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AII amacrine cells in the rabbit retina possess AMPA-, NMDA-, GABA-, and glycine-activated currents

Published online by Cambridge University Press:  23 June 2004

CHENGWEN ZHOU
Affiliation:
Department of Ophthalmology, University of Alabama at Birmingham, Birmingham
RAMON F. DACHEUX
Affiliation:
Department of Ophthalmology, University of Alabama at Birmingham, Birmingham

Abstract

Physiological properties of ligand-activated currents were characterized for morphologically identified AII amacrine cells in the rabbit retina by using whole-cell recordings in a superfused retina slice preparation. The AII amacrine cells were identified based on their distinct narrow-field, bistratified morphology. In the present study, the whole-cell recordings from AII amacrine cells synaptically isolated from presynaptic influences demonstrated the presence of glutamate AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid) receptors, but no kainate receptors. The presence of only AMPA receptors on rabbit AII amacrine cells is in contrast to an earlier study on rabbit AII amacrine cells by Bloomfield and Xin (2000), but consistent with previous studies on rat AII amacrine cells. In addition, NMDA (N-methyl-D-aspartate) -activated currents blocked by the NMDA antagonist D-AP7 (D-2-amino-7-phosphonoheptanoic acid) were found on the AII amacrine cells. These most likely extrasynaptic NMDA-activated currents were attenuated by the presence of Co2+ interacting with Mg2+ and Ca2+ as they competed for divalent cation-binding sites within the NMDA channel. AII amacrine cells also possessed GABA (γ-aminobutyric acid) -activated currents that were unaffected by the GABAC receptor antagonist TPMPA (1,2,5,6-tetrahydropyridine-4-yl methylphosphinic), but were completely blocked by the GABAA antagonist bicuculline. This indicates that the major inhibitory inputs were mediated by only GABAA receptors located directly on the AII amacrine cells. Furthermore, although the AII amacrine cells were glycinergic amacrine cells, they also possessed glycine-activated currents that may be mediated by autoreceptors.

Type
Research Article
Copyright
2004 Cambridge University Press

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