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Journal of Neuroscience, Vol 14, 6102-6120, Copyright © 1994 by Society for Neuroscience
The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1
RS Petralia, YX Wang and RJ Wenthold
Laboratory of Neurochemistry, NIDCD, NIH, Bethesda, Maryland 20892.
Neuronal plasticity associated with learning, memory and development is
controlled, in part, by NMDA receptors, which are complexes consisting of
the subunit NMDAR1 (NR1) and one or more NMDAR2 subunits (NR2A- NR2D). We
made a polyclonal antibody to a C-terminus peptide of NR2A. In analysis of
transfected cell membranes, this antibody recognizes NR2A and NR2B, and to
a slight extent, NR2C and NR2D. In Western blots of rat brain, the antibody
labeled a single band that comigrated with NR2A and NR2B. This antibody
(NR2A/B) did not cross-react with extracts from transfected cells
expressing other glutamate receptor subunits, nor did it label non-neuronal
tissues. Immunostained sections of rat brain showed significant staining
throughout the nervous system, including olfactory bulb, cerebral cortex,
hippocampus, caudate- putamen, and many brainstem nuclei, as well as in
neurons of spinal cord and sensory ganglia. This widespread distribution of
staining was similar to that found with an antibody to NR1, supporting the
presence of functional NR1/NR2 complexes throughout the nervous system. In
the cerebellum, in contrast to staining with NR1 antibody, Purkinje cell
staining with NR2A/B antibody was low, indicating that these neurons may
lack functional NMDA receptors. EM examination revealed dense staining in
dendrites and postsynaptic densities in cerebral cortex and hippocampus,
similar to those seen with antibody to NR1. Since functional NMDA receptor
complexes at synapses appear to require both NR1 and NR2 subunit proteins
for full function, this study provides structural evidence for functional
NR1/NR2 receptors in vivo in the nervous system.
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