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The “Orphan” Na + /Cl ‐ ‐Dependent Transporter, Rxt1, Is Primarily Localized Within Nerve Endings of Cortical Origin in the Rat Striatum
Author(s) -
Kachidian P,
Masson J,
Aïdouni Z,
Gaspar P,
Hamon M,
Mestikawy S. El,
Goff L. KerkerianLe
Publication year - 1999
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 - 10.1046/j.1471-4159.1999.0730623.x
Subject(s) - striatum , excitatory postsynaptic potential , neuroscience , denervation , biology , immunogold labelling , kainic acid , immunocytochemistry , chemistry , glutamate receptor , microbiology and biotechnology , biochemistry , anatomy , ultrastructure , endocrinology , dopamine , inhibitory postsynaptic potential , receptor
: Previous studies have shown that the striatum expresses very low levels of Na + /Cl ‐ ‐dependent “orphan” transporter Rxt1 transcripts but contains high levels of protein. This study investigated the origin of Rxt1 expression in rat striatum. Striatal Rxt1 contents assessed by immunocytochemistry or western blotting were found to be significantly reduced after corticostriatal denervation but not after striatal or thalamic lesion with kainic acid or selective 6‐hydroxydopamine‐induced nigrostriatal deafferentation. Corticostriatal neurons retrogradely labeled by intrastriatal fluorogold injections were shown to express Rxt1 mRNA. Combination of anterograde biotin‐dextran amine labeling of the corticostriatal pathway with Rxt1 immunogold detection at the ultrastructural level demonstrated the presence of Rxt1 in about one‐third of the corticostriatal synaptic terminals and in numerous unidentified synaptic terminals. All the Rxt1‐positive terminals formed asymmetrical contacts on spines. These data provide evidence that striatal Rxt1 immunoreactivity is mainly of extrinsic origin and more specifically associated with the corticostriatal pathway. Rxt1 appears as a selective presynaptic marker of synapses formed by presumably excitatory amino acid afferents, but it segregates a subclass of these synapses, thereby revealing a functional heterogeneity among excitatory amino acid systems.