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Relevant bibliographies by topics / Von Willebrand disease (vWD)

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Academic literature on the topic 'Von Willebrand disease (vWD)'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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Journal articles on the topic "Von Willebrand disease (vWD)"

1

Scharrer, I. "Women with von Willebrand disease." Hämostaseologie 24, no. 01 (2004): 44–49. http://dx.doi.org/10.1055/s-0037-1619605.

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SummaryThe clinical presentation of VWD shows sex-related differences of symptoms. In women the most typical symptoms are menorrhagia, bleeding during and after delivery or abortion and bleeding in connection with caesarean section or gynaecological surgery. Menorrhagia is one of the most common symptoms presented to gynaecologists. In 7-20% of menorrhagia the underlying cause is VWD, in our cohort of 185 women with menorrhagia the prevalence of VWD was even 32%. On the other hand in women with VWD menorrhagia with onset at the menarche can be found in 60-93%, influencing substantially their morbidity and quality of life. During pregnancy women with mild VWD experience a decrease of bleeding tendency due to an increase of endogenous VWF. But as the VWF concentration drops rapidly after delivery, the post-partum period is often associated with significant bleeding complications. In severe forms of VWD the bleeding risk is high during delivery and postpartum period. Laboratory monitoring and therapeutical measures should be continued for 8-10 days after delivery. During menopause the clinical situation improves for most of the women with mild or moderate VWD.

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Arif, Mansyur. "Laboratory Diagnosis of von Willebrand's Disease." Indonesian Biomedical Journal 1, no. 3 (December 1, 2009): 57. http://dx.doi.org/10.18585/inabj.v1i3.100.

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von Willebrand's disease (vWD) is an autosomally inherited bleeding disorder caused by a deficiency or abnormality of von Willebrand factor (vWF). vWF is a multimeric adhesive protein that plays an important role in primary hemostasis by promoting platelet adhesion to the subendothelium at the sites of vascular injury. It is also the carrier of factor VIII (FVIII), thus indirectly contributing to the coagulation process. Bleeding symptoms are usually mucocutaneous and postsurgical with varying severity. The diagnosis of vWD requires a personal and family history of bleeding and confirmation by laboratory analysis involving vWF antigen level, vWF ristocetin cofactor, FVIII activity, ristocetin-induced platelet aggregation, and vWF multimer analysis.KEYWORDS: von Willebrand's disease, von Willebrand factor

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Sanders, Yvonne V., Dafna Groeneveld, Karina Meijer, Karin Fijnvandraat, Marjon H. Cnossen, Johanna G. van der Bom, M. Coppens, et al. "von Willebrand factor propeptide and the phenotypic classification of von Willebrand disease." Blood 125, no. 19 (May 7, 2015): 3006–13. http://dx.doi.org/10.1182/blood-2014-09-603241.

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Key Points VWFpp discriminates between type 3 VWD patients and severe type 1 VWD patients with very low VWF levels. The pathophysiological mechanisms of all types of VWD can be defined by the combined ratios of VWFpp/VWF:Ag and FVIII:C/VWF:Ag.

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Varma, Subhash, Pankaj Malhotra, Jasmina Ahluwalia, Aashima Arora, Rashmi Bagga, and Akanksha Jangid. "Von Willebrand Disease in Pregnancy." Journal of Postgraduate Medicine, Education and Research 48, no. 3 (2014): 157–58. http://dx.doi.org/10.5005/jp-journals-10028-1123.

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ABSTRACT Von Willebrand disease (vWD) is the most common inherited bleeding disorder. It is due to deficiency of von Willebrand factor (vWF) which may be either quantitative or qualitative. There are 3 types of vWD out of which Type III is the rarest but the most severe. We report a 27 years second gravida diagnosed with vWD in her index pregnancy. Though her antenatal period was uneventful, she developed complications in the perioperative period following a caesarean section. However, with a multidisciplinary team effort, the maternal and fetal outcome were favourable. How to cite this article Bagga R, Jangid A, Gainder S, Malhotra P, Varma S, Ahluwalia J, Arora A. Von Willebrand Disease in Pregnancy. J Postgrad Med Edu Res 2014;48(3):157-158.

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Trossaërt, Marc, Catherine Ternisien, Armelle Lefrancois, Laura Llopis, Jenny Goudemand, Marianne Sigaud, Marc Fouassier, and Claudine Caron. "Evaluation of an Automated von Willebrand Factor Activity Assay in von Willebrand Disease." Clinical and Applied Thrombosis/Hemostasis 17, no. 6 (August 19, 2010): E25—E29. http://dx.doi.org/10.1177/1076029610379848.

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We evaluated the use of the turbidimetric HemosIL von Willebrand Factor (VWF) Activity assay (VWF:Act) on the STA-R automated coagulometer (Stago, Asnières, France) for the diagnosis of von Willebrand disease (VWD). For this, we prospectively screened 268 patients. As a second part, we retrospectively assayed 111 patients with well-defined VWD subtype. In the first prospective study, we demonstrate that in most cases of VWD, VWF ristocetin cofactor activity (VWF:RCo) and VWF:Act are highly correlated but that they both cannot be considered a good screening assay when used alone, since they could miss about 25% of VWF abnormalities. However, the association of VWF:Act analysis and the Platelet Function Analyzer-100 (PFA-100) test constitutes an excellent screening strategy. In our second retrospective study concerning VWD subtypes, VWF:RCo and VWF:Act were well correlated but could be very discrepant, especially for some cases of type 2M VWD. We consider that VWF:RCo remains the “reference assay” for VWD subtype classification.

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Stufano, Francesca, Marco Boscarino, Paolo Bucciarelli, Luciano Baronciani, Alberto Maino, Giovanna Cozzi, and Flora Peyvandi. "Evaluation of the Utility of von Willebrand Factor Propeptide in the Differential Diagnosis of von Willebrand Disease and Acquired von Willebrand Syndrome." Seminars in Thrombosis and Hemostasis 45, no. 01 (June 18, 2018): 036–42. http://dx.doi.org/10.1055/s-0038-1660481.

