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D-Serine in Glia and Neurons Derives from 3-Phosphoglycerate Dehydrogenase
Open accessAbstract
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.
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“For instance, astrocytes and not neurons express the phosphoglycerate dehydrogenase involved in serine biosynthesis (Ehmsen et al., 2013), which branches off of the main glycolytic pathway.”
From Fueling thought: Management of glycolysis and oxidative phosphorylation in neuronal metabolism (2018) · cites this paper as Ehmsen et al., 2013
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NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor.
Mothet, J., Parent, A., Wolosker, H., Brady, R., Linden, D. J., Ferris, C., Rogawski, M., & Snyder, S. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.97.9.4926 · Cited by 1,164
Production and purification of lentiviral vectors
Tiscórnia, G., Singer, O., & Verma, I. M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.37 · Cited by 974
Glia-Derived d-Serine Controls NMDA Receptor Activity and Synaptic Memory
Panatier, A., Theodosis, D. T., Mothet, J.-P., Touquet, B., Pollegioni, L., Poulain, D. A., & Oliet, S. H. R. (2006) · Cell · doi:10.1016/j.cell.2006.02.051 · Cited by 934
Schell, M. J., Molliver, M. E., & Snyder, S. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3948 · Cited by 832
Wolosker, H., Blackshaw, S., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13409 · Cited by 811
Synaptic and Extrasynaptic NMDA Receptors Are Gated by Different Endogenous Coagonists
Papouin, T., Ladépêche, L., Ruel, J., Sacchi, S., Labasque, M., Hanini, M., Groc, L., Pollegioni, L., Mothet, J., & Oliet, S. H. R. (2012) · Cell · doi:10.1016/j.cell.2012.06.029 · Cited by 798
Purification of serine racemase: biosynthesis of the neuromodulator D-serine.
Wolosker, H., Sheth, K., Takahashi, M., Mothet, J., Brady, R., Ferris, C., & Snyder, S. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.2.721 · Cited by 505
NMDA receptors in clinical neurology: excitatory times ahead
Kalia, L. V., Kalia, S. K., & Salter, M. W. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70165-0 · Cited by 421
Schell, M. J., Brady Jr., R. O., Molliver, M. E., & Snyder, S. H. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-05-01604.1997 · Cited by 415 · cited 3×
“D-Serine localized to neurons and astrocytes As with Srr, reports of D-serine localizations have varied with descriptions of astrocytic (Schell et al., 1997; Kartvelishvily et al., 2006; Williams et al., 2006) and neuronal (Kartvelishvily et al., 2006) sites.”
BackgroundSelf-citationTargeted disruption of serine racemase affects glutamatergic neurotransmission and behavior
Basu, A. C., Tsai, G. E., Ma, C.-L., Ehmsen, J. T., Mustafa, A. K., Han, L., Jiang, Z. I., Benneyworth, M. A., Froimowitz, M., LANGE, N. D., et al. (2008) · Molecular Psychiatry · doi:10.1038/mp.2008.130 · Cited by 340
Hashimoto, A., Nishikawa, T., Oka, T., Takahashi, K., & Hayashi, T. (1992) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/0378-4347(92)80300-f · Cited by 305
l-Serine in disease and development
de Koning, T. J., Snell, K., Durán, M., Berger, R., Poll‐The, B. T., & Surtees, R. A. H. (2003) · Biochemical Journal · doi:10.1042/bj20021785 · Cited by 304
Neuron-derived D-Serine Release Provides a Novel Means to Activate N-Methyl-D-aspartate Receptors
Kartvelishvily, E., Shleper, M., Balan, L., Dumin, E., & Wolosker, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512927200 · Cited by 283
Serine racemase is predominantly localized in neurons in mouse brain
Miya, K., Inoue, R., Takata, Y., Abe, M., Natsume, R., Sakimura, K., Hongou, K., Miyawaki, T., & Mori, H. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21822 · Cited by 251
Shleper, M., Kartvelishvily, E., & Wolosker, H. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3190-05.2005 · Cited by 227
GFAP-positive progenitor cells produce neurons and oligodendrocytes throughout the CNS
Casper, K. B., & McCarthy, K. D. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.12.006 · Cited by 227
