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

Research output: Contribution to journalArticlepeer-review


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 (US)
Pages (from-to)12464-12469
Number of pages6
JournalJournal of Neuroscience
Issue number30
StatePublished - 2013

ASJC Scopus subject areas

  • Neuroscience(all)


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