Glutathione-induced inhibition of Na+-independent and -dependent bindings of L-[3H]glutamate in rat brain

Reduced glutathione (GSH, 10(-7)-10(-3) M) was found to exert a profound suppressive action on the Na+-independent and -dependent bindings of L-[3H]glutamic acid (Glu) in a temperature-independent manner. Similarly significant reduction of the bindings resulted from the addition of oxidized glutathi...

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Published inLife sciences (1973) Vol. 39; no. 25; p. 2411
Main Authors Ogita, K, Kitago, T, Nakamuta, H, Fukuda, Y, Koida, M, Ogawa, Y, Yoneda, Y
Format Journal Article
LanguageEnglish
Published Netherlands 22.12.1986
Subjects
Animals
Brain - metabolism
Glutamates - metabolism
Glutathione - pharmacology
Kinetics
Oligopeptides - metabolism
Rats
Sodium - metabolism
Synaptosomes - metabolism
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Summary:Reduced glutathione (GSH, 10(-7)-10(-3) M) was found to exert a profound suppressive action on the Na+-independent and -dependent bindings of L-[3H]glutamic acid (Glu) in a temperature-independent manner. Similarly significant reduction of the bindings resulted from the addition of oxidized glutathione (GSSG). Scatchard analysis revealed that GSH as well as GSSG invariably decreased the affinity of the binding sites for [3H]Glu without significantly affecting the number of the binding sites. These results suggest that GSH (GSSG) may in part participate in the synaptic transmission at central Glu neurons through interaction with the receptors and/or the uptake sites for Glu.
ISSN:0024-3205
DOI:10.1016/0024-3205(86)90482-0