Studies on factor VIII-related protein IV. Interaction of galactose-specific lectins with human factor VIII/von willebrand factor

Furlan, Miha; Perret, Beat A.; Beck, Eugene A.

doi:10.1016/0005-2795(80)90269-x

Cited by 5 publications

(4 citation statements)

References 18 publications

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“…All these data raise the possibility that galactose is essential for the maintenance of a normal multimeric structure. Such an hypothesis has already been suggested by Gralnick et al (13) and the possible relationships between the galactose content and the molecular weight of polymers of FVIII/vWF has also been reported by other investigators working on the reactivity of FVIII/ vWF protein with galactose-specific lectins (29,30). As the ristocetin-mediated binding of FVIII/vWF to platelets has been shown to be preferentially associated with the larger molecular weight polymers (31,32), the defect of ristocetin-mediated binding occurring after galactose removal might be a consequence of the alteration of the multimeric structure although it might be due also to the absence of galactose per se.…”

Section: Discussionsupporting

confidence: 57%

Effect of Carbohydrate Modifications of Factor VIII/ von Willebrand Factor on Binding to Platelets

Goudemand¹,

Mazurier²,

Samor³

et al. 1985

Thromb Haemost

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SummaryThis study compares the ability of unmodified and carbohydrate-modified forms of factor VIII/von Willebrand factor (FVIII/vWF) protein to bind to platelets in the presence of ristocetin or thrombin. Treatment of intact FVIII/vWF with α-D- neuraminidase results in more than 95% desialylation. Asialo FVIII/vWF retains total activity in ristocetin- and thrombin- mediated binding to platelets as demonstrated by direct and competitive binding assays. Examination of its multimeric pattern by sodium dodecyl sulfate-agarose electrophoresis reveals a normal multimeric structure. Treatment of intact FVIII/vWF with β-D-galactosidase results in the removal of 20% of galactose (agalacto FVIII/vWF) whereas 55% of galactose is released from asialo FVIII/vWF (asialo agalacto FVIII/vWF). Agalacto and asialo-agalacto FVIII/vWF are both unable to bind to platelets in the presence of ristocetin. In contrast, they still bind to thrombin- stimulated human (except thrombasthenic) platelets. Removal of either ultimate (agalacto FVIII/vWF) or ultimate and penultimate (asialo-agalacto FVIII/vWF) galactose results in the same loss of the larger molecular weight multimers and in an increase of smaller multimers. These results suggest (1) that sialic acid does not play a significant role in ristocetin- or thrombin-mediated FVIII/vWF-platelets interactions and multimeric structure of FVIII/vWF (2) that ultimate β-linked galactose residues are essential for the maintenance of a normal multimer organization (3) that ristocetin- and thrombin-mediated binding of FVIII/vWF to platelets differ in FVIII/vWF galactose requirement.

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Section: Discussionsupporting

confidence: 57%

Effect of Carbohydrate Modifications of Factor VIII/ von Willebrand Factor on Binding to Platelets

Goudemand¹,

Mazurier²,

Samor³

et al. 1985

Thromb Haemost

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“…Another possibility may be that each subunit composing the larger multimers contains more galactose residues than the subunit of the smaller ones. Furlan's report (22) suggests that the number of galactose residues accessible to RCA per subunit is higher in normal larger multimers than in the smaller ones. Gralnick et al (19) showed that the oligomers from a patient with the variant form of vWd had a low content of sugars.…”

Section: Discussionmentioning

confidence: 99%

“…Furlan et al (22) demonstrated that the larger multimers of normal FVIIIIvWF protein showed a high affinity for RCA when the reduced protein was electrophoresed through SDS polyacrylamide gel and fluorescein-labelled RCA reacted with them. By the use of SDS PAGE -CIE for determining the molecular size of VIIIR: Ag in the crude sample (9), we developed the combined method of SDS PAGE -CIE and the above-mentioned RCA -CIE in order to follow the changes of immunoprecipitin patterns by RCA, especially the changes of molecular size.…”

