Glutamate receptor antibodies activate a subset of receptors and reveal an agonist binding site

  title={Glutamate receptor antibodies activate a subset of receptors and reveal an agonist binding site},
  author={Roy E. Twyman and Lorise C Gahring and Joachim Spiess and Scott W. Rogers},

Figures from this paper

Autoantibodies to the glutamate receptor kill neurons via activation of the receptor ion channel.
Results show that antibodies to a specific peptide of the GluR can kill neurons by an excitotoxic mechanism, thus mimicking the effects of excess of glutamate, the first example that antibodies can lead to neuronal death in a non-classical complement-independent manner.
Autoantibodies Against an Extracellular Peptide of the GluR3 Subtype of AMPA Receptors Activate Both Homomeric and Heteromeric AMPA Receptor Channels
It is reported here that the affinity-purified anti-GluR3B Abs directly activate GluR 3-containing homomeric and heteromeric AMPA receptor complexes without the requirement of neuronal, glial or blood ancillary molecules.
Identification of Amino Acids in the Glutamate Receptor, GluR3, Important for Antibody-binding and Receptor-specific Activation*
This study produced additional rabbit anti-GluR3B-specific antibodies, ranked them according to their ability to function as GluR agonists and characterized the immunoreactivity using deletion and alanine substitution mutagenesis to conclude that antibody contacts with key residues in the Glu R3B region define a novel GLUR subunit-specific agonist binding site and impart sub unit-specific immunore activity.
Antibodies Against the NH2-Terminus of the GluA Subunits Affect the AMPA-Evoked Releasing Activity: The Role of Complement
The results suggest the presence of GluA2/GluA3-containing release-regulating AMPA autoreceptors in cortical synaptosomes, which could be relevant to the development of autoimmune diseases typified by an overproduction of anti-GLUA subunits.
Glutamate Receptor GluR 3 Antibodies and Death of Cortical Cells gliosis
The goal of this work was to determine whether cirbodies (anti-GluR3) suggested that anti-GLUR3 gained culating anti-R3 antibodies destroyed cortical cells access to the central nervous system where it exerted and if so, by what mechanism, and to confirm and deleterious effects.
Antibodies prepared to neuronal glutamate receptor subunit3 bind IFNalpha-receptors: implications for an autoimmune process.
It is proposed that the IFNAR-1 may be an heteroclitic antigen of GluR3, which may contribute to variable clinical characteristics of certain autoimmune diseases.


Selective distribution of kainate receptor subunit immunoreactivity in monkey neocortex revealed by a monoclonal antibody that recognizes glutamate receptor subunits GluR5/6/7
Data indicate a high degree of selectivity in the distribution of kainate receptors composed of GluR5/6/7 subunits, and suggest that functional specificity and diversity in the ubiquitous excitatory amino acid-utilizing axonal systems in neocortex are achieved in part by the differential association of particular glutamate receptor subunits with specific cortical circuits.
Distribution of the excitatory amino acid receptor subunits GluR2(4) in monkey hippocampus and colocalization with subunits GluR5-7 and NMDAR1
Detailed regional, cellular, and ultrastructural distribution patterns of the EAA receptor subunits GluR2 and GLUR4 in monkey hippocampus are presented based on the use of a monoclonal antibody, 3A11, which was generated against the putative extracellular N-terminal domain of Glu R2.
The characterization and localization of the glutamate receptor subunit GluR1 in the rat brain
The results suggest that glutamate excitatory circuits recognized by these antisera are predominantly found in regions of the limbic system that are reciprocally interconnected.
Autoantibodies to Neuronal Glutamate Receptors in Patients with Paraneoplastic Neurodegenerative Syndrome Enhance Receptor Activation
It is reported here that neuronal glutamate receptors are targets for autoantibodies found in the serum from some patients with well-characterized PNS and the ability of these autoantibia to modulate glutaminergic receptor function suggest that some paraneoplastic neurological injury could result from glutamate-mediated excitotoxicity.
GABAA receptor needs two homologous domains of the & beta;-subunit for activation by GABA but not by pentobarbital
Evidence suggesting that the two identified domains of the β-subunit contribute a major component of the GABA receptor is presented, suggesting these two different classes of agonists activate GABA channels through distinct mechanisms.
Cloned glutamate receptors.
The application of molecular cloning technology to the study of the glutamate receptor system has led to an explosion of knowledge about the structure, expression, and function of this most important
Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.
These results identify a switch in the molecular and functional properties of glutamate receptors operated by alternative splicing.
Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation.
  • Z. Wo, R. Oswald
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
It is shown that a portion of these receptors previously thought to be a large intracellular loop is actually located extracellularly and an alternative model for the transmembrane topology of kainate receptors is proposed that could potentially serve as a framework for future detailed study of the structure of this important class of neurotransmitter receptors.