Glutamate regulates Oct‐2 DNA‐binding activity through α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionate receptors in cultured chick Bergmann glia cells

Méndez, José Alfredo Tirado; López-Bayghen, Esther; Rojas, Fausto; Hernández, Marı́a Elena; Ortega, Alejandra

doi:10.1046/j.1471-4159.2003.02206.x

Cited by 10 publications

(26 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Through the use of Glu analogues we conclude that the Glu receptors involved are ionotropic of the AMPA subtype (Figs. 4,5). In terms of the signaling cascade, the effect is Ca 2+ -independent but sensitive to the Src inhibitor PP2, results which are in line with our previous findings regarding AMPA receptors tyrosine phosphorylation [6].…”

Section: Discussionsupporting

confidence: 90%

“…1). Moreover, PP2A activity depends on Ca 2+ [20], an event linked to AMPA receptors stimulation in cultured chick BGC [5]. Glu has been repeatedly reported to activate PKB in neuronal cells [21] but much less is known about its activity in glial cells.…”

Section: Discussionmentioning

confidence: 99%

“…The repertoire of glutamatergic receptors in these cells include both ionotropic as well as metabotropic receptors [3,4]. 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%

“…Binding of the p85 to a phosphorylated receptor promotes activation of p110 subunit. Activated PI3K generates D3-phosphorylated phosphoinositides, PtdIns [3,4] P2 and PtdIns [3][4][5] P3, a motif recognized by the pleckstrin homology domain present in several protein kinases.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 2006

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

et al. 2006

Self Cite

View full text Add to dashboard Cite

show abstract

“…Glu-dependent transcriptional regulation of the chicken kainate binding protein gene (chkbp) involves a complex Ca 2+ -dependent signaling with a differential time frame that either increases or represses transcription [15,16]. Both effects are dependent on the activation of AMPA receptors.…”

Section: Introductionmentioning

confidence: 99%

Glutamate-Dependent Transcriptional Regulation in Bergmann Glia Cells: Involvement of p38 MAP Kinase

et al. 2008

Self Cite

View full text Add to dashboard Cite

Glutamate (Glu) is the major excitatory neurotransmitter in the Central Nervous System (CNS). Ionotropic and metabotropic glutamate receptors (GluRs) are present in neurons and glial cells and are involved in gene expression regulation. Mitogen-activated proteins kinases (MAPK) are critical for all the membrane to nuclei signaling pathways described so far. In cerebellar Bergmann glial cells, glutamate-dependent transcriptional regulation is partially dependent on p42/44 MAPK activity. Another member of this kinase family, p38 MAPK is activated by non-mitogenic stimuli through its Thr180/Tyr182 phosphorylation and phosphorylates cytoplasmic and nuclear protein targets involved in translational and transcriptional events. Taking into consideration that the role of p38MAPK in glial cells is not well understood, we demonstrate here that glutamate increases p38 MAPK phosphorylation in a time and dose dependent manner in cultured chick cerebellar Bergmann glial cells (BGC). Moreover, p38 MAPK is involved in the glutamate-induced transcriptional activation in these cells. Ionotropic as well as metabotropic glutamate receptors participate in p38 MAPK activation. The present findings demonstrate the involvement of p38 MAPK in glutamate-dependent gene expression regulation in glial cells.

show abstract

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

2005

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Glutamate regulates Oct‐2 DNA‐binding activity through α‐amino‐3‐hydroxy‐5‐methylisoxazole‐4‐propionate receptors in cultured chick Bergmann glia cells

Cited by 10 publications

References 39 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-Dependent Transcriptional Regulation in Bergmann Glia Cells: Involvement of p38 MAP Kinase

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

Contact Info

Product

Resources

About