Von Willebrand Factor, Dysfunction of the Vascular Endothelium, and the Development of Renal and Vascular Complications in Diabetes

1998 ◽  
pp. 199-208
Author(s):  
Coen D. A. Stehouwer
Keyword(s):  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Vascular Complications ◽  
Von Willebrand ◽  
Willebrand Factor

The Endothelial Glycocalyx Contributes to the Anchorage of von Willebrand Factor Fibers to the Vascular Endothelium

2019 ◽  
Author(s):  
T. Kalagara ◽  
T. Moutsis ◽  
Y. Yang ◽  
K.I. Pappelbaum ◽  
A. Farken ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Endothelial Glycocalyx ◽  
Von Willebrand ◽  
Willebrand Factor

Desmopressin testing in children with von Willebrand syndrome in haemostaseologic centers of Saxonia, Saxonia-Anhalt and Thuringia

2009 ◽  
Vol 29 (S 01) ◽  
pp. S98-S102 ◽  
Author(s):  
B. Huhn ◽  
A. Hofmann ◽  
K. Hofmann ◽  
H. Sirb ◽  
V. Aumann ◽  
...  
Keyword(s):  
Partial Response ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Test Performance ◽  
Coagulation Factor ◽  
Syndrome Type ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryThe influence of desmopressin on hemostasis is mediated by the release of von Willebrand factor and of coagulation factor VIII from vascular endothelium. The necessity of testing desmopressin effectiveness on hemostasis is a matter of controversy and the performance of the test is not yet standardized. For this reason the desmopressin tests in 114 children with von Willebrand syndrome (type 1, n=98; type 2A, n=12; type 2M, n=2; type 2N, n=2) carried out in 7 paediatric haemostaseologic centers were retrospectively analyzed. The effectiveness of desmopressin was assessed using defined response criteria. As expected, the test performance showed a wide variation among the centers. In 99 children desmopressin was given intravenously as a short infusion at a dosage ranging from 0.25 to 0.41 μg/kg and in 15 intranasally at an absolute dose of 40 to 300 μg. The points of time for blood taking after desmopressin application ranged from 0.5 to 12 h. The absent desmopressin response in 7 patients (6%) and the partial response in 15 indicate the necessity of testing desmopressin effectiveness before the first therapeutic use. The application of desmopressin was well tolerated by the patients.

scholarly journals Fluid Shear Stress Modulates von Willebrand Factor Release From Human Vascular Endothelium

Blood ◽  
1997 ◽  
Vol 90 (4) ◽  
pp. 1558-1564 ◽  
Author(s):  
Miriam Galbusera ◽  
Carla Zoja ◽  
Roberta Donadelli ◽  
Simona Paris ◽  
Marina Morigi ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Shear Stress ◽  
Laminar Flow ◽  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Fluid Shear Stress ◽  
Fluid Shear ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Cell Supernatant

Fluid shear stress generated by blood flow on arterial wall may play a role in the process of atherosclerosis, not only affecting the mass transport phenomena that take place in blood, but also by modulation of synthesis and secretion of humoral factors released by vascular endothelium that mediate platelet-vessel wall interactions. The present study was designed to investigate whether shear stress, induced by laminar flow, modulates von Willebrand factor (vWF ) release from cultured human umbilical vein endothelial cells (HUVEC) and whether this physical stimulation can affect vWF synthesis. Monolayers of HUVEC were exposed to laminar flow of varying magnitude (from 2 to 12 dynes/cm2) using a cone-and-plate device. The release of vWF in cell supernatant and in extracellular matrix by cells exposed to flow or maintained in static conditions was evaluated by enzyme-linked immunosorbent assay. HUVEC exposed to laminar flow released higher amounts of vWF into the cell supernatant within few hours of exposure and vWF secretion was dependent on shear stress magnitude. vWF released in extracellular matrix was also higher in cell monolayers exposed to shear than in static controls. vWF mRNA expression in HUVEC was not affected by exposure of cells to laminar flow, indicating that shear-induced vWF release reflected enhanced secretion without de novo protein synthesis. Immunofluorescence studies showed that the release of vWF is due to exocytosis from Weibel-Palade bodies, the storage organelles of vWF. These data indicate a novel mechanism by which local hemodynamic shear forces modulate endothelial cell function and may play a role in development of arterial thrombotic events.

scholarly journals Vimentin Is a Novel Molecule Required for the Formation of Von Willebrand Factor Strings from the Vascular Endothelium

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 2237-2237 ◽  
Author(s):  
Titilope Ishola ◽  
Qi Da ◽  
Sean P Marrelli ◽  
Miguel A. Cruz
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Knockout Mice ◽  
Platelet Adhesion ◽  
Endothelial Surface ◽  
String Formation ◽  
Von Willebrand ◽  
A2 Domain ◽  
Willebrand Factor

