scholarly journals Interaction of the actin cytoskeleton with microtubules regulates secretory organelle movement near the plasma membrane in human endothelial cells

2003 ◽  
Vol 116 (19) ◽  
pp. 3927-3938 ◽  
Author(s):  
J.-B. Manneville
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Actin Cytoskeleton ◽  
Human Endothelial Cells ◽  
Organelle Movement

scholarly journals Evidence that agonists stimulate bivalent-cation influx into human endothelial cells

1988 ◽  
Vol 255 (1) ◽  
pp. 179-184 ◽  
Author(s):  
T J Hallam ◽  
R Jacob ◽  
J E Merritt
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Umbilical Vein ◽  
Free Calcium ◽  
Human Endothelial Cells ◽  
Bivalent Cation ◽  
Human Umbilical Vein ◽  
Fura 2 ◽  
Bivalent Cations ◽  
Umbilical Vein Endothelial Cells

Human umbilical-vein endothelial cells stimulated with thrombin or histamine show an increase in [Ca2+]i (cytoplasmic free calcium concn.) that is maintained well above the basal pre-stimulated value as long as agonist and a source of extracellular Ca2+ are present. These results provide circumstantial evidence that agonists stimulate influx of Ca2+ across the plasma membrane and into the cytoplasm. Here, we have used Mn2+ as the extracellular bivalent cation which can bind to the fluorescent Ca2+ indicator fura-2 to quench its fluorescence completely. Human umbilical-vein endothelial cells were loaded with fura-2 and, in the presence of extracellular Mn2+, thrombin and histamine were shown to cause quenching of the intracellular dye. This result demonstrates conclusively that agonists can stimulate the influx of bivalent cations. Stimulated discharge of Ca2+ from intracellular stores and influx of Mn2+ were temporally resolved in the same cells to show that release of Ca2+ from intracellular stores clearly precedes influx. Influx of Mn2+ was also demonstrated when extracellular Mn2+ was added after agonist at a time when [Ca2+]i had fallen back to the basal value, showing that influx is not dependent on elevated [Ca2+]i.

scholarly journals The Tetraspanin CD63/lamp3 Cycles between Endocytic and Secretory Compartments in Human Endothelial Cells

2000 ◽  
Vol 11 (5) ◽  
pp. 1829-1843 ◽  
Author(s):  
Toshihide Kobayashi ◽  
Ulrich M. Vischer ◽  
Corinne Rosnoblet ◽  
Cécile Lebrand ◽  
Margaret Lindsay ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Late Endosome ◽  
Human Endothelial Cells ◽  
Late Endosomes ◽  
Lysobisphosphatidic Acid ◽  
Type C ◽  
Niemann Pick ◽  
Tetraspanin Cd63

In the present study, we show that in human endothelial cells the tetraspanin CD63/lamp3 distributes predominantly to the internal membranes of multivesicular–multilamellar late endosomes, which contain the unique lipid lysobisphosphatidic acid. Some CD63/lamp3 is also present in Weibel–Palade bodies, the characteristic secretory organelle of these cells. We find that CD63/lamp3 molecules can be transported from late endosomes to Weibel–Palade bodies and thus that CD63/lamp3 cycles between endocytic and biosynthetic compartments; however, movement of CD63/lamp3 is much slower than that of P-selectin, which is known to cycle between plasma membrane and Weibel–Palade bodies. When cells are treated with U18666A, a drug that mimics the Niemann-Pick type C syndrome, both proteins accumulate in late endosomes and fail to reach Weibel–Palade bodies efficiently, suggesting that P-selectin, like CD63/lamp3, cycles via late endosomes. Our data suggest that CD63/lamp3 partitions preferentially within late endosome internal membranes, thus causing its accumulation, and that this mechanism contributes to CD63/lamp3 retention in late endosomes; however, our data also indicate that the protein can eventually escape from these internal membranes and recycle toward Weibel–Palade bodies to be reused. Our observations thus uncover the existence of a selective trafficking route from late endosomes to Weibel–Palade bodies.

scholarly journals Cultured human endothelial cells synthesize a plasma membrane protein complex immunologically related to the platelet glycoprotein IIb/IIIa complex

Blood ◽  
1986 ◽  
Vol 67 (4) ◽  
pp. 1176-1180 ◽  
Author(s):  
OC Leeksma ◽  
J Zandbergen-Spaargaren ◽  
JC Giltay ◽  
JA van Mourik
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Endothelial Cell ◽  
Membrane Protein ◽  
Protein Complex ◽  
Platelet Glycoprotein ◽  
Plasma Membrane Protein ◽  
Human Endothelial Cells ◽  
Membrane Protein Complex ◽  
Crossed Immunoelectrophoresis

Abstract We have previously demonstrated that endothelial cells synthesize a plasma membrane protein indistinguishable from platelet glycoprotein (GP) IIa. The present study provides evidence for a further analogy between the platelet and the endothelial cell membrane by showing that cultured endothelial cells also synthesize a membrane protein complex immunologically related to the platelet GP IIb/GP IIIa complex. This evidence is based on the following observations: (1) C17, a murine monoclonal antiplatelet GP IIIa antibody, consistently precipitates two proteins, apparent molecular weights, respectively, 115,000 and 125,000 reduced and 95,000 and 135,000 nonreduced, from metabolically (35S- methionine) as well as surface 125I-labeled cultured human endothelial cells; (2) upon crossed immunoelectrophoresis of solubilized endothelial cells against a polyclonal rabbit antiplatelet antiserum and 125I-labeled C17 IgG, a single precipitate of the protein(s) recognized by C17 is observed. As judged by their mobility in 9% polyacrylamide gels, both endothelial proteins appear to have a somewhat larger molecular weight than their platelet counterparts. Patterns obtained by crossed immunoelectrophoresis are also indicative of a difference in electrophoretic behavior of the platelet GP IIb/IIIa complex and the endothelial cell protein complex.

