scholarly journals von Willebrand's disease characterized by increased ristocetin sensitivity and the presence of all von Willebrand factor multimers in plasma

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 668-672 ◽  
Author(s):  
L Holmberg ◽  
E Berntorp ◽  
M Donner ◽  
IM Nilsson
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Severe Bleeding ◽  
Molecular Defect ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Coagulant Activity ◽  
The One ◽  
Von Willebrand ◽  
Willebrand Factor

In eight members of one family, platelets in platelet-rich plasma aggregated at much lower ristocetin concentrations than normal. Ivy bleeding time was variously prolonged, and von Willebrand factor antigen (vWF:Ag), ristocetin cofactor activity, and factor VIII coagulant activity were decreased. Most of the affected members had had slight to rather severe bleeding symptoms. Platelet-type von Willebrand's disease (vWD) could be ruled out. All multimers of vWF:Ag were found in plasma as well as platelets. Administration of 1-desamino- 8-D-arginine vasopressin (DDAVP) to the propositus did not cause thrombocytopenia, and platelet-poor plasma obtained immediately after did not aggregate normal platelets. The molecular defect in this family, inherited as an autosomal dominant, resembles the one in type IIB because of the response to ristocetin but differs from IIB because all vWF:Ag multimers are present in plasma and the response to DDAVP is atypical. We conclude that this family has a new subtype of vWD and propose that structural as well as functional criteria should be used for a proper classification of vWD.

scholarly journals von Willebrand's disease characterized by increased ristocetin sensitivity and the presence of all von Willebrand factor multimers in plasma

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 668-672 ◽  
Author(s):  
L Holmberg ◽  
E Berntorp ◽  
M Donner ◽  
IM Nilsson
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Severe Bleeding ◽  
Molecular Defect ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Coagulant Activity ◽  
The One ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract In eight members of one family, platelets in platelet-rich plasma aggregated at much lower ristocetin concentrations than normal. Ivy bleeding time was variously prolonged, and von Willebrand factor antigen (vWF:Ag), ristocetin cofactor activity, and factor VIII coagulant activity were decreased. Most of the affected members had had slight to rather severe bleeding symptoms. Platelet-type von Willebrand's disease (vWD) could be ruled out. All multimers of vWF:Ag were found in plasma as well as platelets. Administration of 1-desamino- 8-D-arginine vasopressin (DDAVP) to the propositus did not cause thrombocytopenia, and platelet-poor plasma obtained immediately after did not aggregate normal platelets. The molecular defect in this family, inherited as an autosomal dominant, resembles the one in type IIB because of the response to ristocetin but differs from IIB because all vWF:Ag multimers are present in plasma and the response to DDAVP is atypical. We conclude that this family has a new subtype of vWD and propose that structural as well as functional criteria should be used for a proper classification of vWD.

scholarly journals Characterization of the defect of the factor VIII/von Willebrand factor protein in von Willebrand's disease

Blood ◽  
1982 ◽  
Vol 59 (3) ◽  
pp. 542-548 ◽  
Author(s):  
HR Gralnick ◽  
MC Cregger ◽  
SB Williams
Keyword(s):  
Sialic Acid ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Molecular Forms ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Platelet Receptor ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract The factor VIII/von Willebrand factor (f.VIII/vWf) protein was purified from the plasma of a patient with von Willebrand's disease (vWd). The patient had all of the classic laboratory findings of vWd except for the ristocetin-induced platelet aggregation of his own platelet-rich plasma. The disease has been documented in three generations. Comparison of the purified normal and vWd f.VIIi/vWf protein revealed several abnormalities, including decreased concentration of f.VIII/vWf antigen; decreased specific vWf activity; absence of the larger molecular forms of the f.VIII/vWf protein; carbohydrate deficiencies affecting the sialic acid, penultimate galactose and N- acetylglucosamine moieties; and decreased binding of the f.VIII/vWf protein to its platelet receptor. These studies indicate the multiplicity of biochemical and functional abnormalities associated with the f.VIII/vWf protein in vWd. f.VIII/vWf protein to normal f.VIII/vWf protein that had been treated with 2-mercaptoethanol (2-ME) to reduce the multimer size and then treated with specific exoglycosidases to remove the sialic acid and penultimate galactose residues revealed similar biologic properties.

