The role of gangliosides in the organisation of the node of Ranvier examined in glycosyltransferase transgenic mice

McGonigal, R. and Willison, H. J. (2022) The role of gangliosides in the organisation of the node of Ranvier examined in glycosyltransferase transgenic mice. Journal of Anatomy, 241(5), pp. 1259-1271. (doi: 10.1111/joa.13562) (PMID:34605014) (PMCID:PMC9558150)

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Abstract

Gangliosides are a family of sialic acid containing glycosphingolipids highly enriched in plasma membranes of the vertebrate nervous system. They are functionally diverse in modulating nervous system integrity, notably at the node of Ranvier, and also act as receptors for many ligands including toxins and autoantibodies. They are synthesised in a stepwise manner by groups of glycosyl- and sialyltransferases in a developmentally and tissue regulated manner. In this review, we summarise and discuss data derived from transgenic mice with different transferase deficiencies that have been used to determine the role of glycolipids in the organisation of the node of Ranvier. Understanding their role at this specialised functional site is crucial to determining differential pathophysiology following directed genetic or autoimmune injury to peripheral nerve nodal or paranodal domains, and revealing the downstream consequences of axo-glial disruption.

Item Type:Articles
Additional Information:This work was funded by the Wellcome Trust (Grants 092805 and 202789).
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:McGonigal, Dr Rhona and Willison, Professor Hugh
Authors: McGonigal, R., and Willison, H. J.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Journal of Anatomy
Publisher:Wiley
ISSN:0021-8782
ISSN (Online):1469-7580
Published Online:03 October 2021
Copyright Holders:Copyright © 2021 The Authors
First Published:First published in Journal of Anatomy 241(5): 1259-1271
Publisher Policy:Reproduced under a Creative Commons License

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
165079The structural and functional diversity of anti-glycolipid antibody repertoires and their nerve binding domains in human autoimmune neuropathyHugh WillisonWellcome Trust (WELLCOTR)092805/Z/10/ZIII - Immunology
173549Pathophysiological factors in the diagnosis and treatment of the Guillain-Barre syndromesHugh WillisonWellcome Trust (WELLCOTR)202789/Z/16/ZIII - Immunology