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AbstractAn increased von Willebrand factor propeptide (VWFpp) to VWF antigen (VWF:Ag) ratio (VWFpp/VWF:Ag) indicates an enhanced clearance of VWF. This finding has been described in von Willebrand disease (VWD) and in acquired von Willebrand syndrome (AVWS). A distinction between these two diseases, one congenital and the other acquired, is primarily based on family and personal history of bleeding. However, if this information is scanty, the diagnosis might be challenging due to the lack of an effective diagnostic biomarker. In this cross-sectional study, we assessed the ability of VWFpp/VWF:Ag for the differential diagnosis between VWD and AVWS. VWFpp/VWF:Ag was measured in a group of 153 patients (125 with VWD and 28 with AVWS). Most patients with AVWS and VWD showed an increased VWFpp/VWF:Ag, although to variable degrees. A marked increase of VWFpp/VWF:Ag was mainly associated with the diagnosis of AVWS and VWD type 1 Vicenza. A receiver operating characteristic curve was used to identify the optimal cutoff of VWFpp/VWF:Ag for discrimination of patients with a modestly increased (most VWD cases) versus those with a markedly increased clearance (AVWS and VWD type 1 Vicenza), and this cutoff was identified at the value of 3.9 (sensitivity: 0.70, specificity: 0.97). The ROC curve sorting from a logistic model containing VWFpp/VWF:Ag, age, and sex had an area under the curve (AUC) of 0.88 (95% confidence interval: 0.80–0.95). A subsequent molecular evaluation discriminated VWD type 1 Vicenza from AVWS. In conclusion, VWFpp/VWF:Ag appears helpful to discriminate patients with a markedly increase VWF clearance (AVWS or VWD type 1 Vicenza) from those with a modestly increased clearance (most VWD patients).

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Periayah, Mercy Halleluyah, Ahmad Sukari Halim, Arman Zaharil Mat Saad, Nik Soriani Yaacob, and Faraizah Abdul Karim. "Report on von Willebrand Disease in Malaysia." Open Access Macedonian Journal of Medical Sciences 4, no. 1 (February 29, 2016): 112–17. http://dx.doi.org/10.3889/oamjms.2016.030.

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BACKGROUND: Von Willebrand disease (vWD) is an inherited hemostatic disorder that affects the hemostasis pathway. The worldwide prevalence of vWD is estimated to be 1% of the general population but only 0.002% in Malaysia.AIM: Our present paper has been written to disclose the statistical counts on the number of vWD cases reported from 2011 to 2013.MATERIAL AND METHODS: This article is based on sociodemographic data, diagnoses and laboratory findings of vWD in Malaysia. A total of 92 patients were reported to have vWD in Malaysia from 2011 to 2013.RESULTS: Sociodemographic-analysis revealed that 60% were females, 63% were of the Malay ethnicity, 41.3% were in the 19-44 year old age group and 15.2% were from Sabah, with the East region having the highest registered number of vWD cases. In Malaysia, most patients are predominately affected by vWD type 1 (77.2%). Factor 8, von Willebrand factor: Antigen and vWF: Collagen-Binding was the strongest determinants in the laboratory profiles of vWD.CONCLUSION: This report has been done with great interest to provide an immense contribution from Malaysia, by revealing the statistical counts on vWD from 2011-2013.

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Lavin, Michelle, and James S. O’Donnell. "New treatment approaches to von Willebrand disease." Hematology 2016, no. 1 (December 2, 2016): 683–89. http://dx.doi.org/10.1182/asheducation-2016.1.683.

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Abstract von Willebrand disease (VWD) is the commonest inherited bleeding disorder and results from either a quantitative or qualitative deficiency in the plasma glycoprotein von Willebrand factor (VWF). Recent large cohort studies have significantly enhanced our understanding of the molecular mechanisms involved in the pathogenesis of VWD. In contrast, however, there have been relatively few advances in the therapeutic options available for the treatment of bleeding in patients with VWD. Established treatment options include tranexamic acid, 1-deamino-8-d-arginine vasopressin (DDAVP), and plasma-derived VWF concentrates. In addition, a recombinant VWF has also recently been developed. In this review, we focus on how recent insights into the clinical and molecular aspects underpinning VWD are already beginning to influence treatment in the clinic. For example, a number of different bleeding assessment tools (BATs) have been developed to objectively assess bleeding symptoms in patients with VWD. Interestingly, however, these BAT scores may also have an important role to play in predicting bleeding risk in VWD. Furthermore, recent studies have demonstrated that enhanced VWF clearance plays a critical role in the etiology of both type 1 and type 2 VWD. These findings have direct translational relevance with respect to the use of DDAVP in patients with VWD. As understanding of the mechanisms involved in VWD pathogenesis continues to advance, novel treatment options are likely to emerge. Critically, however, large adequately powered and stratified clinical trials will be required to address the outstanding questions that remain regarding VWD treatment optimization.

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Henniker, Anthony, David Facey, Mark Hertzberg, and Emmanuel Favaloro. "Discrimination of von Willebrands Disease (VWD) Subtypes: Direct Comparison of von Willebrand Factor:Collagen Binding Assay (VWF:CBA) with Monoclonal Antibody (MAB) Based VWF-capture Systems." Thrombosis and Haemostasis 84, no. 10 (2000): 541–47. http://dx.doi.org/10.1055/s-0037-1614064.

