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The biological significance of von Willebrand factor o-linked glycosylation

Glycosylation is a key posttranslational modification, known to occur on more than half of all secreted proteins in man. As such, the role of N- and O-linked glycan structures in modulating various aspects of protein biology is an area of much research. Given their prevalence, it is perhaps unsurprising that variations in glycan structures have been demonstrated to play critical roles in modulating protein function and have been implicated in the pathophysiology of human diseases. von Willebrand factor (VWF), a plasma glycoprotein that is essential for normal hemostasis, is heavily glycosylated, containing 13 N-linked and 10 O-linked glycans. Together, these carbohydrate chains account for 20% of VWF monomeric mass, and have been shown to modulate VWF structure, function, and half-life. In this review, we focus on the specific role played by O-linked glycans in modulating VWF biology. Specifically, VWF O-linked glycans have been shown to modulate tertiary protein structure, susceptibility to ADAMTS13 proteolysis, platelet tethering, and VWF circulatory half-life.

Funding

Science Foundation Ireland Principal Investigator Award (11/PI/1066)

History

Comments

The original article is available at https://www.thieme-connect.de

Published Citation

Ward S, O'Sullivan JM, O'Donnell JS. The biological significance of von Willebrand Factor O-Linked glycosylation. Semin Thromb Hemost. 2021.

Publication Date

15 June 2021

PubMed ID

34130346

Department/Unit

  • Irish Centre for Vascular Biology
  • School of Pharmacy and Biomolecular Sciences

Research Area

  • Health Professions Education
  • Vascular Biology
  • Cancer
  • Immunity, Infection and Inflammation

Publisher

Georg Thieme Verlag KG

Version

  • Accepted Version (Postprint)