Cyclosporine And Cremaphor Modulate Von Willebrand Factor Release From Cultured Human Endothelial Cells

1993 ◽  
Vol 56 (5) ◽  
pp. 1218-1222 ◽  
Author(s):  
Peter Collins ◽  
Martin Wilkie ◽  
Khalid Razak ◽  
Stewart Abbot ◽  
Suzanne Harley ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Human Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Release

Von Willebrand Factor Release and P-Selectin Expression Is Stimulated by Thrombin and Trypsin but not IL-1 in Cultured Human Endothelial Cells

1993 ◽  
Vol 70 (02) ◽  
pp. 346-350 ◽  
Author(s):  
Peter W Collins ◽  
Marion G Macey ◽  
Mary R Cahill ◽  
Adrian C Newland
Keyword(s):  
Flow Cytometry ◽  
Endothelial Cells ◽  
Cell Membrane ◽  
Von Willebrand Factor ◽  
Surface Expression ◽  
Monocyte Adhesion ◽  
Human Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Release

SummaryThe stimulated release of von Willebrand factor (vWF) from endothelial cells by secretagogues such as thrombin is associated with the translocation of Weibel-Palade bodies to the cell membrane and the surface expression of P-selectin (also known as GMP 140, PADGEM and CD 62). P-selectin, which is stored in Weibel-Palade bodies, is a neutrophil and monocyte adhesion molecule important in the initiation of inflammation.We have developed a simple assay for the detection of P-selectin on endothelial cells using indirect immunofluorescence and flow cytometry and have confirmed that this is temporally related to vWF release. The assay has been used to demonstrate that IL-1 does not cause Weibel-Palade body degranulation but that trypsin does. This has implications for the use of passaged endothelial cells in the study of vWF release and the assay has numerous possible applications in study of mechanisms of stimulated vWF release.

TRYPSIN INDUCED VON WILLEBRAND FACTOR RELEASE FROM HUMAN ENDOTHELIAL CELLS IS MEDIATED BY PAR-2 ACTIVATION

1996 ◽  
Vol 84 (6) ◽  
pp. 463-473 ◽  
Author(s):  
Josef Storck ◽  
Benno Küsters ◽  
Michael Vahland ◽  
Corinna Morys-Wortmann ◽  
Eberhard R Zimmermann
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Human Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Release

scholarly journals Tspan18 is a novel regulator of the Ca2+ channel Orai1 and von Willebrand factor release in endothelial cells

Haematologica ◽  
2018 ◽  
Vol 104 (9) ◽  
pp. 1892-1905 ◽  
Author(s):  
Peter J. Noy ◽  
Rebecca L. Gavin ◽  
Dario Colombo ◽  
Elizabeth J. Haining ◽  
Jasmeet S. Reyat ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Release

scholarly journals Gamma-interferon modulates von Willebrand factor release by cultured human endothelial cells

Blood ◽  
1990 ◽  
Vol 75 (11) ◽  
pp. 2177-2184 ◽  
Author(s):  
SH Tannenbaum ◽  
HR Gralnick
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
High Molecular Weight ◽  
Von Willebrand Factor ◽  
Inflammatory Mediators ◽  
Interleukin 1 ◽  
Gamma Interferon ◽  
Human Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Endothelial cells (EC) synthesize and secrete von Willebrand factor (vWF), a multimeric glycoprotein required for normal hemostasis. Within human endothelial cells, vWF multimers of extremely high molecular weight are stored in rod-shaped organelles known as Weibel-Palade bodies. Inflammatory mediators, such as interleukin-1, induce in vitro a variety of procoagulant responses by EC, including the secretion of stored vWF. We postulated that other inflammatory mediators might act to balance this procoagulant reaction, thereby assisting in the maintenance of blood fluidity during immune activation. Both gamma- interferon (gamma-IFN) and tumor necrosis factor (TNF) were found to act independently and cooperatively to depress the stimulated release of vWF from EC. Analysis of stored vWF in either gamma-IFN and/or TNF- treated EC demonstrated a loss of high molecular weight multimers while immunofluorescent studies documented a loss of visible Weibel-Palade bodies. This suggests that gamma-IFN and TNF interfere with normal vWF storage. gamma-IFN acted in a dose-, time-, and RNA-dependent fashion, and its inhibition of vWF release was reversible with time. No effect of gamma-IFN on EC was noted when anti-serum to gamma-IFN was added. Unlike gamma-IFN, alpha-interferon did not effect EC vWF. Therefore, gamma-IFN and TNF may be important in decreasing vWF release during inflammatory or immunologic episodes.

scholarly journals Studies of Multimerin in Human Endothelial Cells

Blood ◽  
1998 ◽  
Vol 91 (4) ◽  
pp. 1304-1317 ◽  
Author(s):  
Catherine P. M. Hayward ◽  
Elisabeth M. Cramer ◽  
Zhili Song ◽  
Shilun Zheng ◽  
Roxanna Fung ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Culture Media ◽  
Cellular Membrane ◽  
Human Endothelial Cells ◽  
Early Passage ◽  
Endothelial Cell Cultures ◽  
Dense Core Granules ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Multimerin is a novel, massive, soluble protein that resembles von Willebrand factor in its repeating, homomultimeric structure. Both proteins are expressed by megakaryocytes and endothelial cells and are stored in the region of platelet α-granules resembling Weibel-Palade bodies. These findings led us to study the distribution of multimerin within human endothelial cells. Multimerin was identified in vascular endothelium in situ. In cultured endothelial cells, multimerin was identified within round to rod-shaped, dense-core granules, some of which contained intragranular, longitudinally arranged tubules and resembled Weibel-Palade bodies. However, multimerin was found primarily in different structures than the Weibel-Palade body proteins von Willebrand factor and P-selectin. After stimulation with secretagogues, multimerin was observed to redistribute from intracellular structures to the external cellular membrane, without detectable accompanied secretion of multimerin into the culture media. In early passage endothelial cell cultures, multimerin was associated with extensive, fibrillary, extracellular matrix structures, in a different distribution than fibronectin. Although multimerin and von Willebrand factor are stored together in platelets, they are mainly found within different structures in endothelial cells, indicating that there are tissue-specific differences in the sorting of these soluble, multimeric proteins.

Cytotoxicity of silica nanoparticles through exocytosis of von Willebrand factor and necrotic cell death in primary human endothelial cells

Biomaterials ◽  
2011 ◽  
Vol 32 (33) ◽  
pp. 8385-8393 ◽  
Author(s):  
Alexander T. Bauer ◽  
Elwira A. Strozyk ◽  
Christian Gorzelanny ◽  
Christoph Westerhausen ◽  
Anna Desch ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Death ◽  
Silica Nanoparticles ◽  
Von Willebrand Factor ◽  
Necrotic Cell Death ◽  
Human Endothelial Cells ◽  
Necrotic Cell ◽  
Von Willebrand ◽  
Willebrand Factor
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