Glutamate activates PP125(FAK) through AMPA/kainate receptors in Bergmann glia

Glial glutamate receptors are likely to play a role in plasticity, learning, and memory and in a number of neuropathologies. An enhanced glutamate-dependent tyrosine phosphorylation has been detected in such processes. Using primary cultures of chick Bergmann glia cells and chick cerebellar slices,...

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Bibliographic Details
Published in:Journal of neuroscience research 2001-11, Vol.66 (4), p.723-729
Main Authors: Millán, A, Aguilar, P, Méndez, J A, Arias-Montaño, J A, Ortega, A
Format: Article
Language:English
Subjects:
Animals
Antibodies - pharmacology
Cell Adhesion - drug effects
Cell Adhesion - physiology
Cell Differentiation - drug effects
Cell Differentiation - physiology
Cells, Cultured - cytology
Cells, Cultured - drug effects
Cells, Cultured - metabolism
Cerebellum - drug effects
Cerebellum - embryology
Cerebellum - metabolism
Chick Embryo
Cytoskeleton - drug effects
Cytoskeleton - metabolism
Dose-Response Relationship, Drug
Focal Adhesion Protein-Tyrosine Kinases
Glutamic Acid - metabolism
Glutamic Acid - pharmacology
Immunoblotting
Neuroglia - cytology
Neuroglia - drug effects
Neuroglia - metabolism
Organ Culture Techniques
Phosphatidylinositol 3-Kinases - metabolism
Phosphorylation - drug effects
Precipitin Tests
Protein-Tyrosine Kinases - antagonists & inhibitors
Protein-Tyrosine Kinases - drug effects
Protein-Tyrosine Kinases - metabolism
Receptors, AMPA - drug effects
Receptors, AMPA - metabolism
Receptors, Kainic Acid - drug effects
Receptors, Kainic Acid - metabolism
Signal Transduction - drug effects
Signal Transduction - physiology
Tyrosine - metabolism
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Summary:Glial glutamate receptors are likely to play a role in plasticity, learning, and memory and in a number of neuropathologies. An enhanced glutamate-dependent tyrosine phosphorylation has been detected in such processes. Using primary cultures of chick Bergmann glia cells and chick cerebellar slices, we addressed whether glial glutamate receptors can activate the nonreceptor tyrosine kinase pp125 focal adhesion kinase (pp125(FAK)). A dose- and time-dependent tyrosine phosphorylation of pp125(FAK) was found in both preparations upon glutamate treatment. This effect was mediated through alpha-amino-3-hydroxy-5-methyl-4-isoaxazolepropionate (AMPA)/kainate (KA) receptors, as shown by its inhibition by the specific antagonists 2,3-dioxo-6-nitro-1,2,3,4-tetrahydrobenzo[f]quinoxaline-7- sulfonamide (NBQX) and 6,7-dinitroquinoxaline-2,3-dione (DNQX) and the lack of effect of metabotropic agonists. FAK tyrosine phosphorylation was dependent on phosphatidylinositol 3-kinase activity. As expected, an increase in pp125(FAK) catalytic activity was found upon glutamate treatment. Immunprecipitation experiments demonstrated that FAK associates with ionotropic glutamate receptors. Taken together, these results suggest a role for glial glutamate receptors in cytoskeletal rearrengments and focal adhesion contact formation and provide new insight into the signaling transactions elicited by this neurotransmitter in glial cells.
ISSN:0360-4012
1097-4547
DOI:10.1002/jnr.10034