scholarly journals Inhibitory effect of dilazep, an adenosine potentiator, on high-affinity transport process of adenosine in cultured vascular endothelial cells

1992 ◽  
Vol 58 ◽  
pp. 116
Author(s):  
Sohei Tanabe ◽  
Taro Tamaki ◽  
Yasushi Wada
Keyword(s):  
Endothelial Cells ◽  
Transport Process ◽  
Vascular Endothelial Cells ◽  
Inhibitory Effect ◽  
Vascular Endothelial ◽  
High Affinity

scholarly journals miR-181c-5p mediates apoptosis of vascular endothelial cells induced by hyperoxemia via ceRNA crosstalk

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jizhi Wu ◽  
Guangqi Zhang ◽  
Hui Xiong ◽  
Yuguang Zhang ◽  
Gang Ding ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Oxygen Therapy ◽  
Vascular Endothelial Cells ◽  
Inhibitory Effect ◽  
Vascular Endothelial ◽  
Pulmonary Capillaries ◽  
Pulmonary Capillary ◽  
Capillary Endothelial Cells ◽  
Nasal Inhalation ◽  
Induced Apoptosis

AbstractOxygen therapy has been widely used in clinical practice, especially in anesthesia and emergency medicine. However, the risks of hyperoxemia caused by excessive O2 supply have not been sufficiently appreciated. Because nasal inhalation is mostly used for oxygen therapy, the pulmonary capillaries are often the first to be damaged by hyperoxia, causing many serious consequences. Nevertheless, the molecular mechanism by which hyperoxia injures pulmonary capillary endothelial cells (LMECs) has not been fully elucidated. Therefore, we systematically investigated these issues using next-generation sequencing and functional research techniques by focusing on non-coding RNAs. Our results showed that hyperoxia significantly induced apoptosis and profoundly affected the transcriptome profiles of LMECs. Hyperoxia significantly up-regulated miR-181c-5p expression, while down-regulated the expressions of NCAPG and lncRNA-DLEU2 in LMECs. Moreover, LncRNA-DLEU2 could bind complementarily to miR-181c-5p and acted as a miRNA sponge to block the inhibitory effect of miR-181c-5p on its target gene NCAPG. The down-regulation of lncRNA-DLEU2 induced by hyperoxia abrogated its inhibition of miR-181c-5p function, which together with the hyperoxia-induced upregulation of miR-181c-5p, all these significantly decreased the expression of NCAPG, resulting in apoptosis of LMECs. Our results demonstrated a ceRNA network consisting of lncRNA-DLEU2, miR-181c-5p and NCAPG, which played an important role in hyperoxia-induced apoptosis of vascular endothelial injury. Our findings will contribute to the full understanding of the harmful effects of hyperoxia and to find ways for effectively mitigating its deleterious effects.

scholarly journals Inhibitory effect of caveolin-1 in vascular endothelial cells, pericytes and smooth muscle cells

Oncotarget ◽  
2017 ◽  
Vol 8 (44) ◽  
pp. 76165-76173 ◽  
Author(s):  
Hongping Xu ◽  
Liwei Zhang ◽  
Wei Chen ◽  
Jiazhou Xu ◽  
Ruting Zhang ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Endothelial Cells ◽  
Muscle Cells ◽  
Inhibitory Effect ◽  
Vascular Endothelial ◽  
Caveolin 1

scholarly journals High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells--implications for the modulation of FGF-2.

1995 ◽  
Vol 128 (6) ◽  
pp. 1221-1228 ◽  
Author(s):  
A Hanneken ◽  
P A Maher ◽  
A Baird
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Protein Interactions ◽  
Binding Proteins ◽  
Vascular Endothelial Cells ◽  
Extracellular Domain ◽  
Cytoplasmic Domain ◽  
Basement Membranes ◽  
Vascular Endothelial ◽  
High Affinity

