Novel neuroglial and glioglial relationships mediated by L-serine metabolism

Shigeki Furuya, Masahiko Watanabe

研究成果: ジャーナルへの寄稿評論記事

47 引用 (Scopus)

抄録

L-Serine is a non-essential amino acid that can be synthesized in the body. It derives from an intermediate of the glycolytic pathway, 3-phosphoglycerate, and utilized for the syntheses of proteins, other amino acids, membrane lipids, heme, and nucleotides. Emerging evidence indicates that L-serine functions as a glia-derived trophic factor, which strongly promotes the survival and differentiation of cultured neurons. L-Serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase (3PGDH) and small neutral amino acid transporter ASCT1 have been revealed to be expressed preferentially in the radial glia-astrocyte lineage and olfactory ensheathing glia of both adult and developing rodent brains. In contrast, these biosynthetic and transporter molecules for L-serine are faint or undetectable in neurons and phagocytic cells. In this review, we summarize recent progress to propose that L-serine synthesis in these glial cells and its supply to nearby neurons and other glia constitute a novel metabolic unit in the brain. Based on these neuroglial and glioglial relationships, glucose in neurons and phogocytes can be strategically used for energy production, while a variety of L-serine-derived biomolecules required for their proliferaton, survival, differentiation, and function are synthesized in and supplied from the radial glia-astrocyte lineage and olfactory ensheathing glia. A transient capillary expression of ASCT1 in fetal and neonatal brains further suggests that, in addition to the glia-borne L-serine, an active transport of blood-borne L-serine would play an essential role in neural development.

元の言語英語
ページ(範囲)109-121
ページ数13
ジャーナルArchives of Histology and Cytology
66
発行部数2
DOI
出版物ステータス出版済み - 5 1 2003
外部発表Yes

Fingerprint

Neuroglia
Serine
Neurons
Astrocytes
Phosphoglycerate Dehydrogenase
Brain
Neutral Amino Acid Transport Systems
Amino Acids
Active Biological Transport
Phagocytes
Membrane Lipids
Heme
Rodentia
Nucleotides
Glucose
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Histology

これを引用

Novel neuroglial and glioglial relationships mediated by L-serine metabolism. / Furuya, Shigeki; Watanabe, Masahiko.

:: Archives of Histology and Cytology, 巻 66, 番号 2, 01.05.2003, p. 109-121.

研究成果: ジャーナルへの寄稿評論記事

@article{9d79e5e0f3c74554bce917c33009311b,
title = "Novel neuroglial and glioglial relationships mediated by L-serine metabolism",
abstract = "L-Serine is a non-essential amino acid that can be synthesized in the body. It derives from an intermediate of the glycolytic pathway, 3-phosphoglycerate, and utilized for the syntheses of proteins, other amino acids, membrane lipids, heme, and nucleotides. Emerging evidence indicates that L-serine functions as a glia-derived trophic factor, which strongly promotes the survival and differentiation of cultured neurons. L-Serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase (3PGDH) and small neutral amino acid transporter ASCT1 have been revealed to be expressed preferentially in the radial glia-astrocyte lineage and olfactory ensheathing glia of both adult and developing rodent brains. In contrast, these biosynthetic and transporter molecules for L-serine are faint or undetectable in neurons and phagocytic cells. In this review, we summarize recent progress to propose that L-serine synthesis in these glial cells and its supply to nearby neurons and other glia constitute a novel metabolic unit in the brain. Based on these neuroglial and glioglial relationships, glucose in neurons and phogocytes can be strategically used for energy production, while a variety of L-serine-derived biomolecules required for their proliferaton, survival, differentiation, and function are synthesized in and supplied from the radial glia-astrocyte lineage and olfactory ensheathing glia. A transient capillary expression of ASCT1 in fetal and neonatal brains further suggests that, in addition to the glia-borne L-serine, an active transport of blood-borne L-serine would play an essential role in neural development.",
author = "Shigeki Furuya and Masahiko Watanabe",
year = "2003",
month = "5",
day = "1",
doi = "10.1679/aohc.66.109",
language = "English",
volume = "66",
pages = "109--121",
journal = "Archives of Histology and Cytology",
issn = "0914-9465",
publisher = "Japan Society of Histological Documentation",
number = "2",

}

TY - JOUR

T1 - Novel neuroglial and glioglial relationships mediated by L-serine metabolism

AU - Furuya, Shigeki

AU - Watanabe, Masahiko

PY - 2003/5/1

Y1 - 2003/5/1

N2 - L-Serine is a non-essential amino acid that can be synthesized in the body. It derives from an intermediate of the glycolytic pathway, 3-phosphoglycerate, and utilized for the syntheses of proteins, other amino acids, membrane lipids, heme, and nucleotides. Emerging evidence indicates that L-serine functions as a glia-derived trophic factor, which strongly promotes the survival and differentiation of cultured neurons. L-Serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase (3PGDH) and small neutral amino acid transporter ASCT1 have been revealed to be expressed preferentially in the radial glia-astrocyte lineage and olfactory ensheathing glia of both adult and developing rodent brains. In contrast, these biosynthetic and transporter molecules for L-serine are faint or undetectable in neurons and phagocytic cells. In this review, we summarize recent progress to propose that L-serine synthesis in these glial cells and its supply to nearby neurons and other glia constitute a novel metabolic unit in the brain. Based on these neuroglial and glioglial relationships, glucose in neurons and phogocytes can be strategically used for energy production, while a variety of L-serine-derived biomolecules required for their proliferaton, survival, differentiation, and function are synthesized in and supplied from the radial glia-astrocyte lineage and olfactory ensheathing glia. A transient capillary expression of ASCT1 in fetal and neonatal brains further suggests that, in addition to the glia-borne L-serine, an active transport of blood-borne L-serine would play an essential role in neural development.

AB - L-Serine is a non-essential amino acid that can be synthesized in the body. It derives from an intermediate of the glycolytic pathway, 3-phosphoglycerate, and utilized for the syntheses of proteins, other amino acids, membrane lipids, heme, and nucleotides. Emerging evidence indicates that L-serine functions as a glia-derived trophic factor, which strongly promotes the survival and differentiation of cultured neurons. L-Serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase (3PGDH) and small neutral amino acid transporter ASCT1 have been revealed to be expressed preferentially in the radial glia-astrocyte lineage and olfactory ensheathing glia of both adult and developing rodent brains. In contrast, these biosynthetic and transporter molecules for L-serine are faint or undetectable in neurons and phagocytic cells. In this review, we summarize recent progress to propose that L-serine synthesis in these glial cells and its supply to nearby neurons and other glia constitute a novel metabolic unit in the brain. Based on these neuroglial and glioglial relationships, glucose in neurons and phogocytes can be strategically used for energy production, while a variety of L-serine-derived biomolecules required for their proliferaton, survival, differentiation, and function are synthesized in and supplied from the radial glia-astrocyte lineage and olfactory ensheathing glia. A transient capillary expression of ASCT1 in fetal and neonatal brains further suggests that, in addition to the glia-borne L-serine, an active transport of blood-borne L-serine would play an essential role in neural development.

UR - http://www.scopus.com/inward/record.url?scp=0037593543&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037593543&partnerID=8YFLogxK

U2 - 10.1679/aohc.66.109

DO - 10.1679/aohc.66.109

M3 - Review article

C2 - 12846552

AN - SCOPUS:0037593543

VL - 66

SP - 109

EP - 121

JO - Archives of Histology and Cytology

JF - Archives of Histology and Cytology

SN - 0914-9465

IS - 2

ER -