Abstract Background: Von Willebrand factor (VWF) is a multimeric plasma and subendothelial glycoprotein which is produced and secreted by endothelial cells. With intense stimulation (e.g. after vascular injury), endothelial cells secrete unusually large multimers of VWF in a hyper-adhesive string arrangement. Upon secretion, these long multimers or strings remain anchored to the cell surface and are capable of quickly attracting circulating platelets through interaction with the receptor GPIbα. In the absence of the VWF-protease, the VWF strings attached to the endothelium mediate spontaneous platelet adhesion that leads to the formation of microthrombi on the endothelial surface, resulting in vessel occlusion. To date, it is not clear which molecules allow VWF strings to remain docked on the surface of the endothelium once secreted. Vimentin is a cytoskeletal molecule and its extracellular form has been shown to be expressed on the surface of various cell types, including endothelial cells. Recent work from our lab has highlighted the role of extracellular vimentin in mediating platelet adhesion to VWF and that anti-vimentin antibodies inhibit this interaction. We have also found that vimentin binds the A2 domain of VWF, which is exposed on the newly secreted VWF strings. Therefore, we hypothesize that vimentin mediates the anchorage of VWF strings to the vascular endothelium. Understanding these interactions is important as VWF strings have been implicated in the pathophysiology of several disease states, such as sickle cell disease and malaria. Methods: Commercial human umbilical vein endothelial cells (HUVECs) were used. Cells were stimulated with histamine and analyzed under flow conditions to assess the quantity of VWF strings in the presence of soluble recombinant A2 domain, soluble recombinant vimentin, or anti-vimentin antibodies versus control buffer. VWF strings were visualized by tagging with commercial fluorescent-conjugated antibody. We also evaluated VWF string adherence to the endothelium of intact pressurized cerebral arteries from vimentin knockout mice versus wild-type (WT) mice ex vivo. Cerebral middle cerebral artery and parenchymal arterioles from mice were isolated, pressurized, and luminally perfused in a perfusion chamber. Histamine was applied to activate the endothelium and elicit VWF string formation. The negative control was an irrelevant isotype antibody. After histamine treatment, the arteries/arterioles were processed for VWF immunofluorescence to assess VWF string formation. VWF strings were quantified as length normalized to endothelial surface area. Results: As expected, HUVECs expressed surface vimentin as determined using flow cytometry and confocal microscopy. The presence of either soluble A2 or soluble vimentin significantly reduced the amount of VWF string formation from histamine-stimulated HUVECs in comparison to control. In some experiments, anti-vimentin antibodies decreased VWF string formation but findings were not significant. Vascular endothelial cells from vimentin knockout mice failed to form VWF strings after histamine stimulation in comparison to vimentin WT mice. Conclusions: These novel findings show that extracellular vimentin appears to play a role in VWF string formation likely via A2 domain binding. Further studies are necessary to shed light on the intricate pathways regulating VWF-mediated platelet adhesion. Our long term goals are to understand the novel interactions between vimentin and VWF strings in governing hemostasis and thrombosis. Disclosures No relevant conflicts of interest to declare.

scholarly journals FEATURES ОF METABOLIC ACTIVITY ОF VASCULAR ENDOTHELIUM IN PATIENTS WITH PULMONARY TUBERCULOSIS

2012 ◽  
Vol 67 (11) ◽  
pp. 29-33
Author(s):  
G. O. Kaminskaya ◽  
R. Yu. Abdaullaev ◽  
O. G. Komissarova
Keyword(s):  
Nitric Oxide ◽  
Pulmonary Tuberculosis ◽  
Von Willebrand Factor ◽  
Vascular Endothelium ◽  
Endothelin 1 ◽  
Von Willebrand Factor Antigen ◽  
Nitric Oxide Level ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Antigen

81 patients with active pulmonary tuberculosis were investigated. The morpho-functional status of vascular endothelium was evaluated by plasma levels of stable metabolites of nitric oxide, endothelin-1 and von Willebrand factor antigen. Typical increase of endothelin-1 in positive correlation with systemic inflammatory response syndrome (SIRS) expression was established. Nitric oxide level decreased in patients with chronic and severe course of disease. Decrease of nitric oxide level was not associated with SIRS but was consequence of specific intoxication. von Willebrand factor antigen decreased in patients with recent and limited spread of tissue damage but increased progressively with intensity of SIRS. This complex of changes (contrast shifts of nitric oxide and endothelin-1 and von Willebrand factor antigen increase) manifested in endothelium metabolic dysfunction syndrome and developed pre-conditions for microcirculation disturbances.

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