We recently characterized three FGF-binding proteins (FGF-BPs) which are soluble forms of the extracellular domains of the high affinity FGF receptors (Hanneken, A. M., W. Ying, N. Ling, and A. Baird. Proc. Natl. Acad. Sci. USA. 1994. 91:9170-9174). These proteins circulate in blood and have been proposed to modulate the biological activity of the FGF family of proteins. Immunohistochemical studies now demonstrate that these soluble, truncated FGF receptors are also present in the basement membranes of retinal vascular endothelial cells. These immunoreactive proteins can be detected with antibodies raised to the extracellular domain of FGFR-1 but not with antibodies raised to either the juxtamembrane domain or the cytoplasmic domain of FGFR-1. Western blotting of human retinal extracts with the antibody raised to the extracellular domain of FGFR-1 detects specific, low molecular mass proteins at 85 kD and 55 kD, corresponding in size to the FGF-BPs, which are not detected with antibodies against the cytoplasmic domain of the receptor. The interaction of this receptor with the extracellular matrix is not dependent on the presence of FGF-2. Immunoreactive receptors are still detected in vascular basement membranes after the removal of FGF-2 with heparitinase. In addition, the recombinant extracellular domain of FGFR-1 continues to bind to corneal endothelial cell matrix after endogenous FGF-2 has been removed with 2 M NaCl. Acid treatment, which has been shown to disrupt protein interactions with the extracellular matrix, leads to a significant reduction in the presence of the matrix form of the FGF receptor. This loss can be restored with exogenous incubations of the recombinant extracellular domain of FGFR-1. This report is the first demonstration that a truncated form of a high affinity growth factor receptor can be localized to the extracellular matrix. These findings add to the list of binding proteins associated with the extracellular matrix (IGFBP-5) and suggest a potentially new regulatory mechanism for controlling the biological availability of FGF, and other peptide growth factors, in the extracellular matrix.

Peroxynitrite modulates receptor-activated Ca2+ signaling in vascular endothelial cells

1996 ◽  
Vol 270 (6) ◽  
pp. L954-L961 ◽  
Author(s):  
S. J. Elliott
Keyword(s):  
Endothelial Cells ◽  
Superoxide Dismutase ◽  
Endothelial Cell ◽  
Vascular Endothelial Cells ◽  
Inhibitory Effect ◽  
Vascular Endothelial ◽  
No Donor ◽  
Time Points ◽  
Inactive Metabolite ◽  
Spermine Nonoate

Peroxynitrite (ONOO-) is formed from superoxide (O2-) and .NO. We have previously reported that O2- does not alter endothelial cell Ca2+ signaling. To test whether .NO alters Ca2+ signaling, cells were incubated with the .NO donor, spermine NONOate. Neither spermine NONOate nor S-nitroso-N-acetyl penicillamine (SNAP) altered bradykinin-stimulated Ca2+ signaling. By contrast, 3-morpholinosydnonimine (SIN-1), which generates ONOO- by releasing O2- and .NO essentially in a simultaneous manner, significantly inhibited signaling. Initially, the inhibitory effect of 1 mM SIN-1 was selective toward agonist-stimulated influx of external Ca2+. At later time points, SIN-1 additionally depleted internal stores of releasable Ca2+. When cells were coincubated with SIN-1 plus superoxide dismutase, a technique designed to scavenge O2- and convert SIN-1 to purely an .NO-donor compound, Ca2+ signaling was identical to control. SIN-1C, the inactive metabolite of SIN-1, had no effect on [Ca2+]i. This study demonstrates that exogenously generated ONOO- modulates endothelial cell Ca2+ signaling, suggesting that ONOO- is of biological relevance to vasoregulation.

Prostacyclin: Production by Vascular Endothelium and Effects on Platelet Aggregation

1979 ◽  
Author(s):  
S. Moncada ◽  
S. Bunting
Keyword(s):  
Endothelial Cells ◽  
Arachidonic Acid ◽  
Platelet Aggregation ◽  
Vascular Endothelium ◽  
Vascular Endothelial Cells ◽  
Specific Inhibitor ◽  
Inhibitory Effect ◽  
Vascular Endothelial ◽  
Prostacyclin Production

The inhibitory effect of vascular endothelial cells on platelet aggregation is due to their ability to release prostacyclin. The existence of an ADPase has been confirmed in endothelial cells but this enzymes does not seem to be related to the anti-aggregating properties of vascular endothelium. In vitro, the release of prostacyclin by humand and rabbit endothelial cells persists after several subcultures. The production of PGI2 can be demonstrated by its inhibition by aspirin-like drugs or 15-hydroperoxy arachidonic acid (a specific inhibitor of PGI2 synthesis). Moreover, the antiaggregating activity is antagonised by an antibody to 5,6 dihydro prostacyclin which cross reacts and neutralises prostacyclin.

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