VWF propeptide and ratios between VWF, VWF propeptide, and FVIII in the characterization of type 1 von Willebrand disease

Eikenboom, Jeroen; Federici, Augusto B.; Dirven, Richard; Castaman, Giancarlo; Rodeghiero, Francesco; Budde, Ulrich; Schneppenheim, Reinhard; Batlle, J.; Canciani, Maria Teresa; Goudemand, Jenny; Peake, I. R.; Goodeve, Anne

doi:10.1182/blood-2012-09-455089

Cited by 95 publications

(136 citation statements)

References 23 publications

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“…Figure 1A). This is in accordance with previously published data by Eikenboom et al 12 In type 2 patients, median VWFpp was 104 U/dL ( IQR, 81 to 136 U/dL), which was higher than that in type 1 patients (P , .001). Median VWFpp/VWF:Ag ratio was 4.5 (IQR, 3.2 to 6.0), and median FVIII:C/VWF:Ag ratio was 1.6 (IQR, 1.2 to 2.0) in the type 2 patients.…”

Section: Resultssupporting

confidence: 82%

“…The normal range (2.5th to 97.5th percentile) used for VWFpp was 82 to 173 U/dL, for the VWFpp/VWF:Ag ratio 0.8 to 2.2, and for the FVIII: C/VWF:Ag ratio 0.6 to 1.9, as previously reported by Eikenboom et al 12 …”

Section: Definitionsmentioning

confidence: 67%

“…19 VWFpp was measured centrally at the Leiden University Medical Center (Leiden, The Netherlands). This assay was also used in the previous report by Eikenboom et al 12 and was measured at the same center. VWFpp antigen was determined with an enzyme-linked immunoassay by using antibodies from Sanquin (Amsterdam, The Netherlands) as described.…”

Section: Laboratory Measurementsmentioning

confidence: 99%

“…11 Low VWF levels are caused by reduced VWF synthesis or secretion, increased VWF clearance, or a combination thereof. Recently, Eikenboom et al 12 have shown that the VWFpp/VWF:Ag and FVIII:C/VWF:Ag ratios represent the pathophysiology of VWD and correspond to different There is an Inside Blood Commentary on this article in this issue.…”

Section: Introductionmentioning

confidence: 99%

“…VWFpp antigen was determined with an enzyme-linked immunoassay by using antibodies from Sanquin (Amsterdam, The Netherlands) as described. 7,12 First, microtiter plates were coated with antibody CLB-Pro 35 overnight at 4°C and then blocked with 1% bovine serum albumin at room temperature for 2 hours. Next, the diluted samples were incubated for 2 hours at 37°C.…”

Section: Laboratory Measurementsmentioning

confidence: 99%

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von Willebrand factor propeptide and the phenotypic classification of von Willebrand disease

Sanders

Groeneveld

Meijer

et al. 2015

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Section: Resultssupporting

confidence: 82%

Section: Definitionsmentioning

confidence: 67%

Section: Laboratory Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Laboratory Measurementsmentioning

confidence: 99%

See 3 more Smart Citations

von Willebrand factor propeptide and the phenotypic classification of von Willebrand disease

Sanders

Groeneveld

Meijer

et al. 2015

Blood

Self Cite

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show abstract

Von Willebrand Disease

Castaman

Tosetto

Rodeghiero

2016

Practical Hemostasis and Thrombosis

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Von Willebrand disease type Vicenza: In search of a classification for the archetype of reduced von Willebrand factor survival

Casonato

Galletta

Galvanin

et al. 2021

eJHaem

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Type Vicenza von Willebrand disease (VWD) features a von Willebrand factor (VWF) with a very short half‐life, and is classified as a form of type 1 VWD. To test the appropriateness of type Vicenza VWD classification, the main features of 17 patients from eight unrelated families were analysed. They had low VWF antigen levels and function (always below 20 U/dl); ristocetin‐induced platelet aggregation sometimes normal, sometimes reduced/absent (even in the same patient); normal platelet VWF levels; an increased VWF propeptide to VWF antigen ratio (8.74 ± 1.65 vs. normal 1.04 ± 0.28) and a reduced VWF half‐life. Plasma VWF multimer levels were homogeneously reduced, and unusually large VWF multimers were sometimes present. Recombinant p.R1205H VWF showed a normal synthesis, release, function, and multimer pattern, with no ultra‐large VWF multimers. The mathematical model by Galvanin et al. was used to explore the kinetic changes in VWF after DDAVP. It showed that the release, but especially the proteolysis (kproteol 1.0−3 ± 2.5−3 vs. normal 4.5−4 ± 6.4−4) and elimination (kel 1.0−2 ± 5.2−3 vs. normal 1.1−3 ± 6.8−4) of type Vicenza VWF were significantly higher than normal. The increased elimination is consistent with the short half‐life, while the increased proteolysis was unexpected. As a shorter survival of VWF is wholly responsible for the type Vicenza VWD phenotype (VWF synthesis, structure and function are normal), it might be better to classify it as a type 2 VWD (rather than type 1) to emphasise the greater interaction with clearance receptors as a new VWF functional defect.

show abstract

VWF propeptide and ratios between VWF, VWF propeptide, and FVIII in the characterization of type 1 von Willebrand disease

Abstract: Key Points VWFpp/VWF:Ag and FVIII:C/VWF:Ag ratios define the pathophysiological mechanisms that play a role in VWD and various VWF mutations. A high VWFpp/VWF:Ag ratio indicates increased clearance of VWF and a high FVIII:C/VWF:Ag ratio decreased synthesis of VWF.

Cited by 95 publications

References 23 publications

von Willebrand factor propeptide and the phenotypic classification of von Willebrand disease

von Willebrand factor propeptide and the phenotypic classification of von Willebrand disease

Von Willebrand Disease

Von Willebrand disease type Vicenza: In search of a classification for the archetype of reduced von Willebrand factor survival

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