Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2001-9-21
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7691-704
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11567059-Aging, pubmed-meshheading:11567059-Animals, pubmed-meshheading:11567059-Antibody Specificity, pubmed-meshheading:11567059-Astrocytes, pubmed-meshheading:11567059-Brain, pubmed-meshheading:11567059-Carbohydrate Dehydrogenases, pubmed-meshheading:11567059-Cell Differentiation, pubmed-meshheading:11567059-Cell Lineage, pubmed-meshheading:11567059-Dendrites, pubmed-meshheading:11567059-Gene Expression Regulation, Developmental, pubmed-meshheading:11567059-Immunohistochemistry, pubmed-meshheading:11567059-In Situ Hybridization, pubmed-meshheading:11567059-Mice, pubmed-meshheading:11567059-Mice, Inbred C57BL, pubmed-meshheading:11567059-Microscopy, Immunoelectron, pubmed-meshheading:11567059-Neuroglia, pubmed-meshheading:11567059-Olfactory Bulb, pubmed-meshheading:11567059-Organelles, pubmed-meshheading:11567059-Phosphoglycerate Dehydrogenase, pubmed-meshheading:11567059-RNA, Messenger, pubmed-meshheading:11567059-Serine, pubmed-meshheading:11567059-Stem Cells, pubmed-meshheading:11567059-Synapses
pubmed:year
2001
pubmed:articleTitle
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.
pubmed:affiliation
Department of Anatomy, Hokkaido University School of Medicine, Sapporo 060-8638, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't