Glycine receptor autoantibody binding to the extracellular domain is independent from receptor glycosylation.

ABSTRACT: Glycine receptor (GlyR) autoantibodies are associated with stiff-person syndrome and the life-threatening progressive encephalomyelitis with rigidity and myoclonus in children and adults. Patient histories show variability in symptoms and responses to therapeutic treatments. A better understanding of the autoantibody pathology is required to develop improved therapeutic strategies. So far, the underlying molecular pathomechanisms include enhanced receptor internalization and direct receptor blocking altering GlyR function. A common epitope of autoantibodies against the GlyRα1 has been previously defined to residues ¹A-³³G at the N-terminus of the mature GlyR extracellular domain. However, if other autoantibody binding sites exist or additional GlyR residues are involv

SUBMITTER: Rauschenberger V 

PROVIDER: S-EPMC9969106 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature