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D-Serine as a putative glial neurotransmitter

Published online by Cambridge University Press:  22 June 2005

ASIF K. MUSTAFA ,
PAUL M. KIM  and
SOLOMON H. SNYDER
ASIF K. MUSTAFA
Affiliation:
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore
PAUL M. KIM
Affiliation:
Department of Pharmacology and Molecular Science, Johns Hopkins University School of Medicine, Baltimore
SOLOMON H. SNYDER
Affiliation:
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore Department of Pharmacology and Molecular Science, Johns Hopkins University School of Medicine, Baltimore Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore
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Abstract

Abundant recent evidence favors a neurotransmitter/neuromodulator role for D-serine. D-serine is synthesized from L-serine by serine racemase in astrocytic glia that ensheath synapses, especially in regions of the brain that are enriched in NMDA-glutamate receptors. D-serine is more potent than glycine at activating the ‘glycine’ site of these receptors. Moreover, selective degradation of D-serine but not glycine by D-amino acid oxidase markedly reduces NMDA neurotransmission. D-serine appears to be released physiologically in response to activation by glutamate of AMPA-glutamate receptors on D-serine-containing glia. This causes glutamate-receptor-interacting protein, which binds serine racemase, to stimulate enzyme activity and D-serine release. Thus, glutamate triggers the release of D-serine so that the two amino acids can act together on postsynaptic NMDA receptors. D-serine also plays a role in neural development, being released from Bergmann glia to chemokinetically enhance the migration of granule cell cerebellar neurons from the external to the internal granular layer.

Keywords

α-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate receptorD-serineN-methyl-D-aspartate receptorserine racemase
Type
Research Article
Information
Neuron Glia Biology , Volume 1 , Issue 3 , August 2004 , pp. 275 - 281
Copyright
© Cambridge University Press 2005

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