Glycine receptor autoantibodies disrupt inhibitory neurotransmission

Author:

Crisp Sarah J1ORCID,Dixon Christine L1,Jacobson Leslie2,Chabrol Elodie1,Irani Sarosh R2ORCID,Leite M Isabel2,Leschziner Guy34,Slaght Sean J5,Vincent Angela12,Kullmann Dimitri M1ORCID

Affiliation:

1. UCL Institute of Neurology, University College London, London, UK

2. Nuffield Department of Clinical Neurosciences, University of Oxford, Oxford, UK

3. Department of Neurology, Guy’s and St Thomas’ NHS Foundation Trust, London, UK

4. Department of Clinical Neuroscience, King’s College London, London, UK

5. Wessex Neurological Centre, University Hospital Southampton NHS Foundation Trust, Southampton, UK

Abstract

Immunoglobulin G autoantibodies to glycine receptors are found in many patients with progressive encephalomyelitis with rigidity and myoclonus (PERM). Crisp et al. show that purified patient IgGs disrupt inhibitory neurotransmission in cultured motoneurons, and provide evidence for direct antagonistic actions on glycine receptors.

Funder

Wellcome Trust

National Institute for Health Research

BMA Foundation

National Organisation for Rare Disorders

BMA Research Grants- Vera Down

Epilepsy Research UK

NIHR

Oxford Biomedical Research Centre

Nuffield Department of Clinical Neurosciences

Medical Research Council

Publisher

Oxford University Press (OUP)

Subject

Neurology (clinical)

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