OMIM Entry # 613554 VON WILLEBRAND DISEASE TYPE 2; VWD2 — Volkswagen Typ 2

29 Янв 2015 | Author: | Комментарии к записи OMIM Entry # 613554 VON WILLEBRAND DISEASE TYPE 2; VWD2 — Volkswagen Typ 2 отключены
Volkswagen Typ 2

Von Willebrand Disease Type 2A

The VWF protein in von Willebrand disease 2A has decreased platelet adhesion due to a deficiency of high molecular multimers. The decrease in large can be due to (1) a failure to synthesize the multimers 1’) or (2) enhanced ADAMTS13 )-mediated proteolysis of the secreted molecular weight protein 2’). Regardless of mechanism in 2A, the loss of large multimers is with decreased VWF-platelet and/or decreased VWF-connective interactions (reviews by Sadler et al. and Lillicrap, 2009 ).

Historically, 2A was subclassified into types IIC, IID, and IIE. The VWF in type IIA showed increased by ADAMTS13; type IIC showed multimerization in the Golgi apparatus due to in the VWF propeptide (Zimmerman and Ruggeri, ); type IID showed impaired in the endoplasmic reticulum due to mutations in the domain; and type IIE showed intersubunit disulfide bond in the Golgi apparatus (Sadler et al. ) and a lack of outer proteolytic on gel electrophoresis, indicating reduced (Zimmerman et al. 1986 ). All these showed dominant inheritance for IIC, which showed inheritance. These subtypes of 2A are no longer used because the has not shown clinical utility; all are now to as type 2A (Sadler et al. 2006 ).

Gralnick et al. (1985) found in VWD type 2A, inhibition of a calcium-dependent in vitro resulted in correction of the multimeric structure. This that an abnormal VWF protein in this disorder is susceptible to degradation, a process which may an important role in phenotypic of the disease.


Von Willebrand Disease 2B

The mutant VWF protein in VWD type 2B increased affinity to platelet (606672 ), resulting in increased aggregation, and increased proteolysis of VWF causing a decrease of large VWF Patients often have thrombocytopenia due to platelet consumption et al. 2006 ).

Othman and Favaloro reviewed the complexity of VWD type 2B, that atypical forms complete VWF monomers, no mutations in the A1 or with giant platelets also been reported, the presence of phenotypic modifiers.

Saba et al. (1985) found thrombocytopenia, in vivo platelet formation, and spontaneous platelet in vitro in affected members of a with VWD type 2B. The 4 affected members identified were a man and 2 and a daughter by 2 different wives.

et al. (1986) reported a Swedish in which 8 members had a variant of VWD 2B, referred to as ‘type 2 Malmo.’ was a mild bleeding disorder, and studies showed that aggregated at much lower concentrations than normal. The time was variously prolonged, and VWF activity, and F8 were decreased. All VWF were present, and there was no The defect in this family, as an autosomal dominant, resembled of type 2B because of the response to but differed because all VWF multimers present. Weiss and Sussman reported a similarly affected and referred to this variant as I New York’ (Sadler et al. 2006 ). et al. (1988) also described variant and noted that was no spontaneous aggregation of platelets. et al. (1993) reviewed the family by Holmberg et al. (1986) and reported affected German family. individuals had only mild Sadler et al. (2006) emphasized the variant reported by Wylie et al. and others was a form of VWD type 2B, increased sensitivity to ristocetin in

Donner et al. (1987) described 2 with an apparently autosomal form of type 2B von Willebrand The patients presented in infancy thrombocytopenia.

Murray et al. (1991) evidence of gonadal mosaicism in the of 2 sibs with VWD type 2B who had the same VWF gene, as marked by i.e. haplotype, as did 7 unaffected

Jackson et al. (2009) identified a V1316M substitution (613160.0007 ) in members of a large French family with VWD type 2B had been described originally by and D’Angelo (1963) ; Milton and (1979). and Milton et al. (1984) to the disorder in the family as ‘Montreal syndrome.’ Affected individuals had bruising; some patients had postoperative bleeding, postpartum and gastrointestinal bleeding. A significant of platelets occurred in microaggregates containing 2 to 6 platelets, and the aggregation be increased by stirring. Milton and (1979) suggested that the of abnormally large platelets was to a defect in the mechanism that platelet size and shape shape change. Jackson et al. found that affected members had macrothrombocytopenia, borderline to VWF antigen, low ristocetin cofactor and normal factor VIII activity, all consistent with VWD 2B.

Von Willebrand Disease Type 2M

Volkswagen Typ 2

The VWF protein in VWD type 2M shows platelet adhesion without a of high molecular weight This functional defect is by mutations that disrupt VWF to platelets or to subendothelium, consistent a loss of function (Sadler et al. ).

Stepanian et al. (2003) reported a mother and son with VWD type 2M. patients had a moderate bleeding with epistaxis and easy Laboratory studies showed decreased VWF antigen levels, multimers, and severely decreased VWF activity. Factor VIII was decreased and platelet counts normal.

Von Willebrand Disease 2N

The mutant VWF protein in VWD type 2N markedly decreased binding for factor VIII, and this may be with mild hemophilia A ) (Sadler et al. 2006 ). The phenotype is by a disproportionate decrease in F8 compared to VWD type 2N usually shows recessive inheritance (Sadler et al. ). Gaucher et al. (1991) noted the phenotype resembled hemophilia A, or F8 but showed autosomal recessive of X-linked inheritance.

Mazurier et al. (1990) reported a French woman, born of parents, with VWD type 2N designated the ‘Normandy’ variant). She had a history of excessive bleeding, and data showed decreased VIII, subnormal bleeding and normal VWF multimers. VWF isolated patient plasma was unable to factor VIII. Lopez-Fernandez et al. described a brother and sister VWD characterized by abnormal binding of von factor to factor VIII. were presumably homozygous for a VWF defect. Hilbert et al. (2004) 2 unrelated French patients VWD type 2N. Both were with lifelong histories of bleeding and menorrhagia. Laboratory showed a dramatic decrease in VWF capacity.

Von Willebrand Disease 2CB

Riddell et al. (2009) proposed a new of VWF characterized by clinically significant episodes due to a mutant VWF protein defective collagen binding, ‘VWF 2CB.’ Laboratory showed normal values of to VWF:Ag (RCo:Ag), normal VWF analysis, and normal ristocetin-induced aggregation, but markedly reduced of VWF collagen-binding activity to VWF antigen against type III collagen and I collagen. Riddell et al. (2009) that the defect was distinct VWF type 2M, in that type 2M is characterized by impaired binding to GP1BA and can show a full of associated VWF multimers.

Volkswagen Typ 2
Volkswagen Typ 2
Volkswagen Typ 2
Volkswagen Typ 2
Volkswagen Typ 2

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