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SummaryDiscrimination of von Willebrand’s Disease (VWD) subtypes is important since it influences management. Qualitative [ie Type 2A, 2B, 2M] defects exhibit von Willebrand factor (VWF) discordance and give high VWF:Ag to VWF:’activity’ ratios. Classically, VWF:’activity’ is assessed using the VWF:RCof assay. The VWF:CBA is an ELISAbased VWF-functional adhesive assay which has consistently proved to be superior to VWF:RCof. A commercially available monoclonal antibody (MAB) based ELISA assay system claimed to mimic a VWF:RCof-like activity has also been recently described (‘SE’), as has the production and characterisation of a large number [n = 10] of locally generated anti-VWF MAB. In the current study, we have adapted these MAB to in-house ELISA assays to assess their utility for VWD diagnosis and subtype discrimination, and to compare them with other assay systems. Thus, the VWF:CBA, VWF:RCof by agglutination, the SE assay, and in-house MAB based assays have been directly compared for their ability to discriminate Type 1 [n = 9] from Type 2 VWD samples [phenotypes 2A and 2B; n = 11]. In summary, MAB-based systems can be used to measure VWF and confirm a diagnosis of VWD, as well as exhibiting some VWD-subtype-discriminatory capabilities. However, better evidence of VWF-discordance was usually achieved using the VWF:RCof (agglutination) assay, while the greatest degree of VWFdiscordance was consistently observed using the VWF:CBA assay. In conclusion, the VWF:CBA assay proved to offer the best diagnostic predictive tool for a Type 2 VWD defect, while MAB-based systems appear to be less effective in this regard. Abbreviations: HMW: High Molecular Weight [VWF], MAB: Monoclonal antibody (/antibodies), PNP: Pooled Normal Plasma, RIPA: Ristocetin induced platelet aggregation, VWD: von Willebrands disease (/disorder), VWF: von Willebrand Factor, VWF:Ag: von Willebrand Factor Antigen (assay), VWF:CBA: Collagen Binding [Activity] Assay for VWF, VWF:RCof: Ristocetin Cofactor Assay for VWF

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Batlle, Javier, Almudena Pérez-Rodríguez, Irene Corrales, Nina Borràs, Joana Costa Pinto, María Fernanda López-Fernández, and Francisco Vidal. "Update on Molecular Testing in von Willebrand Disease." Seminars in Thrombosis and Hemostasis 45, no. 07 (April 30, 2019): 708–19. http://dx.doi.org/10.1055/s-0039-1679922.

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AbstractDiagnosis of von Willebrand disease (VWD) depends on personal and family history of bleeding and confirmatory laboratory testing. Currently available phenotypic tests for VWD contain potential sources for error that may distort results. Despite an exponential growth of information about the von Willebrand factor gene (VWF), the role of molecular diagnosis in VWD is still controversial. Due to the complexity and high cost of conventional molecular analyses, some investigators have recommended limiting this approach to distinguish suspected type 2N VWD from hemophilia A, type 2B from platelet-type VWD, and the exploration of type 3 VWD. New genetic methodologies and approaches are becoming available, but there is still some reluctance for their implementation in VWD diagnosis. This article discusses the pros and cons of molecular testing in VWD considering the experience obtained through the multicenter project “Molecular and Clinical Profile of VWD in Spain (PCM-EVW-ES).”

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Dissertations / Theses on the topic "Von Willebrand disease (vWD)"

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Jenkins, Peter Vincent. "A molecular analysis of Von Willebrand disease." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313808.

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Yadegari, Baharanchi Hamideh [Verfasser]. "Identifying Genetic Basis and Molecular Mechanisms in Different Types of von Willebrand Disease (VWD) / Hamideh Yadegari Baharanchi." Bonn : Universitäts- und Landesbibliothek Bonn, 2013. http://d-nb.info/1044971975/34.

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Siu, Long-kei, and 蕭朗基. "Von Willebrand factor: collagen binding assay(VWF: CBA) assisting in diagnosis of von Willebrand disease inindividuals with menorrhagia." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B46632645.

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Webb, Clare Elizabeth. "Analysis of von Willebrand factor (vWF) multimers in acquired haemostatic disorders." Thesis, University of Portsmouth, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.236399.

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Santos, Karen Freitas. "Enzimas que hidrolisam nucleotídeos de adenina em plaquetas, agregação plaquetária e polimorfismo do gene α2 da integrina α2β1 em pacientes com a doença de von willebrand." Universidade Federal de Santa Maria, 2009. http://repositorio.ufsm.br/handle/1/11105.

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Von Willebrand disease (vWD) is one of the most common inherited bleeding diseases, caused by a qualitative or quantitative deficiency of the von Willebrand factor (vWF). vWF is a multimeric glycoprotein synthesized by megakaryocytes and endothelial cells and it is present in the subendothelial matrix, blood plasma, platelets and endothelium. This glycoprotein represents an important role in thrombus formation by initiating platelet adhesion to sites of injury as well as platelet aggregation. The objective of this study was determine the activities of NTPDase (CD39), 5 -nucleotidase (EC 3.1.3.5, CD73) and Ectonucleotide Pyrophosphatase/Phosphodiesterase (E-NPP) enzymes in platelets patients from von Willebrand disease and healthy patients, as well as ristocetin-induced platelet aggregation (RIPA) and polymorphisms of the α2 gene of the α2β1 integrin. The following groups were studied: 14 patients diagnosed with vWD and 14 healthy patients for control group. For ristocetin-induced platelet aggregation was used a Platelet Rich Plasma (PRP) and Platelet Poor Plasma (PPP), using a final concentration of ristocetin in 1.25mg/mL. The polymorphisms of the α2 gene was analyzed through the Polymerase chain reaction (PCR), used for digestion of the PCR product of the Bgl II restriction site. NTPDase and E-NPP were decreased in platelets of patients with vWD compared to the group control. Moreover, the activity of the enzyme 5'- nucleotidase was not statistically significant. The results of the RIPA were significantly reduced in patients with vWD compared with the control. The allelic frequencies among vWD patients were found to be 78.57% for 807C and 21.43% for 807T. Our results indicate an decreased NTPDase and E-NPP activities in platelets, may be related to the low adhesiveness of platelets in patients with vWD. The allelic frequency 807C predominant suggests, in agreement with other studies, this polymorphism and factor characteristic of hemorrhagic manifestations in patients with DvW.
A doença de von Willebrand (DvW) é uma das mais comuns entre as doenças hemorrágicas, e é provocada por uma deficiência qualitativa ou quantitativa do fator de von Willebrand (FvW). O FvW é uma glicoproteína multimérica sintetizada por megacariócitos e células endoteliais e está presente no matriz subendotelial, no plasma sanguíneo, nas plaquetas e no endotélio. Esta glicoproteína desempenha um papel importante na formação do trombo plaquetário, iniciando a adesão plaquetária ao local do dano vascular, bem como, a agregação plaquetária. O objetivo deste estudo foi determinar a atividade das enzimas NTPDase (EC 3.6.1.5, CD39), 5'-nucleotidase (EC 3.1.3.5, CD73) e Ectonucleotideo pirofasfatase/fosfodiesterase (E-NPP) em plaquetas de pacientes com a DvW e em plaquetas de pacientes saudáveis, bem como agregação plaquetária induzida pela ristocetina (RIPA) e o polimorfismo do gene α2 da integrina α2β1 da superfície de plaquetas. Os grupos foram divididos da seguinte forma: 14 pacientes diagnosticados com DvW e 14 pacientes saudáveis, para o grupo controle. Para a RIPA foram utilizados um Plasma Rico em Plaquetas (PRP) e um Plasma Pobre em Plaquetas (PPP), utilizando-se uma concentração final de ristocetina de 1.25mg/mL. O polimorfismo do gene α2 foi analisado através da reação em cadeia de polimerase (PCR), utilizando para a digestão do produto da PCR a enzima de restrição Bgl II. Constatou-se que a atividade das enzimas NTPDase e E-NPP foram reduzidas em plaquetas de pacientes com DvW comparadas ao grupo controle. Por outro lado, a atividade da enzima 5'-nucleotidase não foi estatisticamente significativa. Os resultados para os RIPA foram significativamente reduzidos em pacientes com DvW comparado com o controle. A freqüência alélica encontrada entre os pacientes com DvW foi de 78,57% para o alelo 807C e de 21,43% para o alelo 807T. Nossos resultados indicam que a redução da atividade da NTPDase e da E-NPP em plaquetas pode estar relacionada à baixa adesividade das plaquetas em pacientes com DvW. A freqüência alélica 807C predominante sugere, de acordo com outros estudos, que este polimorfismo é fator característico das manifestações hemorrágicas em pacientes portadores da DvW.

