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Thromb Haemost 1985; 53(03): 390-395
DOI: 10.1055/s-0038-1661321
Original Article
Schattauer GmbH Stuttgart

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

Jenny Goudemand
Université des Sciences et Techniques de Lille I, France
,
Claudine Mazurier
Université des Sciences et Techniques de Lille I, France
,
B Samor
Université des Sciences et Techniques de Lille I, France
,
S Bouquelet
*   The Laboratoire d’Hémostase du Centre Régional de Transfusion Sanguine de Lille et Laboratoire de Chimie Biologique et Laboratoire associé au CNRS n° 217
,
J Montreuil
*   The Laboratoire d’Hémostase du Centre Régional de Transfusion Sanguine de Lille et Laboratoire de Chimie Biologique et Laboratoire associé au CNRS n° 217
,
M Goudemand
Université des Sciences et Techniques de Lille I, France
› Author Affiliations
Further Information

Publication History

Received 13 December 1984

Accepted 21 March 1985

Publication Date:
21 August 2018 (online)

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Summary

This 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.

Keywords

von Willebrand factor - Carbohydrates - Platelet binding
 

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