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Neurochem Int. 1987;10(4):565-70. doi: 10.1016/0197-0186(87)90086-6.

Characterization of [(3)H]glutamate binding sites on frozen sections from rat adrenal.

Neurochemistry international

H Nakamuta, K Ogita, Y Fukuda, M Koida, Y Yoneda

Affiliations

  1. Department of Pharmacology, Setsunan University, Hirakata, Osaka 573-01, Japan.

PMID: 20501132 DOI: 10.1016/0197-0186(87)90086-6

Abstract

Some biochemical characteristics of [(3)H]glutamate (Glu) binding sites on frozen sections from the rat adrenal glands were studied. Adrenal frozen sections exhibited stereo-selective, saturable and temperature-dependent binding of [(3)H]Glu. An agonist for one of the subclasses of central Glu receptors, quisqualic acid (QA), elicited a significant inhibition of the binding, whereas neither N-methyl-d-aspartic acid nor kainic acid, agonists for other subclasses of the receptors, had such a significant effect on the binding at the concentration range similar to QA. In vitro addition of sodium acetate (100 mM) resulted in a significant inhibition of [(3)H]Glu binding to frozen sections of the rat adrenal glands. It thus appears that there exist QA-sensitive binding sites of [(3)H]Glu in the rat adrenal glands which exhibit pharmacological characteristics distinctly different from those in the brain.

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