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Phospholipase A 2 enhances [ 3 H]AMPA binding to a putative homomeric GluR‐B receptor in the rat spinal cord
Author(s) -
Cruickshank Alison M.,
Henley Jeremy M.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80408-7
Subject(s) - ampa receptor , homomeric , kainate receptor , chemistry , spinal cord , glutamate receptor , receptor , biochemistry , protein subunit , neuroscience , biology , gene
[ 3 H]AMPA and [ 3 H]kanine binding to rat spinal cord was localised most densely in the substantia gelatinosa of the dorsal horn. Phospholipase A 2 elicited a dose‐dependent increase in specific [ 3 H]AMPA binding but not in [ 3 H]kainate binding. The enhancement of [ 3 H]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 [ 3 H]kainate, these results suggest phospholipase A 2 may modulate [ 3 H]AMPA binding to putative homomeric GluR‐B receptors.