α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid receptors signaling complexes in Bergmann glia

Millán, Alejandro; Arias‐Montaño, José‐Antonio; Méndez, José Alfredo Tirado; Hernández‐Kelly, Luisa C.; Ortega, Arturo

doi:10.1002/jnr.20237

Cited by 13 publications

(19 citation statements)

References 33 publications

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“…6, both PKB and GSK3-b phosphorylation are still present in a Ca 2+ -free medium that contains 500 lM ethylenediaminotetraacetic acid (EDTA). These results are compatible with the fact that AMPA receptors activate the non-receptors tyrosine kinases Lyn and FAK and even become tyrosine phosphorylated in an ion-influx-independent manner [6,15]. Although the pharmacological characterization of the Glu response suggested an AMPA receptors-mediated effect, we decided to explore the possibility of a Glu-dependent release of Ca 2+ from intracellular stores.…”

Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationsupporting

confidence: 66%

“…The reported physical interaction of PI3-K with ionotropic Glu receptors in neurons and glial cells [6,19] as well as its Glu-dependent activation, prompted us to evaluate if the PKB/GS3K-b signaling pathway was being activated. A time and dose-dependence PKB phosphorylation could be unequivocally established after Glu (Figs.…”

Section: Discussionmentioning

confidence: 99%

“…*P < 0.001, **P < 0.01 (ANOVA) AMPA receptors. As already mentioned, in BGC, AMPA receptors once activated, become tyrosine phosphorylated and by these means interact and activate PI-3K [6]. Therefore, it was critical to evaluate if the increase in PKB and GSK3-b phosphorylation was dependent on PI-3K activity.…”

Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationmentioning

confidence: 99%

“…Although the identity of the tyrosine kinase involved in AMPA receptors phosphorylation has not been fully established, a role for Src has been suggested [6]. Therefore, we exposed the cultured cells to a 10 nM concentration of the Src inhibitor 4-amino-5-(4-chlorophenyl)-7-(tbutyl)pyrazolol [3,4-d]pyrimidine (PP2), previous to Glu.…”

Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationmentioning

confidence: 99%

“…Glu released from the parallel fibers depolarizes the BGC triggering not only a significant Ca 2+ influx but also a membrane to nuclei cascade that is involved in transcriptional regulation [5]. Interestingly, AMPA receptors are involved in this process and become tyrosine phosphorylated leading to the recruitment and activation of transduction molecules such as the focal adhesion kinase pp125 FAK and the phosphatidilinositol-3 kinase (PI-3K) [6].…”

Section: Introductionmentioning

confidence: 99%

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Glutamate Activates Protein Kinase B (PKB/Akt) through AMPA Receptors in Cultured Bergmann Glia Cells

et al. 2006

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Glutamate is involved in gene expression regulation in neurons and glial cells through the activation of a diverse array of signaling cascades. In Bergmann glia, Ca2+ -permeable alpha-hydroxy-5-methyl-4-isoazole-propionic acid (AMPA) receptors become tyrosine phosphorylated after ligand binding and by these means form multiprotein signaling complexes. Of the various proteins that associate to these receptors, the phosphatidylinositol 3-kinase (PI-3K) deserves special attention since D3-phosphorylated phosphoinositides are docking molecules for signaling proteins with a pleckstrin homology domain. In order to characterize the role of PI-3K in AMPA receptors signaling, in the present report we analyze the involvement of the serine/threonine protein kinase B in this process. Our results demonstrate an augmentation in protein kinase B phosphorylation and activity after glutamate exposure. Interestingly, the effect is independent of Ca2+ influx, but sensitive to Src blockers. Our present findings broaden our current knowledge of glial glutamate receptors signaling and their involvement glutamatergic neurotransmission.

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Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationmentioning

confidence: 99%

Section: Ampa Receptors Mediate Pkb and Gsk-b Phosphorylationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glutamate Activates Protein Kinase B (PKB/Akt) through AMPA Receptors in Cultured Bergmann Glia Cells

et al. 2006

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Glutamate activation of Oct-2 in cultured chick Bergmann glia cells: Involvement of NFκB

2005

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Glutamate, the major excitatory neurotransmitter in the central nervous system, is critically involved in gene expression regulation at the transcriptional and translational levels. Its activity through ionotropic as well as metabotropic receptors modifies the protein repertoire in neurons and glial cells. In avian cerebellar Bergmann glia cells, glutamate receptors trigger a diverse array of signaling cascades that include activity-dependent transcription factors such as the activator protein-1, the cAMP response-element binding protein, and Oct-2. We analyze the upstream regulatory elements involved in Oct-2 activation. Our results demonstrate that Ca2+ influx, protein kinase C, phosphatidylinositol-3 kinase, Src, and nuclear factor (NF)kappaB are involved in this signaling pathway. Our findings link alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor activation to a negative phase of chkbp gene regulation, controlled by NFkappaB.

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Glutamate transporters in the biology of malignant gliomas

Robert

Sontheimer

2013

Cell. Mol. Life Sci.

102

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Malignant gliomas are relentless tumors that offer a dismal clinical prognosis. They develop many biological advantages that allow them to grow and survive in the unique environment of the brain. The glutamate transporters System xc− and Excitatory Amino Acid Transporters (EAAT) are emerging as key players in the biology and malignancy of these tumors. Gliomas manipulate glutamate transporter expression and function to alter glutamate homeostasis in the brain, which supports their own growth, invasion, and survival. As a consequence, malignant cells are able to quickly destroy and invade surrounding normal brain. Recent findings are painting a larger picture of these transporters in glioma biology, and as such are providing opportunities for clinical intervention for patients. This review will detail the current understanding of glutamate transporters in the biology of malignant gliomas and highlight some of the unique aspects of these tumors that make them so devastating and difficult to treat.

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α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid receptors signaling complexes in Bergmann glia

Cited by 13 publications

References 33 publications

Glutamate Activates Protein Kinase B (PKB/Akt) through AMPA Receptors in Cultured Bergmann Glia Cells

Glutamate Activates Protein Kinase B (PKB/Akt) through AMPA Receptors in Cultured Bergmann Glia Cells

Glutamate activation of Oct-2 in cultured chick Bergmann glia cells: Involvement of NFκB

Glutamate transporters in the biology of malignant gliomas

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