Relationship between the Binding Sites for von Willebrand Factor, Phospholipid, and Human Factor VIII C2 Inhibitor Alloantibodies within the Factor VIII C2 Domain

2007 ◽  
Vol 85 (4) ◽  
pp. 317-322 ◽  
Author(s):  
Keiji Nogami ◽  
Midori Shima ◽  
John Giddings ◽  
Masahiro Takeyama ◽  
Ichiro Tanaka ◽  
...  
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Binding Sites ◽  
Human Factor ◽  
C2 Domain ◽  
Human Factor Viii ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Factor VIII/von Willebrand factor in subendothelium mediates platelet adhesion

Blood ◽  
1985 ◽  
Vol 65 (4) ◽  
pp. 823-831 ◽  
Author(s):  
VT Turitto ◽  
HJ Weiss ◽  
TS Zimmerman ◽  
II Sussman
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Vessel Wall ◽  
Platelet Adhesion ◽  
Human Factor ◽  
Rabbit Aorta ◽  
Human Factor Viii ◽  
Plasma Factor ◽  
Von Willebrand ◽  
Willebrand Factor

The present studies were undertaken to determine whether factor VIII/von Willebrand factor (vWF) present in the vessel wall (in addition to that in plasma) may mediate the attachment of platelets to subendothelium. Subendothelium from everted rabbit aorta was exposed to human citrated blood flowing through an annular perfusion chamber at 40 mL/min (wall shear rate of 2,600 s-1 for five minutes). The vessel segments were incubated at 37 degrees C for one hour with various dilutions of either goat-anti-rabbit factor VIII/vWF serum or an IgG fraction prepared from the serum. Control segments were incubated with serum or IgG from a nonimmunized goat. Values of platelet contact (C), platelet adhesion (C + S), and thrombus formation (T) on the subendothelium were evaluated by a morphometric technique. Compared with vessels incubated with fractions prepared from a normal goat, a significant decrease in platelet adhesion (C + S), ranging from 45% to 65%, was observed on vessels incubated with various dilutions (1:5 to 1:50) of either serum or IgG fractions of goat-anti-rabbit factor VIII/vWF. A similar decrease in platelet adhesion was observed with vessels incubated with an F(ab')2 fragment against rabbit factor VIII/vWF prepared in the goat. When goat-anti-rabbit factor VIII/vWF IgG was added to rabbit blood (1:75 dilution), platelet adhesion was reduced to the same extent (65%) on normal rabbit vessels and on vessels pre-incubated with goat-anti-rabbit factor VIII/vWF. Immunofluorescence studies revealed the presence of rabbit factor VIII/vWF in the subendothelium of rabbit aorta and the continued binding of the goat-anti-factor VIII/vWF antibodies on subendothelium during the perfusion studies. No uptake of human factor VIII/vWF on the rabbit subendothelium was observed by this immunologic technique; human factor VIII/vWF was found to be entirely associated with the attached human platelets. Thus, factor VIII/vWF in the vessel wall may mediate platelet attachment to subendothelium in a manner similar to that of plasma factor VIII/vWF.

scholarly journals von Willebrand Factor Activity in Plasmin Digests of Factor VIII

1977 ◽  
Author(s):  
J. A. Guisasola ◽  
C. Cockburn ◽  
R. M. Hardisty
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Human Factor ◽  
Factor Activity ◽  
Group Iii ◽  
Molecular Weights ◽  
Human Factor Viii ◽  
Group Ii ◽  
Von Willebrand ◽  
Willebrand Factor

Purified human factor VIII was incubated for up to 24 hours with plasmin, and the activity of the breakdown products studied at intervals. Factor VIII coagulant activity was lost within the first hour, but von Willebrand factor activity (FVIIIR:WF) was retained for two hours, and then declined slowly during the subsequent incubation. Analysis of the 24-hour breakdown products by immuno-electrophoresis, sepharose 4B chromatography and SDS Polyacrylamide electrophoresis revealed three main groups of fragments recognised by rabbit anti-human factor VIII anti-serum, and having molecular weights in the following ranges: Group 1 300,000=500,000; Group II, 150–200,000; Group III, 100,000. FVIIIR:WF activity, which was found only in Group II, appeared to be associated with glycopeptide(s) of up to 155,000 daltons.

scholarly journals Characterization of human factor VIII and interaction with von Willebrand factor. An electron microscopic study

1990 ◽  
Vol 194 (2) ◽  
pp. 491-498 ◽  
Author(s):  
Harry F. G. HEIJNEN ◽  
Joost. A. KOEDAM ◽  
Helena SANDBERG ◽  
Nel H. BEESER-VISSER ◽  
Jan. W. SLOT ◽  
...  
Keyword(s):  
Factor Viii ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Von Willebrand Factor ◽  
Human Factor ◽  
Electron Microscopic ◽  
Human Factor Viii ◽  
Von Willebrand ◽  
Willebrand Factor

SYNTHESIS. PROCESSING AND SECRETION OF HUMAN FACTOR VIII IN MAMMALIAN CELLS: REQUIREMENT FOR VON WILLEBRAND FACTOR

1987 ◽  
Author(s):  
Louise C Wasley ◽  
Andrew J Dorner ◽  
Randal C Kaufman
Keyword(s):  
Factor Viii ◽  
Cell Lines ◽  
Von Willebrand Factor ◽  
Light Chain ◽  
Human Factor ◽  
Conditioned Media ◽  
Mammalian Cell Lines ◽  
Human Factor Viii ◽  
Von Willebrand ◽  
Willebrand Factor

In the plasma factor VIII exists as a complex with von Willebrand factor (vWF). The cloning of the cDNA for factor VIII has provided the ability to develop mammalian cell lines which express high levels of factor VIII by using appropriatate expression plasmids and DNA cotransformation with selectable markers. We have studied the synthesis, processing, and secretion of factor VIII expressed in baby hamster kidney cells and in Chinese hamster ovary cells by 35S-methionine pulse and chase labeling and analysis by immunoprecipitation with specific antibodies which recognize the light and heavy chains of factor VIII. In both mammalian cell lines, factor VIII is synthesized as a primary translation product of 230 kDa. A significant amount remains within the endoplasmic reticulum in a stable complex with a glucose regulated protein of 78 kDa. The remainder traverses into the Golgi compartment where it is cleaved to the heavy and light chain forms. Very shortly thereafter the mature factor VIII appears in the conditioned media as the mature heavy and light chain species. Very little single chain factor VIII is secreted into the conditioned media. The accumulation of factor VIII in the conditioned media requires the presence of vWF factor. In the absence of vWF, the factor VIII appears as unassociated heavy and light chains which are rapidly degraded. Bovine, porcine, or human 3WF all effectively stabilize human factor VIII expressed in these rodent cell lines. These results suggest the presence of vWF promotes factor VIII chain association which stabilizes the factor VIII to proteolysis.

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