Journal
CHEMISTRY & BIOLOGY
Volume 17, Issue 8, Pages 831-840Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2010.06.009
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Funding
- National Institutes of Health [R01 CA132630, K99 DA030908]
- Alexander-von-Humboldt Foundation
- Japanese Society for the Promotion of Science
- American Cancer Society
- Daniel Koshland Fellowship in Enzyme Biochemistry
- Skaggs Institute for Chemical Biology
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GDE1 is a mammalian glycerophosphodiesterase (GDE) implicated by in vitro studies in the regulation of glycerophophoinositol (GroPIns) and possibly other glycerophospho (GroP) metabolites. Here, we show using untargeted metabolomics that GroPIns is profoundly (>20-fold) elevated in brain tissue from GDE1(-/-) mice. