Premium
Metabotropic Excitatory Amino Acid Receptor Activation Stimulates Phospholipase D in Hippocampal Slices
Author(s) -
Boss Valerie,
Conn P. Jeffrey
Publication year - 1992
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1992.tb10131.x
Subject(s) - metabotropic glutamate receptor , metabotropic receptor , acpd , metabotropic glutamate receptor 1 , metabotropic glutamate receptor 7 , chemistry , metabotropic glutamate receptor 3 , metabotropic glutamate receptor 2 , metabotropic glutamate receptor 4 , metabotropic glutamate receptor 6 , metabotropic glutamate receptor 5 , biochemistry , glutamate receptor , biophysics , neuroscience , receptor , biology
Metabotropic excitatory amino acid (EAA) receptors are coupled to effector systems through G proteins. Because various G protein‐coupled receptors stimulate the hydrolysis of phosphatidylcholine by phospholipase D (PLD), we examined the possibility that metabotropic EAA receptors exist that are coupled to the activation of PLD. We found that the selective metabotropic glutamate receptor (mGluR) agonists 1 S, 3 R ‐amino‐1,3‐cyclopentanedicarboxylic acid (ACPD) and 1 S, 3 S ‐ACPD, but not the inactive isomer, 1 R, 3 S ‐ACPD, induce a concentration‐dependent increase in PLD activity in hippocampal slices. Selective ionotropic glutamate receptor (iGluR) antagonists did not block 1 S, 3 R ‐ACPD‐induced PLD stimulation. Furthermore, although selective iGluR agonists did not activate this response, the nonselective mGluR‐iGluR agonists, ibotenate and quisqualate, caused significant increases in PLD activity (all in the presence of iGluR antagonists). L‐2‐Amino‐3‐phosphonopropionic acid, which blocks the mGluR that is coupled to phosphoinositide hydrolysis in various brain regions, activates PLD to the same extent as the active isomers of ACPD. These data suggest that metabotropic EAA receptors exist in hippocampus that are coupled to PLD activation and are pharmacologically distinct from phosphoinositide hydrolysis‐coupled mGluRs.