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Putative glutamate receptors in membranes obtained from heads of Drosophila melanogaster
Author(s) -
Fiedler J.L.,
Inestrosa N.C.,
Bustos G.
Publication year - 1986
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490160306
Subject(s) - quisqualic acid , kainic acid , butyric acid , stereochemistry , amino acid , glutamic acid , binding site , glutamate receptor , chemistry , dissociation constant , receptor , biochemistry , biology
The specific binding of L‐[ 3 H]‐glutamic acid (GLU) was examined in membrance preparations derived from heads of Drosophila melanogaster . L‐[ 3 H]‐GLU bound to the membrane preparation with biphasic in a reversible and saturable way. The specific binding was inhibited by Cl − and Ca 2+ ions. Saturation analysis of the data fit a model of two independent binding sites with dissociation constants (K D ) of 29 nM and 249 nM and corresponding binding site densities (B max ) of 5.7 and 24.6 pmol/mg protein. A series of excitatory amino acid receptor agonists and antagonists were tested as inhibitors of L‐[ 3 H]‐GLU specific binding. Some compounds almost totally abolished the specific binding, whereas others reduced the binding to 45% over the concentration range used. Among the first type of inhibitors, L‐GLU was the most potent, D‐aspartate (D‐ASP) and D‐GLU were 10 times less effective than L‐GLU, whereas quisqualic acid had the lowest potency. Among the second type of inhibitors, glutamate diethyl ester, D‐α‐amino adipate, and N‐methyl‐D‐aspartate showed the highest potency, and DL‐2‐amino‐4‐phosphonobutyrate was the less effective. Kainic acid and γ‐amino butyric acid were not able to modify at any concentration used the specific binding of L‐[ 3 H]‐GLU. These data suggest the presence of putative GLU receptors in the brain of Drosophila .