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 journalArticle

56 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

Fingerprint

Phosphoglycerate Dehydrogenase
Neuroglia
Serine
Neurons
Enzymes
Synaptic Transmission
Transgenic Mice
Ligands

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Cite this

Ehmsen, J. T., Ma, T. M., Sason, H., Rosenberg, D., Ogo, T., Furuya, S., ... 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

D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase. / Ehmsen, Jeffrey T.; Ma, Ting Martin; Sason, Hagit; Rosenberg, Dina; Ogo, Tadashi; Furuya, Shigeki; Snyder, Solomon H.; Wolosker, Herman.

In: Journal of Neuroscience, Vol. 33, No. 30, 30.07.2013, p. 12464-12469.

Research output: Contribution to journalArticle

Ehmsen, JT, Ma, TM, Sason, H, Rosenberg, D, Ogo, T, Furuya, S, Snyder, SH & Wolosker, H 2013, 'D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase', Journal of Neuroscience, vol. 33, no. 30, pp. 12464-12469. https://doi.org/10.1523/JNEUROSCI.4914-12.2013
Ehmsen, Jeffrey T. ; Ma, Ting Martin ; Sason, Hagit ; Rosenberg, Dina ; Ogo, Tadashi ; Furuya, Shigeki ; Snyder, Solomon H. ; Wolosker, Herman. / D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase. In: Journal of Neuroscience. 2013 ; Vol. 33, No. 30. pp. 12464-12469.
@article{b4e2890b59e4454e9afe6ea81ff592c0,
title = "D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase",
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.",
author = "Ehmsen, {Jeffrey T.} and Ma, {Ting Martin} and Hagit Sason and Dina Rosenberg and Tadashi Ogo and Shigeki Furuya and Snyder, {Solomon H.} and Herman Wolosker",
year = "2013",
month = "7",
day = "30",
doi = "10.1523/JNEUROSCI.4914-12.2013",
language = "English",
volume = "33",
pages = "12464--12469",
journal = "Journal of Neuroscience",
issn = "0270-6474",
publisher = "Society for Neuroscience",
number = "30",

}

TY - JOUR

T1 - D-Serine in glia and neurons derives from 3-phosphoglycerate dehydrogenase

AU - Ehmsen, Jeffrey T.

AU - Ma, Ting Martin

AU - Sason, Hagit

AU - Rosenberg, Dina

AU - Ogo, Tadashi

AU - Furuya, Shigeki

AU - Snyder, Solomon H.

AU - Wolosker, Herman

PY - 2013/7/30

Y1 - 2013/7/30

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84880602282&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84880602282&partnerID=8YFLogxK

U2 - 10.1523/JNEUROSCI.4914-12.2013

DO - 10.1523/JNEUROSCI.4914-12.2013

M3 - Article

C2 - 23884950

AN - SCOPUS:84880602282

VL - 33

SP - 12464

EP - 12469

JO - Journal of Neuroscience

JF - Journal of Neuroscience

SN - 0270-6474

IS - 30

ER -