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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor.

Functional activity of N-methyl-D-aspartate (NMDA) receptors requires both glutamate binding and the binding of an endogenous coagonist that has been presumed to be glycine, although D-serine is a more potent agonist. Localizations of D-serine and it biosynthetic enzyme serine racemase approximate the distribution of NMDA receptors more closely than glycine. We now show that selective degradation of d-serine with D-amino acid oxidase greatly attenuates NMDA receptor-mediated neurotransmission as assessed by using whole-cell patch-clamp recordings or indirectly by using biochemical assays of the sequelae of NMDA receptor-mediated calcium flux. The inhibitory effects of the enzyme are fully reversed by exogenously applied D-serine, which by itself did not potentiate NMDA receptor-mediated synaptic responses. Thus, D-serine is an endogenous modulator of the glycine site of NMDA receptors and fully occupies this site at some functional synapses.[1]

References

  1. D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor. Mothet, J.P., Parent, A.T., Wolosker, H., Brady, R.O., Linden, D.J., Ferris, C.D., Rogawski, M.A., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
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