Glycosaminoglycan neutralization in coagulation control
Date
06/2018Keywords
Metadata
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Abstract
The glycosaminoglycans (GAGs) heparan sulfate, dermatan sulfate and heparin are important anticoagulants that inhibit clot formation through interactions with antithrombin and heparin cofactor II. Unfractionated heparin, low molecular weight heparin and heparin-derived drugs are often the main treatments used clinically to handle coagulatory disorders. A wide range of proteins have been reported to bind and neutralise these GAGs to promote clot formation. Such neutralising proteins are involved in a variety of other physiological processes, including inflammation, transport and signalling. It is clear that these interactions are important for the control of normal coagulation and influence the efficacy of heparin and heparin-based therapeutics. In additon to neutralisation, the anticoagulant activities of GAGs may also be regulated through reduced synthesis or by degradation. In this review we describe GAG neutralisation, the proteins involved and the molecular processes that contribute to the regulation of anticoagulant GAG activity.
Citation
Sobczak , A I S , Pitt , S J & Stewart , A J 2018 , ' Glycosaminoglycan neutralization in coagulation control ' , Arteriosclerosis, Thrombosis, and Vascular Biology , vol. 38 , no. 6 , pp. 1258-1270 . https://doi.org/10.1161/ATVBAHA.118.311102
Publication
Arteriosclerosis, Thrombosis, and Vascular Biology
Status
Peer reviewed
ISSN
1524-4636Type
Journal item
Rights
© 2018 The Authors. Arteriosclerosis, Thrombosis, and Vascular Biology is published on behalf of the American Heart Association, Inc., by Wolters Kluwer Health, Inc. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution, and reproduction in any medium, provided that the original work is properly cited.
Description
This work was supported by the British Heart Foundation (grant codes: PG/15/9/31270 and FS/15/42/31556). S.J. Pitt is supported by a Royal Society of Edinburgh Biomedical Fellowship (XRE013).Collections
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