Intraplatelet von willebrand factor and ABO blood group

Sweeney, Joseph D.; Hoernig, Lynne A.

doi:10.1016/0049-3848(92)90097-t

Cited by 18 publications

(13 citation statements)

References 13 publications

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“…Therefore, it is possible that the AC resulted in increased hepatic flow and clearance of vWf:Ag. Additionally, ABO blood type has been associated with plasma vWf:Ag (Sweeney and Hoernig 1992) which may have contributed to the differences observed among subjects. However, blood type of the subjects in the present study was not assessed.…”

Section: Discussionmentioning

confidence: 91%

Changes in von Willebrand factor and fibrinolysis following a post-exercise cool-down

et al. 2004

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The purpose of this study was to determine the effect of a post-exercise active cool-down on von Willebrand factor and fibrinolysis. Ten subjects performed two maximal oxygen uptake (VO2max) tests followed by a 10-min passive (PC) or an active (AC) cool-down. Blood samples were obtained pre-exercise, post-exercise, post-PC/AC, and 1 h post-exercise and analyzed for von Willebrand factor antigen (vWf:Ag), tissue plasminogen activator (tPA) antigen and activity and plasminogen activator inhibitor-1 (PAI-1) activity. Data were analyzed using repeated measures analysis of variance. No significant differences were found between VO2max tests for treadmill time, VO2max, respiratory exchange ratio, maximal heart rate, or maximal blood lactate concentration. vWf:Ag was significantly elevated (P <0.05)following PC [198.4 (18.3)% normal] versus AC [174.5 (15.6)% normal] and remained elevated 1-h post-exercise [179.4 (16.4)% normal for PC vs 158.6 (13.8)% normal for AC]. There were no differences between tests for tPA or PAI-1 activity, although tPA antigen was significantly elevated following PC versus AC (P <0.05). Following the cool-down, hematocrit was higher (P <0.05) for the PC test [48.90 (0.36)] compared with AC [47.43 (0.51)]. An AC reduces post-exercise vWf:Ag and tPA antigen without affecting tPA or PAI-1 activity.

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Section: Discussionmentioning

confidence: 91%

Changes in von Willebrand factor and fibrinolysis following a post-exercise cool-down

et al. 2004

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“…Platelet VWF has been found to be less effective than plasma VWF in supporting platelet agglutination, despite its particularly large multimeric composition (Williams et al , 1994). Sweeney & Hoernig (1992) reported that platelet VWF does not contain AB antigens. Our studies confirm the absence of AB antigens on platelet VWF.…”

Section: Discussionmentioning

confidence: 99%

Role of A and B blood group antigens in the expression of adhesive activity of von Willebrand factor

et al. 2000

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Summary. ABO (H) blood group antigens are covalently linked to the oligosaccharide side-chains of von Willebrand factor (VWF). In this study, we investigated the role of the A and B antigens in the expression of VWF adhesive activity. VWF of type A, B or O was purified from fresh frozen plasma. Presence of A or B antigen on the VWF was confirmed by enzyme-linked immunosorbent assay (ELISA) and by immunoblotting with monoclonal anti-A or anti-B. The A or B antigen was also detected in the 48/52-kDa fragment of the respective VWF after trypsin digestion. Removal of A antigen with a-N-acetylgalactosaminidase or B antigen with a-galactosidase did not affect its multimer size or antigenic level, but decreased the ristocetin cofactor (RCoF) activity of the respective VWF by 33±39% (P , 0´01±0´002). Removal of A or B antigen from VWF did not affect the binding of the VWF to immobilized type III collagen. A and B antigens were not detected in platelet VWF. These results indicate that AB structures play a role in platelet aggregating activity of VWF.

