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Excitatory amino acid-induced AP-1 DNA binding activity in Müller glia
A M López-Colomé1, J Murbartián, A Ortega
1Instituto de Fisiología Celular-UNAM, Mexico.
Abstract:
The effect of L-glutamate (L-Glu) and its structural analogs N-methyl-D-aspartate (NMDA), quisqualate (QA), and kainate (KA) on the DNA binding activity of the Activator Protein 1 (AP-1) and the Ca2+/cAMP Responsive Element Binding Protein (CREB) families of transcription factors was examined in cultured chick retinal Müller glia cells. L-Glu, NMDA, and KA evoked a dose and time dependent increase in AP-1 DNA binding activity and had no effect on CREB binding. The order of potency for stimulating AP-1 DNA binding was NMDA > or = Glu > KA >> QA. L-Glu responses were partially blocked by 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) and by 3-[RS)-2-carboxypiperazin-4-yl)]-propyl-1-phosphonate (CPP) indicating that the increase in DNA binding is mediated both by an alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA)/low affinity KA and a NMDA subtypes of L-Glu receptors. Since Müller glia L-Glu receptors are probably mediators of the efficacy of the excitatory transmission in the retina, the present findings suggest that a stimulus-transcription coupling triggered by L-Glu in the glial cells might have a role in the long-term modulation of these synapses.