Mechanism of Transport and Storage of Neurotransmitter

Kanner, Baruch I.; Schuldiner, Shimon

doi:10.3109/10409238709082546

Cited by 467 publications

(244 citation statements)

References 185 publications

Supporting

Mentioning

238

Contrasting

Unclassified

Order By: Relevance

“…The glutamate uptake detected in cultured rat pinealocytes shows properties similar to reuptake systems in nervous tissues; these uptake systems are required for an extracellular Na + gradient with similar kinetics and are inhibited to similar extents by inhibitors (Kanner and Schuldiner, 1987;Kanner, 1993;Arriza et al, 1994;Garlin et al, 1995). Furthermore, the extracellular glutamate is actually sequestered in an Na ±-dependent manner in cultured pinealocytes with similar inhibitor sensitivities (Fig.…”

Section: Immunological Localization Of the Glt-1-type Transportermentioning

confidence: 73%

See 1 more Smart Citation

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Yamada¹,

Yatsushiro²,

Yamamoto

et al. 1997

Journal of Neurochemistry

View full text Add to dashboard Cite

Pinealocytes, the neuroendocrine cells that produce melatonin, accumulate glutamate in microvesides through a specific vesicular transporter energetically coupled with vacuolar-type proton ATPase. The glutamate is secreted into the extracellular space through microvesicle-mediated exocytosis and then stimulates neighboring pinealocytes, resulting in inhibition of norepinephrine-dependent melatonin synthesis. In this study, we identified and characterized the plasma membranetype glutamate transporter in rat pinealocytes. The [ 3H]-glutamate uptake by cultured pinealocytes was driven by extracellular Nat, saturated with the [3H]glutamate concentration used, and significantly inhibited by L-glutamate, L-aspartate, ß-threo-hydroxyaspartate, pyrrolidine dicarboxylate, and L-cysteine sulfinate, substrates or inhibitors of the plasma membrane glutamate transporter. Consistently, the clearance of extracellular glutamate, as measured by HPLC, was also dependent on Na~and inhibited by /9-threo-hydroxyaspartate and L-cysteine sulfinate. Immunological studies with site-specific antibodies against three isoforms of the Nat-dependent glutamate transporter (GLT-1, GLAST, and EAAC1) revealed the expression of only the GLT-1 type transporter in pineal glands. Expression of the GLT-1 type transporter in pineal glands was further demonstrated by means of reverse transcription-polymerase chain reaction with specific DNA probes. Immunohistochemical analysis indicated that the immunological counterpart(s) of the GLT-1 is localized in pinealocytes. These results suggested that the GLT-1 -type Nat-dependent transporter is expressed and functions as a reuptake system for glutamate in rat pinealocytes. The physiological role of the transporter in the termination of the glutamate signal in the pineal gland is discussed. Key Words: Na-dependent glutamate transporter-Pinealocyte-Pineal gland -L-Glutamate-GLT-1 -Reuptake-Microvesicle-Endocrine cell.

show abstract

Section: Immunological Localization Of the Glt-1-type Transportermentioning

confidence: 73%

“…In the synaptic cleft, released L-glutamate is rapidly sequestered by Na+ -dependent transporters (Kanner and Schuldiner, 1987;Kanai et al, 1993;Kanner, 1993). The reuptake system is responsible for termination of the glutamate signal in chemical transduction and a reduction in glutamate cytotoxicity toward nervous tissues (Kanai et al, 1993;Kanner, 1993).…”

mentioning

confidence: 99%

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Yamada¹,

Yatsushiro²,

Yamamoto

et al. 1997

Journal of Neurochemistry

View full text Add to dashboard Cite

show abstract

“…This latter technique has the advantage that the membrane potential can be controlled throughout the transport experiments. It is reassuring that the results obtained with both techniques are in harmony with each other (reviewed in [5] and [22]), and they are summarized here briefly. In addition to L-glutamate, D-and L-aspartate are transportable substrates with affinities in the lower micromolar range.…”

