scholarly journals Dense and Dynamic Polyethylene Glycol Shells Cloak Nanoparticles from Uptake by Liver Endothelial Cells for Long Blood Circulation

ACS Nano ◽  
2018 ◽  
Vol 12 (10) ◽  
pp. 10130-10141 ◽  
Author(s):  
Hao Zhou ◽  
Zhiyuan Fan ◽  
Peter Y. Li ◽  
Junjie Deng ◽  
Dimitrios C. Arhontoulis ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Polyethylene Glycol ◽  
Blood Circulation ◽  
Liver Endothelial Cells

scholarly journals Chronic ethanol consumption impairs receptor-mediated endocytosis of MAA-modified albumin by liver endothelial cells

2003 ◽  
Vol 66 (6) ◽  
pp. 1045-1054 ◽  
Author(s):  
Michael J Duryee ◽  
Lynell W Klassen ◽  
Thomas L Freeman ◽  
Monte S Willis ◽  
Dean J Tuma ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Ethanol Consumption ◽  
Chronic Ethanol ◽  
Receptor Mediated Endocytosis ◽  
Chronic Ethanol Consumption ◽  
Liver Endothelial Cells

794 TLR1/2 LIGAND STIMULATED MOUSE LIVER ENDOTHELIAL CELLS PRODUCE IL-12 AND TRIGGER CD8+ T-CELL IMMUNITY

2012 ◽  
Vol 56 ◽  
pp. S311
Author(s):  
J. Liu ◽  
M. Jiang ◽  
Z. Ma ◽  
J. Schlaak ◽  
M. Roggendorf ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
T Cell ◽  
Mouse Liver ◽  
Cd8 T Cell ◽  
T Cell Immunity ◽  
Cell Immunity ◽  
Liver Endothelial Cells

Endothelin-1 production by hepatic endothelial cells: characterization and augmentation by endotoxin exposure

1997 ◽  
Vol 272 (3) ◽  
pp. G605-G611 ◽  
Author(s):  
A. T. Eakes ◽  
K. M. Howard ◽  
J. E. Miller ◽  
M. S. Olson
Keyword(s):  
Endothelial Cells ◽  
Significant Contribution ◽  
Gradual Increase ◽  
Glucose Production ◽  
Cell Types ◽  
Exposure Model ◽  
Mrna Levels ◽  
Endotoxin Challenge ◽  
Endotoxin Exposure ◽  
Liver Endothelial Cells

Activation of endothelin (ET) receptors in the liver causes vasoconstriction, glucose production, and lipid and peptide mediator synthesis. In the intact rat, a bolus infusion of endotoxin into a mesenteric vein served as an acute exposure model of endotoxemia. In response to this challenge, a ninefold increase in hepatic ET-1 mRNA occurred within 3 h. The plasma level of immunoreactive ET-1 (irET-1) increased correspondingly by 8.5-fold within 6 h. ET-1 mRNA levels in liver endothelial cells (EC) isolated from livers of endotoxin-treated rats at various times after endotoxin challenge showed a more gradual increase. Northern blot analyses of the major liver cell types demonstrated that ET-1 mRNA was most abundant in the EC. The present results document a significant increase in the circulating level of irET-1 during episodes of endotoxemia. The increased hepatic ET-1 production in response to endotoxin infusion suggests that ET-1 produced in the liver could make a significant contribution to the plasma irET-1 and may be an important component in the hepatic responses to systemic trauma.

scholarly journals Characterization of the interaction both in vitro and in vivo of tissue-type plasminogen activator (t-PA) with rat liver cells. Effects of monoclonal antibodies to t-PA

1992 ◽  
Vol 284 (2) ◽  
pp. 545-550 ◽  
Author(s):  
M Otter ◽  
J Kuiper ◽  
R Bos ◽  
D C Rijken ◽  
T J van Berkel
Keyword(s):  
Endothelial Cells ◽  
Mannose Receptor ◽  
Liver Cells ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Liver Endothelial Cells ◽  
Parenchymal Cells

The interaction of 125I-labelled tissue-type plasminogen activator (125I-t-PA) with freshly isolated rat parenchymal and endothelial liver cells was studied. Binding experiments at 4 degrees C with parenchymal cells and endothelial liver cells indicated the presence of 68,000 and 44,000 high-affinity t-PA-binding sites, with an apparent Kd of 3.5 and 4 nM respectively. Association of 125I-t-PA with parenchymal cells was Ca(2+)-dependent and was not influenced by asialofetuin, a known ligand for the galactose receptor. Association of 125I-t-PA with liver endothelial cells was Ca(2+)-dependent and mannose-specific, since ovalbumin (a mannose-terminated glycoprotein) inhibited the cell association of t-PA. Association of 125I-t-PA with liver endothelial cells was inhibited by anti-(human mannose receptor) antiserum. Anti-(galactose receptor) IgG had no effect on 125I-t-PA association with either cell type. Degradation of 125I-t-PA at 37 degrees C by both cell types was inhibited by chloroquine or NH4Cl, indicating that t-PA is degraded lysosomally. in vitro experiments with three monoclonal antibodies (MAbs) demonstrated that anti-t-PA MAb 1-3-1 specifically decreased association of 125I-t-PA with the endothelial cells, and anti-t-PA Mab 7-8-4 inhibited association with the parenchymal cells. Results of competition experiments in rats in vivo with these antibodies were in agreement with findings in vitro. Both antibodies decreased the liver uptake of 125I-t-PA, while a combination of the two antibodies was even more effective in reducing the liver association of 125I-t-PA and increasing its plasma half-life. We conclude from these data that clearance of t-PA by the liver is regulated by at least two pathways, one on parenchymal cells (not galactose/mannose-mediated) and another on liver endothelial cells (mediated by a mannose receptor). Results with the MAbs imply that two distinct sites on the t-PA molecule are involved in binding to parenchymal cells and liver endothelial cells.

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