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(Investigative Ophthalmology and Visual Science. 2005;46:3570-3577.)
© 2005 by The Association for Research in Vision and Ophthalmology, Inc.
DOI:  10.1167/iovs.04-1398
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Cell-specific Expression of N-Methyl-D-Aspartate Receptor Subunits in Müller Glia and Neurons from the Chick Retina

Mónica Lamas, Irene Lee-Rivera, and Ana María López-Colomé

From the Instituto de Fisiología Celular, Departamento de Neurociencias, Universidad Nacional Autónoma de México (UNAM).

PURPOSE. Functional N-methyl-D-aspartate (NMDA) receptors (NMDARs) in Müller glia may influence glutamate neurotransmission through feedback loops between glia and neurons. The physiologic properties of NMDARs derive from the subunit composition of the tetrameric receptor. We characterized glycine binding to the NMDAR coagonist site in Müller cell membranes and determined NMDAR subunit expression in chick Müller glia compared with retinal neurons to make predictions about the heteromeric assembly of NMDARs.

METHODS. Kinetic and pharmacologic properties of the glycine coagonist site were determined by radiolabeled ligand binding to membrane preparations from chick Müller glia and retinal neurons in primary culture. The molecular composition of NMDARs was analyzed by RT-PCR amplification and Western blotting.

RESULTS. The NMDAR coagonist site in Müller cell membranes has 5-fold lower affinity for glycine and 30-fold lower affinity for D-serine compared with values obtained for synaptic membranes from whole retina and with reported values in brain tissue. NR1 subunit N-terminal and C-terminal splice-variant expression also differs in Müller cells and retinal neurons.

CONCLUSIONS. Pharmacologic characteristics of NMDAR coagonist-site differ in Müller glia and neurons from the retina, in agreement with the distinct subunit expression profile found. Whereas NMDARs in Müller glia contain exclusively exon 5 that lacks NR1 subunits, receptors in distinct subtypes of neurons may contain NR1 with or without exon 5, suggesting a cell-specific assembly of the NMDAR complex. Structural differences in NMDARs could underlie the differential participation of neurons and glia in the physiologic control of glutamate transmission in the retina.




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K. Holmgaard, C. Aalkjaer, J. D. C. Lambert, and T. Bek
N-Methyl-D-Aspartic Acid Causes Relaxation of Porcine Retinal Arterioles through an Adenosine Receptor-Dependent Mechanism
Invest. Ophthalmol. Vis. Sci., October 1, 2008; 49(10): 4590 - 4594.
[Abstract] [Full Text] [PDF]


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