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Coupling of Inositol Phospholipid Metabolism with Excitatory Amino Acid Recognition Sites in Rat Hippocampus
Author(s) -
Nicoletti F.,
Meek J. L.,
Iadarola M. J.,
Chuang D. M.,
Roth B. L.,
Costa E.
Publication year - 1986
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.1471-4159.1986.tb12922.x
Subject(s) - inositol , quinolinate , kainate receptor , biochemistry , phospholipase c , biology , chemistry , quisqualic acid , glutamate receptor , amino acid , ampa receptor , receptor , tryptophan , quinolinic acid
Ibotenate, a rigid structural analogue of glutamate, markedly enhances the hydrolysis of membrane inositol phospholipids, as reflected by the stimulation of [ 3 H]inositol monophosphate formation in rat hippocampal slices prelabeled with [ 3 H]inositol and treated with Li + . Quisqualate, homocysteate, l ‐glutamate, and l ‐aspartate also induce a significant (albeit weaker) increase in [ 3 H]inositol monophosphate formation, whereas N ‐methyl‐ d ‐aspartate, kainate, quinolinate, and N ‐acetylaspartylglutamate are inactive. The increase in [ 3 H]inositol monophosphate formation elicited by the above‐mentioned excitatory amino acids is potently and selectively antagonized by dl ‐2‐amino‐4‐phosphonobutyric acid, a dicarboxylic amino acid receptor antagonist. These results suggest that, in the hippocampus, a class of dicarboxylic amino acid recognition sites is coupled with phospholipase C, the enzyme that catalyzes the hydrolysis of membrane inositol phospholipids.