QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (59) Citing Articles via Google Scholar Google Scholar Articles by Yamasaki, M. Articles by Watanabe, M. Search for Related Content PubMed PubMed Citation Articles by Yamasaki, M. Articles by Watanabe, M. Pubmed/NCBI databases Gene GEO Profiles HomoloGene Protein UniGene Compound via MeSH Substance via MeSH Hazardous Substances DB L-SERINE

 Previous Article  |  Next Article 

The Journal of Neuroscience, October 1, 2001, 21(19):7691-7704

3-Phosphoglycerate Dehydrogenase, a Key Enzyme for L-Serine Biosynthesis, Is Preferentially Expressed in the Radial Glia/Astrocyte Lineage and Olfactory Ensheathing Glia in the Mouse Brain

Miwako Yamasaki¹, Keiko Yamada¹, Shigeki Furuya², Junya Mitoma³, Yoshio Hirabayashi², and Masahiko Watanabe¹

¹ Department of Anatomy, Hokkaido University School of Medicine, Sapporo 060-8638, Japan, ² Neuronal Circuit Mechanisms Research Group, The Institute of Physical and Chemical Research (RIKEN), Brain Science Institute, Wako, Saitama 351-0198, Japan, and ³  Glycobiology Program, The Burnham Institute, La Jolla, California 92037

L-Serine is synthesized from glycolytic intermediate 3-phosphoglycerate and is an indispensable precursor for the synthesis of proteins, membrane lipids, nucleotides, and neuroactive amino acids D-serine and glycine. We have recently shown that L-serine and its interconvertible glycine act as Bergmann glia-derived trophic factors for cerebellar Purkinje cells. To investigate whether such a metabolic neuron-glial relationship is fundamental to the developing and adult brain, we examined by in situ hybridization and immunohistochemistry the cellular expression of 3-phosphoglycerate dehydrogenase (3PGDH), the initial step enzyme for de novo L-serine biosynthesis in animal cells. At early stages when the neural wall consists exclusively of the ventricular zone, neuroepithelial stem cells expressed 3PGDH strongly and homogeneously. Thereafter, 3PGDH expression was downregulated and eventually disappeared in neuronal populations, whereas its high expression was transmitted to the radial glia and later to astrocytes in the gray and white matters. In addition, 3PGDH was highly expressed throughout development in the olfactory ensheathing glia, a specialized supporting cell that thoroughly ensheathes olfactory nerves. These results establish a fundamental link of the radial glia/astrocyte lineage and olfactory ensheathing glia to L-serine biosynthesis in the brain. We discuss this finding in the context of the hypothesis that 3PGDH expression in these glia cells contributes to energy metabolism in differentiating and differentiated neurons and other glia cells, which are known to be vulnerable to energy loss.

Key words: 3-phosphoglycerate dehydrogenase; L-serine; astrocyte; olfactory ensheathing glia; brain; mouse; development; immunohistochemistry; in situ hybridization

---

Copyright © 2001 Society for Neuroscience  0270-6474/01/21197691-14$05.00/0

This article has been cited by other articles:

				Y. Horibata and Y. Hirabayashi Identification and characterization of human ethanolaminephosphotransferase1 J. Lipid Res., March 1, 2007; 48(3): 503 - 508. [Abstract] [Full Text] [PDF]

				E. Kartvelishvily, M. Shleper, L. Balan, E. Dumin, and H. Wolosker Neuron-derived D-Serine Release Provides a Novel Means to Activate N-Methyl-D-aspartate Receptors J. Biol. Chem., May 19, 2006; 281(20): 14151 - 14162. [Abstract] [Full Text] [PDF]

				T. Yoshida, M. Fukaya, M. Uchigashima, E. Miura, H. Kamiya, M. Kano, and M. Watanabe Localization of diacylglycerol lipase-alpha around postsynaptic spine suggests close proximity between production site of an endocannabinoid, 2-arachidonoyl-glycerol, and presynaptic cannabinoid CB1 receptor. J. Neurosci., May 3, 2006; 26(18): 4740 - 4751. [Abstract] [Full Text] [PDF]

				X. Hu, D. Friedman, S. Hill, R. Caprioli, W. Nicholson, A. C Powers, L. Hunter, and L. E Limbird Proteomic exploration of pancreatic islets in mice null for the {alpha}2A adrenergic receptor J. Mol. Endocrinol., August 1, 2005; 35(1): 73 - 88. [Abstract] [Full Text] [PDF]

				K. Yoshida, S. Furuya, S. Osuka, J. Mitoma, Y. Shinoda, M. Watanabe, N. Azuma, H. Tanaka, T. Hashikawa, S. Itohara, et al. Targeted Disruption of the Mouse 3-Phosphoglycerate Dehydrogenase Gene Causes Severe Neurodevelopmental Defects and Results in Embryonic Lethality J. Biol. Chem., January 30, 2004; 279(5): 3573 - 3577. [Abstract] [Full Text] [PDF]

				K. Sakai, H. Shimizu, T. Koike, S. Furuya, and M. Watanabe Neutral Amino Acid Transporter ASCT1 Is Preferentially Expressed in L-Ser-Synthetic/Storing Glial Cells in the Mouse Brain with Transient Expression in Developing Capillaries J. Neurosci., January 15, 2003; 23(2): 550 - 560. [Abstract] [Full Text] [PDF]

				S. Pind, E. Slominski, J. Mauthe, K. Pearlman, K. J. Swoboda, J. A. Wilkins, P. Sauder, and M. R. Natowicz V490M, a Common Mutation in 3-Phosphoglycerate Dehydrogenase Deficiency, Causes Enzyme Deficiency by Decreasing the Yield of Mature Enzyme J. Biol. Chem., February 22, 2002; 277(9): 7136 - 7143. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help