Section: Discussionmentioning

confidence: 99%

Heterogeneity of Sugar Composition of Factor VIII/ von Willebrand Factor in von Willebrand's Disease: Analysis by Crossed Affinoimmunoelectrophoresis Using Lectin (Ricinus communis Agglutinin-120)

et al. 1983

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SummaryThe nature of sugar chain of factor VTII/von Willebrand factor in plasma of normal subjects and patients with von Willebrand’s disease (vWd) was examined by crossed affinoimmunoelectrophoresis using anti-human factor VIII rabbit serum, with inserted Ricinus communis agglutinin-120 (RCA-120) agarose layer (RCA – CIE). Molecular weights of factor VlU-related antigen (VIIIR: Ag) were estimated by SDS polyacrylamide gel electrophoresis — crossed affinoimmunoelectrophoresis (SDS PAGE – RCA – CIE).VIIIR :Ag, in normal plasma and in classical form of vWd, showed two precipitin peaks on RCA – CIE. The slower moving component of VIIIR :Ag with molecular weights over 3×106 daltons from normal subjects and patients with classical form of vWd showed a high affinity for RCA-120. The faster moving component of VIIIR: Ag below 3×106 daltons from the abovementioned subjects and patients with a variant form (Type IIA) showed a very weak affinity for RCA-120.These results suggested that all of VIIIR: Ag in these variant cases may have a deficiency of galactose residues reactive with RCA, in addition to an incomplete polymerization of VIIIR: Ag, similar to that of the faster moving component of normal subjects.

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“…Previous studies from our laboratory (15) indicated that the galactose-specific lectins preferentially bind to subunits derived from HMW factor VIII. However, the VIII: Rcof activity of LMW factor VIII was considerably less than expected from the relative reactivity of galactose residues with lectins.…”

Section: Lntrodustionmentioning

confidence: 85%

Von Willebrand Activity of Low Molecular Weight Human Factor VIII Increases by Binding to Gold Granules

1981

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SummaryHuman factor VIII/von Willebrand protein is a population of multimers which vary in size but contain apparently identical subunits. Large-molecular-weight forms possess higher ristocetin cofactor/von Willebrand activity than the native smaller oligomers. Disulfide reduction of large factor VIII multimers results in progressively decreasing molecular size and a loss of ristocetin cofactor activity. Small molecular forms of factor VIII were adsorbed onto gold granules (average diameter 20-30 nm) and thereby increased their ristocetin cofactor activity. The amount of adsorbed material and the extent of activation were dependent on the pH of the colloid suspension. The maximum recovery of von Willebrand activity was observed at pH 4.75. Aggregation of fixed human platelets by factor VIII-coated gold particles was dependent on ristocetin concentration and was not competitively inhibited by unbound low-molecular-weight factor VIII. These results suggest that the subunits of the native small factor VIII species possess potential binding affinity for platelet receptors, which is manifested following formation of large factor VIII polymers. We conclude that an optimal size of remarkably high molecular weight is required for efficient aggregation of platelets by factor VIII as occurs during the primary phase of hemostasis.

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Studies on factor VIII-related protein IV. Interaction of galactose-specific lectins with human factor VIII/von willebrand factor

Cited by 5 publications

References 18 publications

Effect of Carbohydrate Modifications of Factor VIII/ von Willebrand Factor on Binding to Platelets

Effect of Carbohydrate Modifications of Factor VIII/ von Willebrand Factor on Binding to Platelets

Heterogeneity of Sugar Composition of Factor VIII/ von Willebrand Factor in von Willebrand's Disease: Analysis by Crossed Affinoimmunoelectrophoresis Using Lectin (Ricinus communis Agglutinin-120)

Von Willebrand Activity of Low Molecular Weight Human Factor VIII Increases by Binding to Gold Granules

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