Phospholipase A2 enhances [3H]AMPA binding to a putative homomeric GluR‐B receptor in the rat spinal cord

Abstract
[3H]AMPA and [3H]kanine binding to rat spinal cord was localised most densely in the substantia gelatinosa of the dorsal horn. Phospholipase A2 elicited a dose‐dependent increase in specific [3H]AMPA binding but not in [3H]kainate binding. The enhancement of [3H]AMPA binding was blocked by bromophenacyi bromide and at 0'C and was not mimicked by arachidonic acid. Since GluR‐B is the only AMPA receptor subunit detectable in the rat spinal cord, and recombinant homomeric GluR‐B assemblies do not bind [3H]kainate, these results suggest phospholipase A2 may modulate [3H]AMPA binding to putative homomeric GluR‐B receptors.
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