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            Antigen Expressed on Circulating von Willebrand Factor Is Modified by ABO Blood Group Genotype and Is a Major Determinant of Plasma von Willebrand Factor Antigen Levels

O’Donnell, James S.; Boulton, Frank; Manning, Richard A.; Laffan, Michael

doi:10.1161/hq0202.103997

Cited by 128 publications

(158 citation statements)

References 35 publications

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“…These results favor the hypothesis that the expression of H antigen on VWF is one of the most important determinants of circulating levels of VWF:Ag. 8 In conclusion, we demonstrated that the circulating levels of VWF:Ag and FVIII in subjects with rare subgroups were similar to those found in group O individuals. These data could contribute to the diagnosis of von Willebrand's disease and to the evaluation of thrombophilia in individuals with different ABO subgroups.…”

Section: Resultssupporting

confidence: 73%

The relationship between ABO groups and subgroups, factor VIII and von Willebrand factor

Sousa¹,

Anicchino-Bizzacchi²,

Locatelli³

et al. 2007

Haematologica

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Section: Resultssupporting

confidence: 73%

The relationship between ABO groups and subgroups, factor VIII and von Willebrand factor

Sousa¹,

Anicchino-Bizzacchi²,

Locatelli³

et al. 2007

Haematologica

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“…The A and B alleles of the ABO locus encode A and B glycosyltransferase activities, which convert precursor H antigen into either A or B determinants, the A and B antigens having an extra saccharide unit to the O unit (N-acetylgalactosamine and galactose, respectively). Group O individuals lack such transferase enzymes (loss of function) and express basic, unchanged H-antigen (7,8).…”

Section: Introductionmentioning

confidence: 99%

Relation of ABO blood groups to coronary lesion complexity in patients with stable coronary artery disease: an observational study

Kaya¹,

Tanboğa²,

Kurt³

et al. 2013

Anadolu Kardiyol Derg

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Objective: We aimed to investigate the relationship between ABO blood groups and complexity of coronary lesions assessed by SYNTAX score (SS) in stable coronary artery disease (CAD) patients. Methods: Our cross-sectional and observational study population consisted of 559 stable CAD patients. From all patients, ABO blood group was determined and the SS was calculated as low SYNTAX score (0-22), intermediate SYNTAX (23-32) score and high SYNTAX score (>32). Statistical analysis was performed using Student's t-test or Mann-Whitney U test, ANOVA, or Kruskal-Wallis test and chi-square test. Multiple logistic regression analysis was used to identify the independent predictors of high SS. Results: The analysis between the SS tertiles revealed that the frequency of non-O blood group was significantly higher in the upper SS tertiles (56.2% vs. 75.9 vs. 80.2%, p<0.05). However, the frequencies of Rh types were similar in all tertiles. Multiple logistic regression analysis was applied for determining the predictors of high SS. Accordingly, non-O blood group (OR: 2.68, 95% CI 1.65-4.35, p<0.001), LV-EF (OR: 0.93, 95% CI 0.91-0.95, p<0.001), LDL(OR: 0.98, p<0.001), and e-GFR (OR: 0.99, 95% CI 0.98-0.98, p<0.001) were found to be the independent predictors of high SS. Conclusion: We showed that there were significant associations between ABO blood groups and complexity of angiographic CAD.

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“…VWF concentration in each fraction was determined using a specific VWF enzyme-linked immunosorbent assay (ELISA), as previously described. 22 The purity of VWF was assessed by reducing SDS-PAGE and silver staining. …”

mentioning

confidence: 99%

Proteolytic inactivation of ADAMTS13 by thrombin and plasmin

Crawley

Lam

Rance

et al. 2005

Blood

212

193

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The multimeric size and the function of circulating von Willebrand factor are modulated via its proteolytic cleavage by the plasma metalloproteinase, AD-AMTS13. It is unclear how ADAMTS13 activity is regulated within the vascular system. In the absence of a regulatory mechanism, ADAMTS13 activity might compromise platelet adhesion at sites of vascular injury. We hypothesized that at sites of vascular injury, ADAMTS13 activity could be regulated locally by coagulation proteinases. Initiation of coagulation in human plasma resulted in the disappearance of added full-length recombinant ADAMTS13. This loss was inhibited by hirudin. Using purified proteins, we showed that ADAMTS13 is proteolyzed at several cleavage sites by thrombin in a time-and concentration-dependent manner. Furthermore, this proteolysis ablated ADAMTS13 activity against purified von Willebrand factor. Preincubation of thrombin with soluble thrombomodulin, but not heparin, inhibited the proteolysis of AD-AMTS13, suggesting the involvement of IntroductionVon Willebrand factor (VWF) is a large (2050 amino acid/ϳ250 kDa) multidomain glycoprotein whose functions are critical for normal hemostasis. 1 VWF has 2 principal roles that influence the hemostatic process: (1) it acts as a carrier protein for coagulation factor VIII 2 and (2) it mediates rapid adhesion of platelets to sites of vascular perturbation. The latter is one of the first hemostatic events following endothelial disruption and occurs through the specific binding of VWF to exposed subendothelial matrix proteins (principally collagen). 3 Once immobilized, VWF affinity for the glycoprotein (GP) Ib-IX-V receptor complex on the surface of circulating platelets is significantly enhanced. 4 This results in the tethering of platelets at sites of vascular damage and in the formation of a primary platelet plug. Tethered platelets are subsequently activated and expose phosphatidylserine-rich surfaces that are critical for efficient thrombin generation to occur. 5 VWF is constitutively secreted into the blood by endothelial cells as multimers of varying size that differ predominantly in the number of component VWF units. A significant proportion is also stored within Weibel-Palade bodies, predominantly as "ultra-large" multimers (UL-VWF) 6 that may exceed 2 ϫ 10 4 kDa. 1 This pool is released on demand in response to endothelial cell activation. 7 The properties of circulating VWF are, in part, dependent on its molecular size. Larger VWF multimers not only bind circulating platelets more readily than smaller forms, but also undergo marked conformational changes in response to the rheologic forces exerted by the circulating blood. 8 Under normal flowing conditions, VWF multimers circulate in a globular form. However, when VWF is exposed to increased shear forces, these molecules unravel into a "stringlike" conformation. This increases the number of exposed platelet/matrix binding sites and thus enhances the platelet tethering potential of the VWF molecule.Thrombotic thrombocytopenic purpura (TTP) is...

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Amount of H Antigen Expressed on Circulating von Willebrand Factor Is Modified by ABO Blood Group Genotype and Is a Major Determinant of Plasma von Willebrand Factor Antigen Levels

Cited by 128 publications

References 35 publications

The relationship between ABO groups and subgroups, factor VIII and von Willebrand factor

The relationship between ABO groups and subgroups, factor VIII and von Willebrand factor

Relation of ABO blood groups to coronary lesion complexity in patients with stable coronary artery disease: an observational study

Proteolytic inactivation of ADAMTS13 by thrombin and plasmin

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