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

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Abstract

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 α-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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Acknowledgments

The authors acknowledge the technical assistance of Luis Cid and Blanca Ibarra. This work was supported by a grant from Conacyt-México (43164-Q) to A.O. Conacyt-México supports M.M. and M.E.G.M. through doctoral fellowships.

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Correspondence to Arturo Ortega.

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Special issue dedicated to Miklós Palkovits.

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Morales, M., González-Mejía, M.E., Bernabé, A. et al. Glutamate Activates Protein Kinase B (PKB/Akt) through AMPA Receptors in Cultured Bergmann Glia Cells. Neurochem Res 31, 423–429 (2006). https://doi.org/10.1007/s11064-005-9034-2

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