scholarly journals Coagulation factor Va binds to human umbilical vein endothelial cells and accelerates protein C activation.

1984 ◽  
Vol 74 (1) ◽  
pp. 224-230 ◽  
Author(s):  
I Maruyama ◽  
H H Salem ◽  
P W Majerus
Keyword(s):  
Endothelial Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Coagulation Factor ◽  
Human Umbilical Vein ◽  
Factor Va ◽  
Umbilical Vein Endothelial Cells

scholarly journals Protein C Activation and Factor Va Inactivation on Human Umbilical Vein Endothelial Cells

1997 ◽  
Vol 17 (11) ◽  
pp. 2765-2775 ◽  
Author(s):  
Matthew F. Hockin ◽  
Michael Kalafatis ◽  
Marie Shatos ◽  
Kenneth G. Mann
Keyword(s):  
Endothelial Cells ◽  
Protein C ◽  
Umbilical Vein ◽  
Human Umbilical Vein ◽  
Factor Va ◽  
Umbilical Vein Endothelial Cells

scholarly journals Alternative mRNA is favored by the A3 haplotype of the EPCR gene PROCR and generates a novel soluble form of EPCR in plasma

Blood ◽  
2008 ◽  
Vol 111 (7) ◽  
pp. 3442-3451 ◽  
Author(s):  
Beatrice Saposnik ◽  
Elodie Lesteven ◽  
Anna Lokajczyk ◽  
Charles T. Esmon ◽  
Martine Aiach ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein C ◽  
Transmembrane Domain ◽  
Umbilical Vein ◽  
Expression Patterns ◽  
Soluble Form ◽  
Cell Protein ◽  
Human Umbilical Cord ◽  
Human Umbilical Vein ◽  
Umbilical Vein Endothelial Cells

Abstract The endothelial cell protein C receptor also exists in soluble form in plasma (sEPCR), resulting from ADAM17 cleavage. Elevated sEPCR levels are observed in subjects carrying the A3 haplotype, which is characterized by a Ser219Gly substitution in the transmembrane domain, rendering the receptor more sensitive to cleavage. Because sEPCR production is not completely blocked by metalloprotease inhibition, we looked for another mechanism. Comparing mRNA expression patterns and levels in A3 and non-A3 cells from 32 human umbilical cord veins, we detected a truncated mRNA in addition to the full-length mRNA. This truncated mRNA was 16 times more abundant in A3 human umbilical vein endothelial cells than in non-A3 human umbilical vein endothelial cells and encoded a protein lacking the transmembrane domain. We stably expressed a recombinant form of this protein (rEPCRisoform) and a protein mimicking the plasma sEPCR (rEPCRsol). Functional studies of the purified recombinant proteins revealed that the rEPCRisoform bound to recombinant protein C with similar affinity than rEPCRsol and that it also inhibited the anticoagulant activity of APC. Trace amounts of the EPCR isoform were found in the plasma of A3 subjects. These results suggest that the sEPCRisoform could contribute to the regulatory effect of sEPCR in plasma.

scholarly journals Enhancement by human umbilical vein endothelial cells of factor Xa- catalyzed activation of factor VII

Blood ◽  
1988 ◽  
Vol 71 (3) ◽  
pp. 791-796
Author(s):  
LV Rao ◽  
SI Rapaport ◽  
M Lorenzi
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Vascular Endothelial Cell ◽  
Factor Xa ◽  
Reaction Rates ◽  
Factor Vii ◽  
Activate Factor ◽  
Human Umbilical Vein ◽  
Factor Va ◽  
Umbilical Vein Endothelial Cells

