A qualitative and quantitative analysis of von Willebrand factor contained in a very high‐purity plasma‐derived FVIII concentrate

Samor, Bruno; Michalski, Catherine; Brandin, M.-P.; André, M.; Chtourou, Sami; Tellier, Z.

doi:10.1111/j.1423-0410.2011.01576.x

Cited by 3 publications

(2 citation statements)

References 42 publications

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Section: Introductionmentioning

confidence: 99%

“…In order to evaluate their clinical efficacy, many previous studies have compared the VWF content of commercially available concentrates in terms of the standard laboratory measure of activity such as ristocetin cofactor activity (VWF:RCo) and collagen binding activity (VWF:CB) performed under static conditions, as well as VWF multimer distribution. [10][11][12][13][14][15] However, relatively few studies have addressed the functionality of these concentrates in terms of their ability to mediate platelet adhesion to collagen surfaces under physiological shear conditions. 16 In this study we have assessed the effect of ten commercially available VWF containing concentrates on platelet adhesion to collagen under shear stress using an in vitro assay.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Evaluation of von Willebrand factor concentrates by platelet adhesion to collagen using an in vitro flow assay

Riddell

Vinayagam

Gomez

et al. 2019

Research and Practice in Thrombosis and Haemostasis

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BackgroundVon Willebrand disease (VWD) results from quantitative or qualitative deficiency of von Willebrand factor (VWF) and is treated using VWF‐containing concentrates. Several studies have compared the function of various VWF containing concentrates however this has not been performed using shear based assays.ObjectivesTo compare the platelet‐capture potential of 10 commercially available, plasma‐derived VWF concentrates under shear conditions.Methods VWF containing concentrates were assessed for VWF:Ag, VWF:CB, VWF:RCo, factor VIII:C ADAMTS13 content, VWF multimeric profile and glycan content using lectin binding assays. Free‐thiol content of each concentrate was investigated using MPB binding assays. An in vitro flow assay was used to determine the ability of each concentrate to mediate platelet capture to collagen.Results VWF multimeric analysis revealed reduction of high molecular weight (HMW) forms in four of the concentrates (Alphante, Octanate and Haemoctin, and 8Y). The high MW multimer distribution of the remaining six concentrates (Optivate, Wilate, Fandhi, Wilfactin, Haemate P, and Voncento) was similar to the plasma control. Lectin analysis demonstrated that 8Y had increased amount of T‐antigen. Although platelet capture after 5 minutes perfusion was similar for all concentrates; Alphante, Octanate, and Haemoctin, demonstrated the lowest levels of platelet capture after 60 seconds of perfusion. Free‐thiol content and ADAMTS13 levels varied widely between the concentrates but was not correlated with function.ConclusionAlphanate, Octanate, and Haemoctin, lacked HMW multimers and had the lowest initial platelet capture levels suggesting that the presence of VWF HMW multimers are required for initial platelet deposition.

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Section: Introductionmentioning

confidence: 99%