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Department of Pharmacology, Georgetown University School of
Medicine, Washington, D.C. 20007
A monoclonal antibody (R1JHL) against the NR1 subunit of the
N-methyl-D-aspartate (NMDA) receptor has
been developed that recognizes an epitope in the region of the
amino-terminal amino acids 341-561 (a region common to all splice
variants of NR1). This monoclonal antibody identifies a broad band at
115 kDa in immunoblots using membranes from NR1-transfected cells and
from rat brain tissue. No cross-reactivity with any NR2 subunit is seen. With the goal to determine quantitatively the subunit composition of cortical NMDA receptors, we used the monoclonal antibody to NR1 and
polyclonal antibodies against the NR2A and NR2B subunits to perform
immunoprecipitations of receptor subunits from solubilized adult rat
cortical membranes. Solubilization of the receptor subunits was
accomplished under both nondenaturing (native) conditions, under which
the subunits seem to remain associated with one another, and denaturing
conditions, under which the subunits are dissociated from each other.
Although each of these antibodies selectively immunoprecipitates only
its corresponding (cognate) subunit when the subunits have been
solubilized under denaturing conditions, each of the antibodies
immunoprecipitates a sizable fraction of the other two NMDA receptor
subunits when membranes are solubilized under nondenaturing conditions,
indicating an interaction in situ. Using quantitative
immunoblot analysis of the three subunits in both the pellets and
supernatants from the immunoprecipitations, we found 1) the dominant
NMDA receptor complex in adult rat cortex contains at least three
subunits, NR1/NR2A/NR2B; 2) a smaller fraction of NMDA receptors are
composed of only two subunits, NR1/NR2B or NR1/NR2A; 3) there are no
complexes that contain NR2A/NR2B that do not contain NR1; 4) only a
small fraction of each subunit is not associated with any other NMDA
receptor subunit; 5) no coimmunoprecipitation of noncognate subunits
occurs unless the subunits are assembled with each other in
situ; and 6) there is no physical interaction between these
NMDA receptor subunits and the
-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor GluR2
or GluR3 subunits. These results suggest that functional studies with
recombinant receptors composed of at least three subunits may be the
most physiologically meaningful.
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