To characterize internalization of NMDA-type glutamate receptors (GluRs) by antibodies to NMDA-type GluRs, we produced rabbit antibodies to N-terminals of human GluN1 and GluN2B, and examined internalization of NMDA-type GluRs in HEK293T cells using confocal microscopy. Internalization of NMDA-type GluRs occurred from at least 10 min after incubation with antibodies to GluN1 and or GluN2B and was temperature-dependent. These findings confirm that antibodies to N-terminals of GluN1 and GluN2B present in the cerebrospinal fluid of patients with NMDAR encephalitis can mediate prompt internalization of NMDA-type GluR complexes.
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http://dx.doi.org/10.1016/j.jneuroim.2020.577427 | DOI Listing |
J Neurosci
December 2024
Department of Neuroscience, Baylor College of Medicine, Houston, TX, USA
Excitatory synapses and the actin-rich dendritic spines on which they reside are indispensable for information processing and storage in the brain. In the adult hippocampus, excitatory synapses must balance plasticity and stability to support learning and memory. However, the mechanisms governing this balance remain poorly understood.
View Article and Find Full Text PDFJ Neurosci
November 2024
Department of Neurobiology and Biophysics, University of Washington School of Medicine. 1705 NE Pacific St., HSB G-424, Seattle, Washington. 98195-7290
NMDA-type glutamate receptors are heterotetrameric complexes composed of two GluN1 and two GluN2 subunits. The precise composition of the GluN2 subunits determines the channel's biophysical properties and influences its interaction with postsynaptic scaffolding proteins and signaling molecules involved in synaptic physiology and plasticity. The precise regulation of NMDAR subunit composition at synapses is crucial for proper synaptogenesis, neuronal circuit development, and synaptic plasticity, a cellular model of memory formation.
View Article and Find Full Text PDFJ Neuroimmunol
December 2020
Department of Molecular Neuroscience, Graduate Schools of Innovative Life Science and Medicine, University of Toyama, Toyama, Japan. Electronic address:
To characterize internalization of NMDA-type glutamate receptors (GluRs) by antibodies to NMDA-type GluRs, we produced rabbit antibodies to N-terminals of human GluN1 and GluN2B, and examined internalization of NMDA-type GluRs in HEK293T cells using confocal microscopy. Internalization of NMDA-type GluRs occurred from at least 10 min after incubation with antibodies to GluN1 and or GluN2B and was temperature-dependent. These findings confirm that antibodies to N-terminals of GluN1 and GluN2B present in the cerebrospinal fluid of patients with NMDAR encephalitis can mediate prompt internalization of NMDA-type GluR complexes.
View Article and Find Full Text PDFJ Neurosci
November 2016
Department of Pharmacology, University of Colorado Denver School of Medicine, Denver, Colorado 80045, and
Unlabelled: Beta amyloid (Aβ) triggers the elimination of excitatory synaptic connections in the CNS, an early manifestation of Alzheimer's disease. Oligomeric assemblies of Aβ peptide associate with excitatory synapses resulting in synapse elimination through a process that requires NMDA-type glutamate receptor activation. Whether Aβ affects synaptic NMDA receptor (NMDAR) function directly and acts locally at synapses to which it has bound and whether synaptic activity influences Aβ synaptic binding and synaptotoxicity have remained fundamental questions.
View Article and Find Full Text PDFBrain Nerve
April 2013
National Epilepsy Center, Shizuoka Institute of Epilepsy and Neurological Disorders, Japan.
Glutamate receptors (GluRs) are classified into metabotropic GluRs and ionotropic GluRs. Ionotropic GluRs include the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) -type, kainate (KA)-type, and N-methyl-D-aspartate (NMDA)-type GluRs (NRs). Antibodies to the NRs have been detected using immunoblot, cell-based assays, and enzyme linked immunosorbent assay (ELISA).
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