Pravastatin Counteracts Angiotensin II-Induced Upregulation and Activation of NADPH Oxidase at Plasma Membrane of Human Endothelial Cells

2010 ◽  
Vol 55 (2) ◽  
pp. 203-212 ◽  
Author(s):  
Ezequiel Alvarez ◽  
Bruno K Rodiño-Janeiro ◽  
Rafael Ucieda-Somoza ◽  
José R González-Juanatey
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Angiotensin Ii ◽  
Nadph Oxidase ◽  
Human Endothelial Cells

scholarly journals Plasma membrane microdomains regulate TACE-dependent TNFR1 shedding in human endothelial cells

2012 ◽  
Vol 16 (3) ◽  
pp. 626-635 ◽  
Author(s):  
Alessio D.’Alessio ◽  
Bianca Esposito ◽  
Claudia Giampietri ◽  
Elio Ziparo ◽  
Jordan S. Pober ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Membrane Microdomains ◽  
Human Endothelial Cells ◽  
Plasma Membrane Microdomains

scholarly journals Cultured human endothelial cells synthesize a plasma membrane protein complex immunologically related to the platelet glycoprotein IIb/IIIa complex

Blood ◽  
1986 ◽  
Vol 67 (4) ◽  
pp. 1176-1180
Author(s):  
OC Leeksma ◽  
J Zandbergen-Spaargaren ◽  
JC Giltay ◽  
JA van Mourik
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Endothelial Cell ◽  
Membrane Protein ◽  
Protein Complex ◽  
Platelet Glycoprotein ◽  
Plasma Membrane Protein ◽  
Human Endothelial Cells ◽  
Membrane Protein Complex ◽  
Crossed Immunoelectrophoresis

We have previously demonstrated that endothelial cells synthesize a plasma membrane protein indistinguishable from platelet glycoprotein (GP) IIa. The present study provides evidence for a further analogy between the platelet and the endothelial cell membrane by showing that cultured endothelial cells also synthesize a membrane protein complex immunologically related to the platelet GP IIb/GP IIIa complex. This evidence is based on the following observations: (1) C17, a murine monoclonal antiplatelet GP IIIa antibody, consistently precipitates two proteins, apparent molecular weights, respectively, 115,000 and 125,000 reduced and 95,000 and 135,000 nonreduced, from metabolically (35S- methionine) as well as surface 125I-labeled cultured human endothelial cells; (2) upon crossed immunoelectrophoresis of solubilized endothelial cells against a polyclonal rabbit antiplatelet antiserum and 125I-labeled C17 IgG, a single precipitate of the protein(s) recognized by C17 is observed. As judged by their mobility in 9% polyacrylamide gels, both endothelial proteins appear to have a somewhat larger molecular weight than their platelet counterparts. Patterns obtained by crossed immunoelectrophoresis are also indicative of a difference in electrophoretic behavior of the platelet GP IIb/IIIa complex and the endothelial cell protein complex.

Tissue factor activity is increased in human endothelial cells cultured under elevated static pressure

1999 ◽  
Vol 277 (2) ◽  
pp. C233-C242 ◽  
Author(s):  
M. D. Silverman ◽  
C. R. Waters ◽  
G. T. Hayman ◽  
J. Wigboldus ◽  
M. M. Samet ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Plasma Membrane ◽  
Tissue Factor ◽  
Static Pressure ◽  
Vena Cava ◽  
Fold Increase ◽  
Molecular Organization ◽  
Mrna Levels ◽  
Human Endothelial Cells ◽  
Tnf Α

We tested the hypothesis that elevated blood pressure, a known stimulus for vascular remodeling and an independent risk factor for the development of atherosclerotic disease, can modulate basal and cytokine-induced tissue factor (TF; CD 142) expression in cultured human endothelial cells (EC). Using a chromogenic enzymatic assay, we measured basal and tumor necrosis factor-α (TNF-α; 10 ng/ml, 5 h)-induced TF activities in human aortic EC (HAEC) and vena cava EC (HVCEC) cultured at atmospheric pressure and at 170 mmHg imposed pressure for up to 48 h. Basal TF activities were 22 ± 10 U/mg protein for HAEC and 14 ± 9 U/mg protein for HVCEC and were upregulated in both cell types >10-fold by TNF-α. Exposure to pressure for 5 h induced additional elevation of basal TF activity by 47 ± 16% ( P < 0.05, n = 6) for HAEC and 17 ± 5% ( P < 0.05, n = 3) for HVCEC. Pressurization also enhanced TF activity in TNF-α-treated cells from 240 ± 28 to 319 ± 32 U/mg protein in HAEC ( P < 0.05, n = 4) and from 148 ± 25 to 179 ± 0.8 U/mg protein ( P < 0.05, n = 3) in HVCEC. Cytokine stimulation caused an ∼100-fold increase in steady-state TF mRNA levels in HAEC, whereas pressurization did not alter either TF mRNA or cell surface antigen expression, as determined by quantitative RT-PCR methodology and ELISA. Elevated pressure, however, modulated the EC plasma membrane organization and/or permeability as inferred from the increased cellular uptake of the fluorescent amphipathic dye merocyanine 540 (33 ± 7%, P < 0.05). Our data suggest that elevated static pressure modulates the hemostatic potential of vascular cells by modifying the molecular organization of the plasma membrane.

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