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Millar, C. M. "Investigation of determinants of clearance of von Willebrand Factor in individuals with type 1 VWD." Thesis, University College London (University of London), 2008. http://discovery.ucl.ac.uk/1444060/.

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The release and clearance of von Willebrand Factor (VWF) in a group of patients with the quantitative deficiency type 1 von Willebrand Disease (VWD) was investigated. This was done by analysis of circulating VWF and VWF released from the endothelial pool on infusion of a vasopressin analogue. A variety of parameters were investigated pre-and post infusion in order to identify VWF gene linked and non-linked variables that could affect VWF clearance. Increased clearance of plasma VWF in a significant proportion of type 1 VWD patients was shown but this was not consistently associated with steady-state levels of VWF, indicating that circulating plasma VWF levels are not a consistent reflection of the VWF life-cycle in this patient group. An association between galactose exposure and reduced levels of VWF was demonstrated by the increased binding of the lectins Ricinus communis and Erythina crystagalli, this was unrelated to clearance. In addition, no significant ABO blood group effect on VWF clearance was demonstrated. The absolute level of ADAMTS-13, and the susceptibility of VWF to cleavage by ADAMTS-13 were not associated with the clearance rate of VWF in patients with type 1 VWD. Three novel candidate mutations were identified in association with significantly accelerated VWF clearance. Notably, candidate mutations were generally identified in patients with steady-state VWF levels reduced to <20 IUdL"1 and family analysis suggests absolute linkage with the VWF gene. Despite demonstrating an increased rate of clearance in the majority of patients with type 1 VWD, no single underlying common characteristic or variable was predominant within this study group.

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Tsui, Sze-pui, and 崔詩珮. "Genotypic characterisation of type 2 von Willebrand disease." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/193528.

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von Willebrand disease (VWD) is the most common autosomal bleeding disorder. It is divided into type 1, 2 and 3. Type 2 VWD shows qualitative defects in VWF and is further sub-classified into type 2A, 2B, 2M and 2N, each having different functional defects in VWF. Most of the associated mutations are located at the exons in VWF which encode for the affected functional domains. Diagnosis of VWD is currently based on history and phenotypic tests, which can be difficult often times. Therefore, molecular diagnosis of type 2 VWD is an attractive alternative. There are only a few genotypic characterisation studies of type 2 VWD in Chinese. This study aims to provide genetic data of type 2 VWD in Hong Kong. Archive DNA samples of 21non-type 2N type 2 VWD patients (Group 1), 15 type 2N/mild haemophilia A (HA) patients (Group2) and 35 control subjects were recruited. VWF exon 27, 28 and exon 18, 19, 20, 23, 24 were Sanger sequenced in Group 1 and Group 2 subjects, respectively. All seven exons were sequenced in the control subjects. Seven of 21 Group 1 subjects were found to have pathogenic mutation sin exon 28, with 2being novel. Only 1 Group 2 subject was found to be heterozygous for a novel non-synonymous variation at exon 23, the significance of which could not be ascertained. Sixteen benign polymorphisms were detected from exons sequenced in patients and controls. The low pathogenic mutation detection rate may suggest that the pattern of mutation in Chinese is different from other populations. The possibility of misdiagnosis in a proportion of these patients cannot be excluded in view of the known difficulty in patient ascertainment in VWD and the limited phenotypic diagnostic tools available in Hong Kong. Further studies of other exons are indicated to document the mutation spectrum of type 2 VWD in our Chinese population. RNA work and functional studies are required to fully characterise novel sequence variations found. High throughput mutation detection platforms and better phenotypic characterisation will facilitate the introduction of VWD genotyping into routine clinical diagnostics.
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Sooteh, Seyed Mohammad Bagher Hashemi. "Molecular basis of type 1 von Willebrand disease." Thesis, University of Sheffield, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.410746.

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Nitu-Whalley, Ioana Camelia. "Diagnosis, classification and treatment of Von Willebrand disease." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270707.

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Al-Buhairan, Ahlam Mubarak. "Characterisation of mutations causing type 1 von Willebrand disease." Thesis, University of Sheffield, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.412786.

