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PMID: 788859 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Immunocytochemical localization of glutamate decarboxylase in rat substantia nigra.

Brain research ·Vol. 116 ·No. 2 ·1976-11-05 ·Pages 287-98

Ribak CE, Vaughn JE, Saito K, Barber R, Roberts E

Abstract

L-Glutamate decarboxylase (GAD, EC 4.1.1.15), the enzyme which catalyzes the alpha-decarboxylation of L-glutamate to form gamma-aminobutyric acid (GABA), was localized both light and electron microscopically in rat substantia nigra by an immunoperoxidase method. Large amounts of GAD-positive reaction produce were seen throughout the substantia nigra in light microscopic preparations, and it appeared to be localized in punctate structures that were apposed to dendrites and somata. Electron microscopic studies revealed that most of the axon terminals in the substantia nigra were filled with GAD-positive reaction product and formed both axodendritic and axosomatic synapses. Many dendrites were extensively surrounded by GAD-positive terminals which most commonly formed symmetric synaptic junctions, although some formed asymmetric synpatic junctions. The results of this investigation are consistent with biochemical, pharmacological and physiological data which have indicated that neurons of the neostriatum and globus pallidus exert a GABA-mediated, postsynaptic inhibition upon the neurons of the substantia nigra. These findings provide another example in the vertebrate central nervous system where Golgi I projection neurons are inhibitory and use GABA as their neurotransmitter.

MeSH Terms
Animals Axons/enzymology Carboxy-Lyases/analysis Dendrites/enzymology Glutamate Decarboxylase/analysis Immunoenzyme Techniques Rats Substantia Nigra/enzymology,ultrastructure Synapses/enzymology
Chemicals
Carboxy-Lyases Glutamate Decarboxylase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ribak C E
Vaughn J E
Saito K
Barber R
Roberts E
Article Info
Journal
Brain research
Abbr.
Brain Res
ISSN
0006-8993
Published
1976-11-05
Pages
287-98
Language
English
Region
Netherlands
NLM ID
0045503
Subset
IM
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