Agglutination of Platelet-Type von Willebrand’s Disease Platelets by Bovine von Willebrand Factor

1985 ◽  
Vol 53 (02) ◽  
pp. 204-207
Author(s):  
Hoyu Takahashi ◽  
Akira Shibata
Keyword(s):  
Von Willebrand Factor ◽  
Binding Sites ◽  
Platelet Rich Plasma ◽  
Membrane Receptors ◽  
Von Willebrand's Disease ◽  
Washed Platelet ◽  
Platelet Receptors ◽  
Von Willebrand’S Disease ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryIt has been shown that platelets from patients with platelet- type von Willebrand’s disease (vWD) agglutinate upon the addition of human von Willebrand factor (vWF) in the absence of ristocetin or botrocetin, suggesting that platelet membrane receptors for human vWF is abnormal. The present work reports the platelet agglutinability on stimulation with bovine vWF in platelet-type vWD. Platelets in patient platelet-rich plasma or washed platelet suspensions and patient platelets treated with formalin agglutinated in the presence of markedly lower concentrations of bovine vWF than those required for normal platelets. This finding provides additional evidence that platelet-type vWD platelets have abnormal expression of binding sites for vWF on their surface, and supports that platelet receptors for bovine vWF are identical or very close to those for human vWF.

scholarly journals In vivo interaction of von Willebrand factor with platelets following cryoprecipitate transfusion in platelet-type von Willebrand's disease

Blood ◽  
1984 ◽  
Vol 63 (1) ◽  
pp. 226-230
Author(s):  
JL Miller ◽  
BD Boselli ◽  
JM Kupinski
Keyword(s):  
Molecular Weight ◽  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Platelet Factor ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Von Willebrand ◽  
Willebrand Factor

Previous studies performed in vitro have indicated that platelets from patients with platelet-type von Willebrand's disease (vWD) have receptors for von Willebrand factor (vWF) already exposed on their surfaces and that the addition of purified vWF or cryoprecipitate to patient platelet-rich plasma under stirring conditions is capable of inducing platelet aggregation and secretion. The present work reports the results of the transfusion of cryoprecipitate in a patient with platelet-type vWD. It is shown that, while factor VIII-related antigen and ristocetin cofactor activities maintain elevated levels for up to 12 hr following transfusion, the highest molecular weight vWF multimers decline rapidly. The platelet count also declines, followed in turn by a rise in the plasma level of platelet factor 4. Shortening of the bleeding time occurs only very transiently. The results of this study provide direct evidence that, in patients with platelet-type vWD, an abnormal interaction of their platelets with plasma vWF occurs in vivo, resulting in the absence of high molecular weight vWF multimers, low platelet counts, and impaired hemostasis that are characteristic of this disease.

scholarly journals Characterization of the defect of the factor VIII/von Willebrand factor protein in von Willebrand's disease

Blood ◽  
1982 ◽  
Vol 59 (3) ◽  
pp. 542-548 ◽  
Author(s):  
HR Gralnick ◽  
MC Cregger ◽  
SB Williams
Keyword(s):  
Sialic Acid ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Molecular Forms ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Platelet Receptor ◽  
Von Willebrand ◽  
Willebrand Factor

The factor VIII/von Willebrand factor (f.VIII/vWf) protein was purified from the plasma of a patient with von Willebrand's disease (vWd). The patient had all of the classic laboratory findings of vWd except for the ristocetin-induced platelet aggregation of his own platelet-rich plasma. The disease has been documented in three generations. Comparison of the purified normal and vWd f.VIIi/vWf protein revealed several abnormalities, including decreased concentration of f.VIII/vWf antigen; decreased specific vWf activity; absence of the larger molecular forms of the f.VIII/vWf protein; carbohydrate deficiencies affecting the sialic acid, penultimate galactose and N- acetylglucosamine moieties; and decreased binding of the f.VIII/vWf protein to its platelet receptor. These studies indicate the multiplicity of biochemical and functional abnormalities associated with the f.VIII/vWf protein in vWd. f.VIII/vWf protein to normal f.VIII/vWf protein that had been treated with 2-mercaptoethanol (2-ME) to reduce the multimer size and then treated with specific exoglycosidases to remove the sialic acid and penultimate galactose residues revealed similar biologic properties.

scholarly journals In vivo interaction of von Willebrand factor with platelets following cryoprecipitate transfusion in platelet-type von Willebrand's disease