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Books on the topic "Von Willebrand disease (vWD)"

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Federici, Augusto B., Christine A. Lee, Erik E. Berntorp, David Lillicrap, and Robert R. Montgomery, eds. Von Willebrand Disease. Oxford, UK: Wiley-Blackwell, 2011. http://dx.doi.org/10.1002/9781444329926.

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James, Andra H. 100 questions & answers about Von Willebrand disease. Sudbury, Mass: Jones and Bartlett, 2009.

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Shapiro, Jane. Diane Dino's dilemma: Diane's story of von Willebrand Disease. Collegeville, PA (500 Arcola Road, Collegville 19426-0107): Armour Pharmaceutical Co., Educational Publications, 1994.

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Jones, Nicola Louise. An investigation of genetic defects in type 1 and type 3 Von Willebrand Disease. Wolverhampton: University of Wolverhampton, 2002.

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1935-, Lusher Jeanne M., and Kessler Craig M, eds. Hemophilia and von Willebrand's disease in the 1990s: A new decade of hopes and challenges : proceedings of the XIX Congress of the World Federation of Hemophilia, Washington, D.C., 14-19 August 1990. Amsterdam: Excerpta Medica, 1991.

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Downey, Laura A., and Nina A. Guzzetta. Von Willebrand Disease. Edited by Kirk Lalwani, Ira Todd Cohen, Ellen Y. Choi, and Vidya T. Raman. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190685157.003.0059.

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Von Willebrand disease (vWD) is the most common bleeding disorder in humans. It is the result of an abnormality in the amount, structure, or function of von Willebrand factor (vWF), a glycoprotein important in maintaining normal hemostasis.. In children with vWD, the most frequent presentation is easy bruising and epistaxis. Other symptoms include hematomas, menorrhagia, and bleeding from minor wounds. Although intraarticular bleeding may occur, especially in certain subtypes, it is much more commonly seen with hemophilia. There are several subtypes of vWD based on the underlying defect in vWF, but, in general, they may be categorized as quantitative (types 1 and 3) or qualitative (all types 2). If vWD is suspected, consultation with a hematologist to establish the correct diagnosis and perioperative approach to hemostasis is essential. Avoidance of medications that interfere with coagulation, anticipation of intraoperative and postoperative bleeding, and an appropriate hemostatic treatment plan should be addressed.

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Global Von Willebrand Disease (VWD) Treatment Market 2022 – Industry Analysis, Market Size, Competitive Trends: Credence Research: Von Willebrand Disease (VWD) Treatment Market. Serena Peter, 2016.

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I, Barnhart Marion, and Lusher Jeanne M. 1935-, eds. Factor VIII/vWF and platelet formation and function in health and disease: A tribute to Marion I. Barnhart. New York, N.Y: New York Academy of Sciences, 1987.

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Von Willebrand factor and Von Willebrand disease. London: Baillière Tindall, 2001.

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Jaques, Michiels Jan, ed. Von Willebrand factor and von Willebrand disease. London: Baillière Tindall, 2001.

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Book chapters on the topic "Von Willebrand disease (vWD)"

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Auerswald, G., B. Eberspächer, W. Kreuz, A. Nimtz, G. Pindur, H. Scheel, and H. H. Wolf. "Successful Treatment of Patients with von Willebrand Disease Using a High-Purity Double Virus Inactivated FVIII/vWF Concentrate (IMMUNATE)." In 30th Hemophilia Symposium Hamburg 1999, 154–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-18240-2_19.

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Nguyen, Trinh, and Lakshmi V. Srivaths. "von Willebrand Disease." In Hematology in the Adolescent Female, 29–42. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-48446-0_3.

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Brown, James P. R., and Joanne Douglas. "von Willebrand Disease." In Consults in Obstetric Anesthesiology, 663–65. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-59680-8_179.

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Castaman, Giancarlo, Alberto Tosetto, and Francesco Rodeghiero. "Von Willebrand Disease." In Practical Hemostasis and Thrombosis, 73–87. Oxford, UK: Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9781444306286.ch8.

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Millar, Carolyn M. "Von Willebrand Disease." In Inherited Bleeding Disorders in Women 2e, 83–99. Chichester, UK: John Wiley & Sons, Ltd, 2018. http://dx.doi.org/10.1002/9781119426080.ch6.

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Castaman, Giancarlo, Alberto Tosetto, and Francesco Rodeghiero. "Von Willebrand Disease." In Practical Hemostasis and Thrombosis, 94–112. Chichester, UK: John Wiley & Sons, Ltd, 2016. http://dx.doi.org/10.1002/9781118344729.ch7.

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Taylor, Jason. "von Willebrand Disease." In Hemostasis and Thrombosis, 23–26. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-09312-3_5.

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Jesudas, Rohith. "von Willebrand Disease." In Benign Hematologic Disorders in Children, 233–45. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-49980-8_16.

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DeLoughery, Thomas G. "Von Willebrand Disease." In Hemostasis and Thrombosis, 33–38. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-19330-0_5.

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Dorgalaleh, Akbar, Shadi Tabibian, Yavar Shiravand, and Emmanuel J. Favaloro. "von Willebrand Disease." In Congenital Bleeding Disorders, 57–102. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-76723-9_3.

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Conference papers on the topic "Von Willebrand disease (vWD)"

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Wu, Q. Y., B. R. Bahnak, L. Coulombel, J. P. Caen, G. Pietu, and D. Meyer. "VON WILLEBRAND FACTOR mRNA IS SEVERELY REDUCED IN PIGS WITH HOMOZYGOUS VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644113.