In blood coagulation on endothelium, an unperturbed vascular endothelial cell surface apparently provides activity equivalent to the phospholipid needed for generation of factor Xa and thrombin in soluble systems. Phospholipid in soluble systems also markedly enhances the ability of factor Xa to activate factor VII; therefore we investigated the influence of an unperturbed monolayer of human umbilical vein endothelial cells (HUVEC) upon factor VII activation. HUVEC were found to augment factor Xa-catalyzed activation of factor VII. This appeared to result from the binding of trace amounts of factor Xa to the cells. Adding active site-inhibited factor Xa to reaction mixtures, but not factor X, abolished the enhanced activation. Adding either anti-factor V antibodies or exogenous factor Va had no effect upon reaction rates. Thus factor Va does not function as a cofactor for the reaction. In further experiments the effect upon activation of factor VII and prothrombin was studied by varying the order of addition of factor Xa and factor Va to supernatants of HUVEC monolayers. Evidence was obtained that HUVEC, unlike platelets, possess a functional factor Xa binding site that is independent of factor Va. Since phospholipid is the only known cofactor for factor Xa/Ca2+-induced activation of factor VII, the demonstration of enhanced activation of factor VII in the presence of unperturbed cultured HUVEC supports a hypothesis that the functional equivalent of procoagulant phospholipid is available on the luminal surface of vascular endothelium in vivo.

scholarly journals Activation of prothrombin in the presence of human umbilical-vein endothelial cells

1992 ◽  
Vol 281 (3) ◽  
pp. 661-664 ◽  
Author(s):  
P Schoen ◽  
C Reutelingsperger ◽  
T Lindhout
Keyword(s):  
Endothelial Cells ◽  
Time Delay ◽  
Umbilical Vein ◽  
Factor Xa ◽  
Fluid Phase ◽  
Human Umbilical Vein ◽  
Factor Va ◽  
Umbilical Vein Endothelial Cells ◽  
Prothrombinase Activity

Addition of Factor Xa, Factor Va and prothrombin to immobilized cultured human umbilical-vein endothelial cells resulted after a time delay in thrombin formation. The prothrombin-converting (prothrombinase) activity, however, was not associated with the cell surface. Rather, perturbation by thrombin, either formed in situ or exogenously added, induced a procoagulant phospholipid surface in the fluid phase, which, in the presence of Factor Xa and Factor Va, enabled the assembly of prothrombinase.

scholarly journals Enhancement by human umbilical vein endothelial cells of factor Xa- catalyzed activation of factor VII

Blood ◽  
1988 ◽  
Vol 71 (3) ◽  
pp. 791-796 ◽  
Author(s):  
LV Rao ◽  
SI Rapaport ◽  
M Lorenzi
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Vascular Endothelial Cell ◽  
Factor Xa ◽  
Reaction Rates ◽  
Factor Vii ◽  
Activate Factor ◽  
Human Umbilical Vein ◽  
Factor Va ◽  
Umbilical Vein Endothelial Cells

Abstract In blood coagulation on endothelium, an unperturbed vascular endothelial cell surface apparently provides activity equivalent to the phospholipid needed for generation of factor Xa and thrombin in soluble systems. Phospholipid in soluble systems also markedly enhances the ability of factor Xa to activate factor VII; therefore we investigated the influence of an unperturbed monolayer of human umbilical vein endothelial cells (HUVEC) upon factor VII activation. HUVEC were found to augment factor Xa-catalyzed activation of factor VII. This appeared to result from the binding of trace amounts of factor Xa to the cells. Adding active site-inhibited factor Xa to reaction mixtures, but not factor X, abolished the enhanced activation. Adding either anti-factor V antibodies or exogenous factor Va had no effect upon reaction rates. Thus factor Va does not function as a cofactor for the reaction. In further experiments the effect upon activation of factor VII and prothrombin was studied by varying the order of addition of factor Xa and factor Va to supernatants of HUVEC monolayers. Evidence was obtained that HUVEC, unlike platelets, possess a functional factor Xa binding site that is independent of factor Va. Since phospholipid is the only known cofactor for factor Xa/Ca2+-induced activation of factor VII, the demonstration of enhanced activation of factor VII in the presence of unperturbed cultured HUVEC supports a hypothesis that the functional equivalent of procoagulant phospholipid is available on the luminal surface of vascular endothelium in vivo.

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