D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase

Jeffrey T. Ehmsen, Ting Martin Ma, Hagit Sason, Dina Rosenberg, Tadashi Ogo, Shigeki Furuya, Solomon H. Snyder, Herman Wolosker

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61 Citations (Scopus)

Abstract

D-Serine is an endogenous ligand for NMDARs generated from L-serine by the enzyme serine racemase (Srr). Both neuronal and glial localizations have been reported for D-serine and Srr. 3-Phosphoglycerate dehydrogenase is an exclusively astrocytic enzyme that catalyzes the first committed step of L-serine biosynthesis. Using transgenic mice expressing enhanced green fluorescent protein under the Srr promoter and mice with targeted deletion of Srr or 3-Phosphoglycerate dehydrogenase, we demonstrate predominantly neuronal sources of D-serine dependent on astrocytic supply of L-serine. These findings clarify the cellular basis for the regulation of NMDAR neurotransmission by D-serine.

Original languageEnglish
Pages (from-to)12464-12469
Number of pages6
JournalJournal of Neuroscience
Volume33
Issue number30
DOIs
Publication statusPublished - Jul 30 2013

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

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    Ehmsen, J. T., Ma, T. M., Sason, H., Rosenberg, D., Ogo, T., Furuya, S., Snyder, S. H., & Wolosker, H. (2013). D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase. Journal of Neuroscience, 33(30), 12464-12469. https://doi.org/10.1523/JNEUROSCI.4914-12.2013