A new GLT1 splice variant: cloning and immunolocalization of GLT1c in the mammalian retina and brain

Rauen, Thomas; Wiessner, Michael; Sullivan, Rodney N.; Lee, Aven; Pow, David V.

doi:10.1016/j.neuint.2004.04.006

Cited by 94 publications

(87 citation statements)

References 33 publications

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“…[31][32][33][34][35][36][37][38] Figure 1 schematically illustrates the locations of antibody epitopes for normally spliced GLAST and the exon-skipping forms of GLAST (GLAST1a and GLAST1b). Multiple GLT1 antisera were used in this study (Figure 2).…”

Section: Primary Antibodies Against Transportersmentioning

confidence: 99%

“…They included antisera directed against the alternate splicings of the extreme carboxyl-terminal region of the GLT1 protein (denoted as GLT1a, GLT1b and GLT1c). 36 Antisera against an amino-terminal epitope (residues 12-26) and an internal epitope (residues 497-508), both of which should be present in all known forms of GLT1, were also investigated. The EAAC1 antibody was directed against the carboxyl-terminal region of the protein (KSYVNGGFAVDKSDTISFTQTSQF), as was the antibody against EAAT4 (KGASRGRGGNESAM).…”

Section: Primary Antibodies Against Transportersmentioning

confidence: 99%

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Expression of multiple glutamate transporter splice variants in the rodent testis

Lee¹,

Anderson²,

Barnett³

et al. 2010

Asian J Androl

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Glutamate is a regulated molecule in the mammalian testis. Extracellular regulation of glutamate in the body is determined largely by the expression of plasmalemmal glutamate transporters. We have examined by PCR, western blotting and immunocytochemistry the expression of a panel of sodium-dependent plasmalemmal glutamate transporters in the rat testis. Proteins examined included: glutamate aspartate transporter (GLAST), glutamate transporter 1 (GLT1), excitatory amino acid carrier 1 (EAAC1), excitatory amino acid transporter 4 (EAAT4) and EAAT5. We demonstrate that many of the glutamate transporters in the testis are alternately spliced. GLAST is present as exon-3-and exon-9-skipping forms. GLT1 was similarly present as the alternately spliced forms GLT1b and GLT1c, whereas the abundant brain form (GLT1a) was detectable only at the mRNA level. EAAT5 was also strongly expressed, whereas EAAC1 and EAAT4 were absent. These patterns of expression were compared with the patterns of endogenous glutamate localization and with patterns of D-aspartate accumulation, as assessed by immunocytochemistry. The presence of multiple glutamate transporters in the testis, including unusually spliced forms, suggests that glutamate homeostasis may be critical in this organ. The apparent presence of many of these transporters in the testis and sperm may indicate a need for glutamate transport by such cells.

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Section: Primary Antibodies Against Transportersmentioning

confidence: 99%

Section: Primary Antibodies Against Transportersmentioning

confidence: 99%

Expression of multiple glutamate transporter splice variants in the rodent testis

Lee¹,

Anderson²,

Barnett³

et al. 2010

Asian J Androl

Self Cite

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show abstract

“…A third functional GLT1 variant encoding yet another novel C-terminus, referred to as GLT1c, was recently identified in the rat and human retina. 27 This splice form includes exons 1 through 10 and then terminates with a small alternate exon spliced in from intron 10. The novel exon encodes 11 unique amino acids at the C-terminus of the protein with a PDZbinding domain, reminiscent of GLT1b.…”

Section: Alternative Splicing Of Glt1mentioning

confidence: 99%

EAAT2 regulation and splicing: relevance to psychiatric and neurological disorders

Lauriat

McInnes

2007

Mol Psychiatry

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The excitatory amino acid transporter 2 (EAAT2) is responsible for the majority of glutamate uptake in the brain and its dysregulation has been associated with multiple psychiatric and neurological disorders. However, investigation of this molecule has been complicated by its complex pattern of alternative splicing, including three coding isoforms and multiple 5 0 -and 3 0 -UTRs that may have a regulatory function. It is likely that these sequences permit modulation of EAAT2 expression with spatial, temporal and or activity-dependent specificity; however, few studies have attempted to delineate the function of these sequences. Additionally, there are problems with the use of antibodies to study protein localization, possibly due to posttranslational modification of critical amino acid residues. This review describes what is currently known about the regulation of EAAT2 mRNA and protein isoforms and concludes with a summary of studies showing dysregulation of EAAT2 in psychiatric and neurological disorders. EAAT2 has been either primarily or secondarily implicated in a multitude of neuropsychiatric diseases in addition to the normal physiology of learning and memory. Thus, this molecule represents an intriguing therapeutic target once we improve our understanding of how it is regulated under normal conditions.

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“…GLT-1a appears to be associated mainly with a population of amacrine cells and bipolor cells, whereas GLT-1b is associated with cone photoreceptors and subpopulations of bipolar cells [52,53]. GLT-1c is normally only expressed by the photoreceptors in the mammalian retina [54].…”

Section: B Glt-1mentioning

confidence: 99%

Excitotoxicity and Glaucoma

Ishikawa¹,

Yoshitomi²,

Izumi³

2014

Ophthalmology - Current Clinical and Research Updates

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A new GLT1 splice variant: cloning and immunolocalization of GLT1c in the mammalian retina and brain

Cited by 94 publications

References 33 publications

Expression of multiple glutamate transporter splice variants in the rodent testis

Expression of multiple glutamate transporter splice variants in the rodent testis

EAAT2 regulation and splicing: relevance to psychiatric and neurological disorders

Excitotoxicity and Glaucoma

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