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

FEBS Letters

Henley, Jeremy M.¹  Cruickshank, Alison M.¹ 

[1] Department of Pharmacology, Medical School, University of Birmingham, Edgbaston, Birmingham, BIS 2TT, England

关键词: Spinal cord;    GluR-B;    AMPA;    Phospholipase A2;    Kainate;    Autoradiography;   

DOI  :  10.1016/0014-5793(94)80408-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

[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.

【 授权许可】

Unknown