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Porcine von Willebrand disease (vWD), an autosomal recessive disorder, is similar to some of the severe forms of vWD in humans and is characterized by a prolonged bleeding time and very low or undetectable amounts of von Willebrand factor (vWF) antigen and activity in plasma, platelets and endothelial cells. The molecular events that control the lack of expression of vWF in the vWD pigs is not known and could be at the transcriptional or post-transcriptional level. Lungs from normal and two homozygous vWD pigs were extracted immediately after harvesting of the animals and placed on dry ice. Tissues were homogenized in 6 M guanidinium thiocyanate and RNA isolated by centrifugation through cesium chloride. Total RNA was analyzed by Northern hybridization including dénaturation in glyoxal, electrophoresis in 1.0 % agarose-2.2 M formaldehyde gels and transfer onto nitrocellulose. Messenger RNA was detected with a nick-translated human vWF cDNA probe or a human actin control probe. The vWF probe, cloned from a human lung library, was 2,280 bp in length and spanned nucleotides 960 to 3,240 of the human cDNA. These human probes were considered valid to detect levels of porcine vWF and actin mRNA because they hybridized with restriction enzyme digested genomic DNA from normal and vWD pig leucocytes under conditions of high stringency. The size of the vWF mRNA in the normal pigs after Northern hybridization was approximately 9.0 kb, similar to that of human vWF mRNA, and was easily detectable at the lowest concentration of RNA blotted (5 ug). In contrast, vWF mRNA from vWD pigs was at the lower limit of detection even at 10 ug of total RNA blotted. Nevertheless, although at extremely low levels, vWF mRNA from vWD pigs appeared to be the same size as the normal mRNA. These results agree with observations on the relationship of vWF secreted from 24 hr. cultures of endothelial cells from the pulmonary artery of normal and vWD pigs where the vWF levels were 0.90 and 0.06 U/108 cells, respectively. Therefore, it appears that the very low expression of vWF in the vWD pigs is due to a lack of transcription of the vWF gene. At this time, however, turnover of unstable transcripts in the vWD pigs can not be ruled out.

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Gralnick, H., L. P. McKeown, S. Williams, and J. van Mourik. "PLATELET VON WILLEBRAND FACTOR-INDUCED SPONTANEOUS PLATELET AGGREGATION IN VON WILLEBRAND'S DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644095.

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We have previously described a form of von Willebrand's disease (vWd) with spontaneous aggregation induced by an abnormal plasma von Willebrand factor (vWf). We have studied the ability of these patient's platelet (P) lysate to induce P aggregation and compared the results with P lysates from other vWd patients.P were prepared from whole blood by centrifugation on an arabino-galactan gradient. The P yield varied from 86-93%. When 125I purified plasma vWf added to whole blood, it was not detectable in the isolated P preparation. The P were lysed by Triton X-100 and after freezing were used in the assays. We found that as little as 25 ul of P lysate (1 x 109 platelets/ml) induced SPA in normal platelet-rich plasma (PRP). Normal or other vWd did not induce PA when (1) a monoclonal antibody directed the fib-rinogen/vWf binding site on the GPIIb/IIIa was incubated with PRP; (2) when Glanzmann's thrombasthenic PRP was used or (3) when platelets were suspended in a fibrinogenemic plasma. The monoclonal antibodies, 10E5 and PLT-1 directed against the GPIIb/IIIa complex, totally inhibited the P-vWf induced platelet aggregation. SPA did not occur unless the plasma fibrinogen concentration was 40 mg/ml. The monoclonal antibody 6D1 (directed against the plasma vWf binding site on GPIb) only partically inhibited the P-vWf SPA. But an antibody directed against the plasma vWf-GPIb binding domain totally inhibited the SPA. We conclude that P-vWf has a domain similar to plasma vWf which binds to GPIb; however, the P-vWf binds to a site on the GPIb which is not identical to the plasma vWf binding site.

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Lillicrap, D., S. Windsor, Benford H. Hoogendorn, and A. R. Giles. "PLATELET VON WILLEBRAND FACTOR: STUDIES IN TYPE II VON WILLEBRAND′S DISEASE VARIANTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644108.

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Recent evidence suggests that platelet von Willebrand factor (vWf) plays an important role in maintenance of primary haemostasis. We have studied a normal population (N=24) and 15 patients with variant forms of von Willebrand's disease (vWd) to determine the utility of platelet vWf:Ag measurement in this disorder. Citrated blood was spun at 100 g for 10 mins at 20°C to prepare platelet rich plasma (PRP). The PRP was removed and platelet count and mean platelet volumes (MPV) were determined on a Coulter S+ counter. A platelet button was prepared by centrifugation of PRP at 3,500 g for 15 mins. Plasma supernatant was aspirated and replaced with 900 nl of DH^O. Platelets were lysed by 5 cycles of freeze/thawing and membrane debris pelleted by centrifugation at 13,000 g for 10 mins. Platelet lysate vWf:Ag was measured by a polyclonal anti-vWf ELISA. All platelet samples were tested at least twice. Bleeding times (BT), platelet sensitivity to ristocetin and other factor VIH/vWf parameters were measured by standard methods. vWf molecular weight profiles were assessed by crossed Immunoelectrophoresis and/or by multimer analysis. In 24 normal individuals, mean vWf:Ag was 31 u/109 platelets (7-68). The mean MPV for this group was 8.0 fl. No correlation was seen between MPV and vWf:Ag content. 15 vWd variant patients were studied. No platelet vWf:Ag was found in one type III patient. In two Type Ila patients mean platelet vWf:Ag was 57 u/109 pits. Patients with laboratory features of Type lib vWd showed two patterns of platelet vWf:Ag content. In two families (5 patients) the mean platelet vWf:Ag was only 24 u/109 pits. In this group the MPV was 9.42 fl. and the mean BT 8.75 mins. In the remaining seven Type IIb patients (4 families), the mean platelet vWf:Ag was 105 u/109 pits., MPV 9.1 fl. and mean BT 8 mins. These results in Type lib vWd suggest further heterogeneity within this disease subtype. The finding of a markedly elevated platelet vWf:Ag appears to identify one group of Type lib vWd patients.

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Berkowitz, S. D., H. Nozaki, K. Titani, T. Murachi, and T. S. Zimmerman. "CALPAIN AND ELASTASE ARE NOT RESPONSIBLE FOR THE VON WILLEBRAND FACTOR FRAGMENTS IN NORMAL PLASMA AND IIA VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644103.

