombin-thrombomodulin complexes. Protein C inhibited both internalization and degradation of 125I-thrombin and diisopropylphosphoryl (DIP) 125I-thrombin in human lung cancer cells (A549). These effects were observed at protein C concentrations found in human plasma. Protein S had no effect on the inhibition of endocytosis of thrombin-thrombomodulin complexes by protein C. We propose that protein C may regulate the rate of endocytosis of thrombin-thrombomodulin complexes in vivo and thereby control the capacity for endothelium to activate protein C.

scholarly journals Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells

Blood ◽  
1987 ◽  
Vol 69 (5) ◽  
pp. 1481-1484 ◽  
Author(s):  
I Maruyama ◽  
PW Majerus
Keyword(s):  
Lung Cancer ◽  
Endothelial Cells ◽  
Cancer Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Protein S ◽  
Lung Cancer Cells ◽  
Human Lung Cancer ◽  
Umbilical Vein Endothelial Cells

We investigated the effect of protein C on the endocytosis of thrombin- thrombomodulin complexes. We previously showed that exposure of umbilical vein endothelial cells to thrombin stimulated the internalization and degradation of thrombin. A similar internalization was stimulated by a monoclonal antithrombomodulin antibody. We have repeated these studies in the presence of protein C and found that endocytosis of 125I-thrombin-thrombomodulin complexes, but not 125I- antithrombomodulin-thrombomodulin complexes, is inhibited. Activated protein C did not inhibit endocytosis of thrombin-thrombomodulin complexes. Protein C inhibited both internalization and degradation of 125I-thrombin and diisopropylphosphoryl (DIP) 125I-thrombin in human lung cancer cells (A549). These effects were observed at protein C concentrations found in human plasma. Protein S had no effect on the inhibition of endocytosis of thrombin-thrombomodulin complexes by protein C. We propose that protein C may regulate the rate of endocytosis of thrombin-thrombomodulin complexes in vivo and thereby control the capacity for endothelium to activate protein C.

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