Localisation of novel forms of glutamate transporters and the cystine-glutamate antiporter in the choroid plexus: Implications for CSF glutamate homeostasis

Lee, Aven, Anderson, Ashley R., Rayfield, Andrew J., Stevens, Melissa G., Poronnik, Philip, Meabon, James S., Cook, David G. and Pow, David V. (2012) Localisation of novel forms of glutamate transporters and the cystine-glutamate antiporter in the choroid plexus: Implications for CSF glutamate homeostasis. Journal Of Chemical Neuroanatomy, 43 1: 64-75. doi:10.1016/j.jchemneu.2011.09.006


Author Lee, Aven
Anderson, Ashley R.
Rayfield, Andrew J.
Stevens, Melissa G.
Poronnik, Philip
Meabon, James S.
Cook, David G.
Pow, David V.
Title Localisation of novel forms of glutamate transporters and the cystine-glutamate antiporter in the choroid plexus: Implications for CSF glutamate homeostasis
Journal name Journal Of Chemical Neuroanatomy   Check publisher's open access policy
ISSN 0891-0618
1873-6300
Publication date 2012-01-01
Year available 2011
Sub-type Article (original research)
DOI 10.1016/j.jchemneu.2011.09.006
Volume 43
Issue 1
Start page 64
End page 75
Total pages 12
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Collection year 2012
Language eng
Abstract The choroid plexus is a structure within each ventricle of the brain that is composed of fenestrated vessels surrounded by secretory epithelial cells. The epithelial cells are linked by tight junctions to create a permeability barrier. The epithelial cells are derived from neuroectoderm, and are thus defined by some authors as a subtype of macroglia. Glutamate is a tightly regulated substance in the CSF, as it is in the rest of the brain. In the brain macroglia express multiple sodium dependent and independent glutamate transporters and are the main regulators of extracellular glutamate. However, the identities of the transporters in the choroid plexus and their localisations have remained poorly defined. In this study we examined the expression and distribution of multiple splice variants of classical sodium-dependent glutamate transporters, as well as the cystine-glutamate antiporter, and the PDZ protein NHERF1, (which acts as a molecular anchor for proteins such as the glutamate transporter GLAST). We identified three forms of sodium-dependent transporters (GLAST1a, GLAST1c and GLT1b) that are expressed at the apical surface of the epithelial cells, a location that matches the distribution of NHERF1 and the cystine-glutamate antiporter. We propose that this coincident localisation of GLAST1a/GLAST1c/GLT1b and the cystine-glutamate antiporter would permit the cyclical trafficking of glutamate and thus optimise the accumulation of cystine for the formation of glutathione in the choroid plexus.
Keyword EAAT
GLAST
GLT1
Glutamate
Transporter
CSF
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Available online 29 September 2011

Document type: Journal Article
Sub-type: Article (original research)
Collections: UQ Centre for Clinical Research Publications
Official 2012 Collection
 
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Created: Wed, 19 Oct 2011, 19:13:20 EST by Roheen Gill on behalf of UQ Centre for Clinical Research