Yamasaki, M., Yamada, K., Furuya, S., Mitoma, J., Hirabayashi, Y., & Watanabe, M. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07691.2001 · Cited by 215
Furuya, S., Tabata, T., Mitoma, J., Yamada, K., Yamasaki, M., Makino, A., Yamamoto, T., Watanabe, M., Kano, M., & Hirabayashi, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200364497 · Cited by 197
Benneyworth, M. A., Li, Y., Basu, A. C., Bolshakov, V. Y., & Coyle, J. T. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-012-9808-4 · Cited by 153
Yang, J. H., Wada, A., Yoshida, K., Miyoshi, Y., Sayano, T., Esaki, K., Kinoshita, M. O., Tomonaga, S., Azuma, N., Watanabe, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.187443 · Cited by 153
Williams, S. M., Díaz, C., Macnab, L. T., Sullivan, R., & Pow, D. V. (2005) · Glia · doi:10.1002/glia.20300 · Cited by 126
Serine Racemase Deletion Protects Against Cerebral Ischemia and Excitotoxicity
Mustafa, A. K., Ahmad, A. S., Zeynalov, E., Gazi, S. K., Sikka, G., Ehmsen, J. T., Barrow, R. K., Coyle, J. T., Snyder, S. H., & Doré, S. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4297-09.2010 · Cited by 115
Grant, S. L., Shulman, Y., Tibbo, P. G., Hampson, D. R., & Baker, G. B. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.07.022 · Cited by 108
Kawakami, Y., Yoshida, K., Yang, J. H., Suzuki, T., Azuma, N., Sakai, K., Hashikawa, T., Watanabe, M., Yasuda, K., Kuhara, S., et al. (2008) · Neuroscience Research · doi:10.1016/j.neures.2008.12.002 · Cited by 32
Sofroniew, M. V. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-452-0_35 · Cited by 20
An Enzymatic-HPLC Assay to Monitor Endogenous d-Serine Release from Neuronal Cultures
Radzishevsky, I. S., & Wolosker, H. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-331-8_19 · Cited by 10
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“…cancer cells, astrocytes perform glycolysis not primarily for energy but rather for anabolic biosynthesis: For instance, astrocytes and not neurons express the phosphoglycerate dehydrogenase involved in serine biosynthesis (Ehmsen et al., 2013), which branches off of the main glycolytic pathway.”
BackgroundDouce, J. L., Maugard, M., Veran, J., Matos, M., Jégo, P., Vigneron, P.-A., Faivre, É., Toussay, X., Vandenberghe, M. E., Balbastre, Y., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.004 · Cited by 336
Metadata
- Authors
- Ehmsen, J. T., Ma, T. M., Sason, H., Rosenberg, D., Ogo, T., Furuya, S., Snyder, S. H., & Wolosker, H.
- Affiliations
- Johns Hopkins University (US)
- Technion – Israel Institute of Technology (IL)
- Kyushu University (JP)
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2013-07-24
- Volume
- 33
- Issue
- 30
- Pages
- 12464-12469
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3721849
- OpenAlex
- W2055652253
- Cited by
- 118
- References
- 27
- Citations by year
- 2026: 4 · 2025: 11 · 2024: 9 · 2023: 8 · 2022: 5 · 2021: 7 · 2020: 11 · 2019: 8 · 2018: 10 · 2017: 13 · 2016: 13 · 2015: 6 · 2014: 12 · 2013: 1
- FWCI
- 4.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- International Mental Health Research Organization
- Legacy Heritage Fund
- Israel Science Foundation
- National Institutes of Health (MH18501)
- Japan Society for the Promotion of Science (18300125, 22380078)
- National Institute of Mental Health (R01MH018501, R37MH018501, MH-18501)
- National Institute of Neurological Disorders and Stroke (NS050275)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Biological Psychiatry › Tryptophan and brain disorders
- Keywords
- D-serine, 3-phosphoglycerate dehydrogenase, serine racemase, NMDA receptor, L-serine biosynthesis, astrocytes, neurons, neuron-glia interactions, transgenic mice
- MeSH terms
- Serine Racemase, Animals, Astrocytes, Cerebral Cortex, Female, Glucose, Male, Mice, Transgenic, Synaptic Transmission, Neurons, Promoter Regions, Genetic, Serine, Racemases and Epimerases, Green Fluorescent Proteins, Phosphoglycerate Dehydrogenase, Mice, Primary Cell Culture
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