Section: The Substrates Of the L-glutamate Transportermentioning

confidence: 99%

Glutamate transporters from brain

Kanner

1993

FEBS Letters

Self Cite

121

View full text Add to dashboard Cite

The removal of neurotransmitters by their transporters in presynaptic nerve terminals and glial cells plays an important role in the termination of synaptic transmission. Many neurotransmitter transporters, which are sodium-and chloride-coupled, have been cloned and shown to constitute a large superfamily. Glutamate is the major excitatory neurotransmitter in the central nervous system. If not efficiently removed, it causes death of neuronal cells. Its transporter couples the flow of glutamate to that of sodium and potassium. Recently three different but related glutamate transporters have been cloned, which have no significant homology to the members of the superfamily.

show abstract

“…Na + ions drive the transport in eukaryotic and H + ions in prokaryotic cells against the gradient of the transported compounds. They cotransport Na + and countertransport K + ions [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Human high affinity, Na⁺‐dependent l‐glutamate/l‐aspartate transporter GLAST‐1 (EAAT‐1) : gene structure and localization to chromosome 5p11‐p12

Stoffel¹,

Sasse²,

Düker³

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

The gene of the human L-glutamate transporter hGLAST-1 (EAAT-1) has been isolated and characterized. The 1626 bp cDNA open reading frame (542 aa) is distributed over ten exons and at least 85 kb on chromosome 5pll-p12. The gene is unrelated to any other previously described neurotransmitter transporter gene family, but its exon/intron structure corresponds largely to that of the Na+-dependent neutral amino acid transporter ASCT-I. GLAST-1, ASCT-1 and the glutamate transporters GLT-1 and EAAC-1 have strongly similar amino acid sequences. The L-glutamate transporter gene structures might help to understand the correlation of L-glutamate reuptake in neurodegenerative disorders.Key words: Glutamate; Aspartate; Neurotransmitter transporter; hGLAST-1 ers (dopamine, serotonine, glycine, GABA, adrenaline) [10] in which transmembrane domains largely correspond to single exons the topology of all GLAST-l-related transporters convincingly reveals only a six TMH motif in the N-terminal half but an undefined C-terminal membrane topology [1-3,11].Here we report the cloning and characterization of the first gene structure of the excitatory amino acid (Glu/Asp) transporter family, hGlast-1 (EAAT-1). The coding sequence is distributed over nine exons with one untranslated exon I preceding.We determined the hGlast-1 locus on chromosome 5pll-p12 by fluorescence in situ hybridization. In a previous communication the mouse and human gene EAAT-1 was assigned to mouse chromosome 15 and a region of syntenic homology on human chromosome 5p13 [12].

show abstract

Mechanism of Transport and Storage of Neurotransmitter

Cited by 467 publications

References 185 publications

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Glutamate transporters from brain

Human high affinity, Na⁺‐dependent l‐glutamate/l‐aspartate transporter GLAST‐1 (EAAT‐1) : gene structure and localization to chromosome 5p11‐p12

Contact Info

Product

Resources

About

Mechanism of Transport and Storage of Neurotransmitter

Cited by 467 publications

References 185 publications

Functional Expression of a GLT‐1 Type Na+‐Dependent Glutamate Transporter in Rat Pinealocytes

Functional Expression of a GLT‐1 Type Na+‐Dependent Glutamate Transporter in Rat Pinealocytes

Glutamate transporters from brain

Human high affinity, Na+‐dependent l‐glutamate/l‐aspartate transporter GLAST‐1 (EAAT‐1) : gene structure and localization to chromosome 5p11‐p12

Contact Info

Product

Resources

About

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Functional Expression of a GLT‐1 Type Na⁺‐Dependent Glutamate Transporter in Rat Pinealocytes

Human high affinity, Na⁺‐dependent l‐glutamate/l‐aspartate transporter GLAST‐1 (EAAT‐1) : gene structure and localization to chromosome 5p11‐p12