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J Thromb Haemost. 2010 Jan;8(1):137-45. doi: 10.1111/j.1538-7836.2009.03665.x. Epub 2009 Oct 24.

The plasma von Willebrand factor O-glycome comprises a surprising variety of structures including ABH antigens and disialosyl motifs.

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1
Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College, London, UK.

Abstract

BACKGROUND:

von Willebrand factor (VWF) is a key component for maintenance of normal hemostasis. Its glycan moieties, accounting for about 20% of its molecular weight, have been shown to affect many of its properties. Previous studies reported correlations between VWF secretion, half-life and the nature or presence of its N-glycans, and more importantly between VWF plasma level and the type of N-linked ABH antigens. Despite the presence of 10 predicted O-glycosylation sites, the O-glycome remains poorly characterized, impairing the complete elucidation of its influence on VWF functions. So far only a single glycan structure, a disialyl core 1 glycan, has been identified.

OBJECTIVES:

To define an exhaustive profile of the VWF O-glycan structures to help the understanding of their role in VWF regulation and properties.

METHODS:

Plasma-derived VWF O-linked sugars were isolated and analyzed using state-of-the-art mass spectrometry methodologies.

RESULTS AND CONCLUSIONS:

We provide here a detailed analysis of the human plasma-derived VWF O-glycome. Eighteen O-glycan structures including both core 1 and core 2 structures are now demonstrated to be present on VWF. Amongst the newly determined structures are unusual tetra-sialylated core 1 O-glycans and ABH antigen-containing core 2 O-glycans. In conjunction with current models explaining VWF activity, knowledge of the complete O-glycome will facilitate research aimed at providing a better understanding of the influence of glycosylation on VWF functions.

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