Distribution of glutamate transporter GLAST in membranes of cultured astrocytes in the presence of glutamate transport substrates and ATP

Shin, Jae-Won, Nguyen, Khoa T. D., Pow, David V., Knight, Toby, Buljan, Vlado, Bennett, Maxwell R. and Balcar, Vladimir J. (2009) Distribution of glutamate transporter GLAST in membranes of cultured astrocytes in the presence of glutamate transport substrates and ATP. Neurochemical Research, 34 10: 1758-1766. doi:10.1007/s11064-009-9982-z


Author Shin, Jae-Won
Nguyen, Khoa T. D.
Pow, David V.
Knight, Toby
Buljan, Vlado
Bennett, Maxwell R.
Balcar, Vladimir J.
Title Distribution of glutamate transporter GLAST in membranes of cultured astrocytes in the presence of glutamate transport substrates and ATP
Journal name Neurochemical Research   Check publisher's open access policy
ISSN 0364-3190
1573-6903
Publication date 2009-10
Sub-type Article (original research)
DOI 10.1007/s11064-009-9982-z
Volume 34
Issue 10
Start page 1758
End page 1766
Total pages 9
Editor Abel Lajtha
Place of publication New York, N.Y. U.S.A.
Publisher Springer New York
Collection year 2010
Language eng
Subject C1
110902 Cellular Nervous System
Formatted abstract
Neurotransmitter L-glutamate released at central synapses is taken up and “recycled” by astrocytes using glutamate transporter molecules such as GLAST and GLT. Glutamate transport is essential for prevention of glutamate neurotoxicity, it is a key regulator of neurotransmitter metabolism and may contribute to mechanisms through which neurons and glia communicate with each other. Using immunocytochemistry and image analysis we have found that extracellular d-aspartate (a typical substrate for glutamate transport) can cause redistribution of GLAST from cytoplasm to the cell membrane. The process appears to involve phosphorylation/dephosphorylation and requires intact cytoskeleton. Glutamate transport ligands L-trans-pyrrolidine-2,4-dicarboxylate and DL-threo-3-benzyloxyaspartate but not anti,endo-3,4-methanopyrrolidine dicarboxylate have produced similar redistribution of GLAST. Several representative ligands for glutamate receptors whether of ionotropic or metabotropic type, were found to have no effect. In addition, extracellular ATP induced formation of GLAST clusters in the cell membranes by a process apparently mediated by P2 receptors. The present data suggest that GLAST can rapidly and specifically respond to changes in the cellular environment thus potentially helping to fine-tune the functions of astrocytes.
Keyword Astrocytes
Glutamate synapses
Glutamate transport
GLAST
GLT
Brain metabolism
Na+, K+-dependent ATPase
Neurotransmitter metabolism
Regulation of transporters
Phosphorylation and dephosphorylation of membrane proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes From the issue entitled "Special Issue in Honor of Dr. Graham A. R. Johnston. Guest Editors: Philip M. Beart, Vladimir J. Balcar"

Document type: Journal Article
Sub-type: Article (original research)
Collections: UQ Centre for Clinical Research Publications
2010 Higher Education Research Data Collection
 
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Citation counts: TR Web of Science Citation Count  Cited 11 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 29 Sep 2009, 13:09:28 EST by Carmen Buttery on behalf of UQ Centre for Clinical Research