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“…10 Platelet VWF content is currently seen as a marker of VWF synthesis, so finding that different ABO blood groups have a similar platelet VWF content ruled out the possibility that the ABO determinant could affect VWF synthesis. 20 Starting from the finding that ABO structures exist on the N-linked oligosaccharide chains associated with VWF and bearing in mind that glycosylation may influence the rate of clearance of proteins like erythropoietin and interferon, mediated by a specific hepatic asialoglycoprotein receptor, 35 we worked on the assumption that ABO blood groups might influence VWF half-life. We tested our hypothesis by analyzing the time course of VWF plasma concentrations in healthy volunteers, following the administration of DDAVP, a vasopressin analog capable of inducing the release of VWF from endothelial cell storage sites.…”

Section: Discussionmentioning

confidence: 99%

A shorter von Willebrand factor survival in O blood group subjects explains how ABO determinants influence plasma von Willebrand factor

Gallinaro

Cattini

Sztukowska

et al. 2008

Blood

260

240

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IntroductionPlatelet plug formation at the site of vascular injury is initiated by von Willebrand factor (VWF) interacting with the subendothelial matrix, followed by its binding to platelet glycoprotein (GP) Ib 1,2 and subsequent platelet activation and aggregation. VWF is synthesized by endothelial cells and megakaryocytes, 3,4 and one of its main particular features is a polymer structure ranging in size from 500 000 to more than 20 million Dalton, 5 the largest forms being hemostatically the most efficient. 6 A broad range of values characterizes plasma VWF levels, which average around 10 g/mL. Acquired and inherited factors both modulate plasma VWF levels, and twin studies have demonstrated that 66% of all variations in plasma VWF are genetically determined, while 30% of them depend on ABO blood group, 7 O blood group individuals having plasma VWF levels 25% lower than non-O subjects. 8 ABO group genotyping shows that O 1 O 1 subjects have the lowest VWF levels, and non-O group individuals heterozygous for the O 1 allele have significantly lower VWF levels than AA, AB, or BB subjects. 9,10 Glycosylation accounts for 19% of VWF by weight, and ABO determinants identified on the N-linked oligosaccharide chains are part of this glycosylation process. 11,12 ABO groups are added to the N-linked glycan chains of VWF in the post-Golgi compartment of endothelial cells before VWF secretion, albeit with the variable contribution of the endothelial cells from different vascular beds. 13 The carbohydrate moiety plays an important part in VWF polymerization and function, 14 and also affects the liver-mediated clearance of VWF. In animal models, the removal of sialic acid has been shown to induce an increase in VWF clearance, 15 and the half-life of VWF is halved in mice characterized by an aberrantly glycosylated VWF (due to the absence of the enzyme ST3Gal-IV). 16 Moreover, recombinant VWF, lacking in carbohydrate, is cleared from the circulation faster than its glycosylated counterpart, 16 and posttranslational changes in VWF induced by Galgt2, aberrantly expressed in endothelial cells, lead to a 20-fold increase in VWF clearance. 17 ABO group determinants may also regulate the susceptibility of VWF to the proteolytic action of ADAMTS13, proteolysis being faster in the case of the O blood group. 18 A different susceptibility to cleavage by ADAMTS13 may thus be one of the ways in which ABO group affects VWF removal from the circulation and consequent VWF levels.Although the mechanisms behind ABO blood group and VWF levels have yet to be fully clarified, it has been clearly demonstrated that the effects are mediated by the ABO antigen structures on the N-linked oligosaccharide chains of circulating VWF, and particularly by H antigen expression. 19 Understanding these mechanisms is of clinical relevance: non-O individuals have been shown to carry a significantly greater risk of venous thromboembolism, ischemic heart disease, and peripheral vascular disease, 21-23 while the O blood group is much more common in von Willebra...

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Intraplatelet von willebrand factor and ABO blood group

Cited by 18 publications

References 13 publications

Changes in von Willebrand factor and fibrinolysis following a post-exercise cool-down

Changes in von Willebrand factor and fibrinolysis following a post-exercise cool-down

Role of A and B blood group antigens in the expression of adhesive activity of von Willebrand factor

A shorter von Willebrand factor survival in O blood group subjects explains how ABO determinants influence plasma von Willebrand factor

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