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Glutamate activates PP125 FAK through AMPA/kainate receptors in Bergmann glia
Author(s) -
Millán Alejandro,
Aguilar Pablo,
Méndez J. Alfredo,
AriasMontaño JoséAntonio,
Ortega Arturo
Publication year - 2001
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10034
Subject(s) - kainate receptor , ampa receptor , glutamate receptor , neuroscience , receptor , chemistry , biology , biochemistry
Abstract 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 α‐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. J. Neurosci. Res. 66:723–729, 2001. © 2001 Wiley‐Liss, Inc.