Blood ◽  
1984 ◽  
Vol 63 (1) ◽  
pp. 226-230 ◽  
Author(s):  
JL Miller ◽  
BD Boselli ◽  
JM Kupinski
Keyword(s):  
Molecular Weight ◽  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Platelet Factor ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Previous studies performed in vitro have indicated that platelets from patients with platelet-type von Willebrand's disease (vWD) have receptors for von Willebrand factor (vWF) already exposed on their surfaces and that the addition of purified vWF or cryoprecipitate to patient platelet-rich plasma under stirring conditions is capable of inducing platelet aggregation and secretion. The present work reports the results of the transfusion of cryoprecipitate in a patient with platelet-type vWD. It is shown that, while factor VIII-related antigen and ristocetin cofactor activities maintain elevated levels for up to 12 hr following transfusion, the highest molecular weight vWF multimers decline rapidly. The platelet count also declines, followed in turn by a rise in the plasma level of platelet factor 4. Shortening of the bleeding time occurs only very transiently. The results of this study provide direct evidence that, in patients with platelet-type vWD, an abnormal interaction of their platelets with plasma vWF occurs in vivo, resulting in the absence of high molecular weight vWF multimers, low platelet counts, and impaired hemostasis that are characteristic of this disease.

VON WILLEBRAND'S DISEASE TYPE IIB ASSOCIATED TO A COMPLEX THROMBOCYTOPENIC THROMBOCYTOPATHY

1987 ◽  
Author(s):  
J Batlle ◽  
M F López-Fernández ◽  
C López-Berges ◽  
R Sánchez ◽  
L G Villarón ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Severe Bleeding ◽  
Platelet Factor ◽  
Von Willebrand's Disease ◽  
Distribution Width ◽  
Heterogeneous Distribution ◽  
Von Willebrand’S Disease ◽  
Platelet Disorder ◽  
Von Willebrand ◽  
Willebrand Factor

A family bleeding disorder characterized by a new association between Type IIB von Willebrand's disease (vWD) and a complex platelet disfunction, with an intermittent thrombocytopenia is described in two patients from the same generation. The mother and a maternal aunt died having severe bleeding diathesis. The platelet abnormalities included: borderline or slightly low platelet count but moderate thrombocytopenia coincedent with the acute bleeding episodes, giant platelet site with a very heterogeneous distribution width, large number of vesicles in platelets by electron-microscopy recalling the "Swiss-Cheese" platelets, abnormal platelet aggregation induced by ADP, collagen, epinephrin and slightly, by thrombin, defective release of 14C-Serotonin, von Willebrand factor (vWF) and platelet factor 4 induced by thrombin or ADP. DDAVP was given to both patient and a partial and transitory correction of bleeding time, thrombocytopenia, presence of platelet aggregates on smear besides a brief appearence of larger multimers of vWF and an increase in all Factor VIII/von Willebrand Factor (FVIII/vWF) properties were seen. Binding of labeled vWF using radiolabelled monoclonal anti-vWF antibody showed an enhanced binding of the patients' vWF, induced by ristocetin, to either normal or patients' platelets. In contrast, the binding of labeled purified normal vWF induced by thrombin to patients' platelets was decreased as compared with the correspondent control. Thus, both patients have platelet disfunctions characteristic for more than one specific platelet disorder. Several associations between platelet and FVIII/vWF abnormalities have been described. This is the first family presenting association of Type IIB vWD and a complex thrombocytopathy. The inherited or acquired (induced by the abnormal IIB vWF platelet interaction) nature of the abnormality is discussed.

Further Studies on Aggregation of Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

1986 ◽  
Vol 55 (03) ◽  
pp. 338-341 ◽  
Author(s):  
H Takahashi ◽  
W Tatewaki ◽  
M Hanano ◽  
R Nagayama ◽  
A Shibata
Keyword(s):  
Von Willebrand Factor ◽  
Ricinus Communis ◽  
Divalent Cations ◽  
Peanut Agglutinin ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Ricinus Communis Agglutinin ◽  
Von Willebrand ◽  
Induced Aggregation ◽  
Willebrand Factor

SummaryPlatelet-type von Willebrand’s disease (vWD) is a bleeding disorder characterized by a heightened interaction between platelets and von Willebrand factor (vWF) as the result of an intrinsic platelet abnormality (probably in GPIb). Platelet aggregability was nearly normal in response to thrombin, wheat germ agglutinin and Ricinus communis agglutinin in this disorder. Unmodified platelets showed no aggregation upon the addition of peanut agglutinin. Partially purified human vWF induced little aggregation of washed patient platelets, but the aggregation was greatly enhanced in the presence of plasma devoid of vWF. Monoclonal antibodies directed against GPIb and GPIIb/IIIa as well as EDTA completely inhibited vWF-induced aggregation. These results indicate that human vWF induces aggregation of platelet-type vWD platelets in the presence of divalent cations and some plasma cofactor(s), and that both GPIb and GPIIb/IIIa are involved in this aggregation.

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