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Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Using monoclonal epitope mapping, we have examined the proteolysis of the von Willebrand factor (vWF) subunit with platelet calcium activated neutral protease (CANP) and human leukocyte elastase and found that they are not responsible for the proteolytic cleavage sejen in normal individuals and IIA vWD. Previously we have shown that in vivo proteolysis of vWF is a normal event with a small but consistent proportion of plasma vWF being composed of 189, 176, and 140 kD fragments cleaved from the 225 kD subunit. In IIA vWD the proportion of cleaved vWF is increased. Because calcium activated neutral protease (CANP, calpain) and one or more enzymes released from polymorphonuclear leukocytes are known to proteolyze vWF in vitro with resultant loss of large multimers similar to that seen in IIA vWD, they have been suggested as being responsible for the proteolysis in vivo. We have now digested highly purified vWF with porcine CANP I and II and performed monoclonal epitope mapping on the resulting fragments. We found no difference in the size, location, and quantity of the fragments produced by calpain I versus calpain II. New fragments were detected of approximately 200, 170, 150, and 125 kD. There was no evidence for generation of the native fragments. Mapping of the 170 and 150 kD calpain-cleaved fragments revealed them to be from different parts of the molecule than the native 176 and 140 kD fragments. Digestion of vWF with human leukocyte elastase produced new fragments at 210/205, 190, 165, 145/140, and 130/125 kD. No generation of native fragments was detected. Monoclonal epitope mapping of the 190 and 145/140 kD elastase-cleaved bands proved that they come from opposite ends of the vWF molecule than the native 189 and 140 kD fragments, respectively. Therefore, CANP and human leukocyte elastase do not produce the proteolyzed fragments present in normal and IIA vWD and probably do not cause the loss of large multimers seen in that disorder.

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Johnsson, H., A. Silveira, L. Adamson, S. Schulman, and B. Hessel. "INDUCED ANTIBODIES TO VON WILLEBRAND FACTOR (VWF)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644112.

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Plasma from 11 patients have been investigated for the presence of antibodies to VWF using an immunoblot-ting system. Eight patients had severe haemophilia A and 3 had severe VW's disease (VWD). One haemophiliac had a high titer of neutralizing activity against VIII:C, and two had previously shown neutralizing activity against VIII:C. Neutralizing activity against ristocetin cofactor was demonstrated in only two of the VWD-patients. None of the VWD-patients did show antiactivity to VIII:C. All patients except 2 haemophiliacs had been transfused with factor concentrate within the last three weeks before blood sampling. Four different concentrates had been used.The following immunoblotting system was used: Highly purified VWF was applied to agarose gels, and electrophoresis performed. The proteins were blotted to nitrocellulose paper and the paper cut into strips. The strips were incubated with diluted plasma or the IgG-fraction of plasma (obtained by precipitation with ammoniumsulphate) from one or the other of the patients. Thereafter, the strips were treated with a second antibody (goat-anti human IgG) labeled with peroxidase before development with α-chloronaphtol. As a negativ control, normal plasma was used. As a positive control, a peroxidase labeled goat-antihuman VWF was used giving the known multimeric pattern of VWF-antigen.Antibodies to VWF were found in 4 haemophiliacs and in all 3 VWD-patients. The pattern of multimeric bands obtained with the antibodies showed differences in different patients. The in vivo t 1/2 of VIII:C concentrate did not seem to be affected by these antibodies to VWF.

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Takahashi, Hoyu, Wataru Tatewaki, Reizo Nagayama, Masaharu Hanano, Shin-ichiro Takizawa, and Akira Shibata. "HEAT-TREATED FACTOR VIII CONCENTRATES IN VON WILLEBRAND'S DISEASE AND RELATED DISORDERS: STUDIES IN PLATELET-TYPE VON WILLEBRAND'S DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644118.

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Cryoprecipitate has proved to correct the hemostatic defects in von Willebrand1s disease (vWd). However, recent studies have revealed that transmission of the AIDS retrovirus (HIV) occurs through exposure to blood products including cryoprecipitate. Treatment with heat-treated factor VIII concentrates may have certain advantages over treatment with non-heated products, if these preparations are efficacious in vWd and related disorders. We investigated the multimeric compositoin of von Willebrand factor (vWf), contents of vWf antigen (vWf:Ag) and ristocetin cofactor activity (RCof) in the heat-treated factor VIII concentrates and cryoprecipitate, and their capacity to directly induce aggregation of platelet-type (or pseudo-) vWd platelets in vitro. The vWf multimers were visualized by a newly developed, immuno-enzymatic staining of the gel, following a discontinuous SDS-agarose gel electrophoresis. The RCof/vWf:Ag ratio was around 1.0 in cryoprecipitate, and ranged from 0.19 to 0.96 in factor VIII concentrates. Among four commercially available concentrates studied, Haemate P contained the most high-molecular-weight multimers of vWf and the highest RCof relative to vWf:Ag, and induced the aggregation of platelet-type vWd platelets at the lowest concentration. When infused into a patient with platelet-type vWd, Haemate P (144 units vWf:Ag/kg body weight) shortened the prolonged bleeding time and caused spontaneous platelet aggregation in vitro with a mild diminution of platelet count (from the preinfusion value of 183,000μl to 139,000μl at 5 minutes). These results indicate that some of the heat-treated factor VIII concentrates contain the high-molecular-weight vWf multimers and may provide a safer, yet still effective, treatment for platelet-type vWd, and possibly for various types of vWd as well.

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Standen, G., P. Moodie, H. Pannekoek, C. L. Verweij, and I. R. Peake. "ANALYSIS OF THE VON WILLEBRAND FACTOR (vWF) GENE IN 6 PATIENTS WITH SEVERE TYPE III VON WILLEBRANDS DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644641.

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DNA from 6 unrelated patients with severe type III von Willebrands disease (vWF antigen < 0.01u/dl) was studied with a cDNA probe for the 3' end of the vWF gene. DNA was extracted from peripheral blood leucocytes using standard techniques and was digested with a range of restriction enzymes. DNA fragments were separated by electrophoresis in 0.7% agarose and were southern blotted onto hybond-N (Amersham). The probe used was pvWF1100, a 1.1kb PstI fragment derived from the 2.28kb vWFcDNA insert of pvWF2280 isolated from a human endothelial cell cDNA expression library (Verweij et al, Nucleic Acids Res 13 (1985) 4699-4717). The probe corresponds to nucleotides 7083 to 8191 of the vWF cDNA (first nucleotide of initiator methionine as 1).When digested with Bglll and probed with pvWF11000, normal DNA showed two invariant bands (13 and 4.9kb) and polymorphic bands of 9 and/or 7.4kb. This pattern was also seen in 5 of the 6 severe vWD patients DNA suggesting that in this 3' area of the gene they had no major deletions or rearrangements. In the 6th case however the band of 4.9kb was not seen and did not appear to be replaced by any novel fragments, suggesting a partial deletion including some of the 3' end of the gene. This patient had the clinically severest form of the condition in that the patient had developed, some 10 years ago, an antibody (inhibitor) to vWF as detected by the ability of the patients plasma to inhibit restocetin cofactor activity in normal plasma. His parents were related (his mother was his father's second cousin) and had levels of vWFAg, considerably lower than those of factor VIII activity. This situation has been previously reported in carriers of recessive severe vWD. vWD was also present in a second family member, but in a less severe form (vWFAg 3u/dl). This patient and all other members of the family have, to date, given normal restriction fragment patterns with the vWF probe and several enzymes, including BgIII.

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Mannucci, P. M., M. Moia, D. Altieri, J. Monteagudo, and R. Castillo. "BLEEDING TIME IN TREATED PATIENTS WITH SEVERE VON WILLEBRAND DISEASE IS NOT CORRECTED ONLY BY GIVING NORMAL MULTIMERIC PLASMA VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644117.

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Even though it is generally held that cryoprecipitate (cryo) and fraction I-0 correct the prolonged bleeding time (BT) in patients with von Willebrand disease (VWD), perusal of reported data indicates that the correction is usually short lasting and often partial. We decided to do a controlled study of the relationship between the multimeric structure of von Willebrand factor (VWF) in 5 patients with severe VWD after infusion of three plasma concentrates : "wet" cryo, lyophilized (lyo) cryo, and fraction 1-0 given in random order. The dosage of concentrates was tailored to achieve post infusion levels of RiCof above the lower normal limit (50 U/dL) for at least 3 hours. The post-infusion BT values are shown in the table.These findings indicate that the attainment of a normal BT is the exception rather than the rule after infusion of three plasma fractions used for treatment of severe VWD. In all the concentrates the proportions of large VWF multimers, calculated by scanning the electrophoretic gels, were the same as in normal standard plasmas. An intact multimeric structure was recovered in post-infusion plasma of patients treated with wet cryo, whereas there was post infusion loss of large multimers after lyo and fraction I-O. In conclusion, an intact multimeric structure in post infusion plasmas is necessary but not sufficient to sustain a normal BT in VWD patients.

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Ngo, K. Y., D. Lynch, J. Gitscher, N. Ciavarella, Z. Ruggeri, and T. Zimmerman. "HOMOZYGOUS AND HETEROZYGOUS COMPLETE DELETIONS OF THE VON WILLEBRAND FACTOR GENE CODING REGION IN SEVERE VON WILLEBRAND DISEASE AND CARRIERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643931.

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Severe von Willebrand disease (vWD) is characterized by undetectable levels of von Willebrand factor (vWF), or trace amounts, in plasma and tissue stores. We have studied the genomic DNA of ten affected individuals from five families with this disorder using two cDNA probes. One probe extended from 175 base pairs of the 5’ untranslated region to the nucleotides encoding amino acid 618 of pro-vWF; the second extended from the nucleotides encoding amino acid 2225 of pro-vWF to 100 bp into the 3’ untranslated region. Three variants of the disorder were identified. Southern blots of restriction endonuclease digests and slot blots of undigested genomic DNA showed complete homozygous deletion of the vWF gene coding region in four affected siblings, three of whom had developed allo-antibodies. Gene dosage analysis performed with slot blots and laser densitometry were consistent with complete heterozygous deletions in both parents. The second variant was characterized by a complete heterozygous deletion of the vWF gene coding region in the propositus and one asymptomatic parent, suggesting that a different type of genetic abnormality was inherited from the other parent and that the patient was doubly heterozygous for distinct genetic abnormalities affecting vWF. In a third variant, no abnormalities could be detected. These techniques should prove useful in identifying carriers of severe vWD and also defining patients at risk of developing allo-antibodies to vWF.

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Verweij, C. L., R. Quadt, E. Briët, and H. Pannekoek. "TWO VON WILLEBRAND FACTOR (vWF) GENE POLYMORPHISMS SEGREGATE WITH VON WILLEBRAND'S DISEASE (vWD) TYPE IIA: ASSIGNMENT OF THE DEFECTIVE GENE LOCUS IN vWD TYPE IIA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644646.

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Patients with autosomal, dominant von Willebrand's disease (vWD) type IIA display a decreasedristocetin cofactor activity and lack the large and intermediate size von Willebrand factor (vWF) multimers. As yet the cause for this abnormal vWF protein is not known. In this study we determined whether vWD type IIA is due to a mutation in the vWF gene or by a defect in another gene involved, in for example, vWF processing.Restriction fragment-length polymorphisms (RFLP's), using the enzymes BgIII and XbaI in conjunction with human vWF cDNA probes, have been described. Restriction endonuclease analysis of genomic vWF DNA revealed that these genetic marker are located within the vWF gene. The vWF gene was determined to comprise about 160 kb and harbors at least 20 exons. The RFLP's were applied to study the segregation of alleles associated withvWD type IIA in a comprehensive, affected family. It is demonstrated that both RFLP's are completely linked with the vWD type-IIA trait. From this finding, we conclude that the defect, causing the vWD type IIA, is most likely due to a mutation in the vWF gene and not to a mutation in another gene involved in, for example, post-translational processing of the vWF protein.

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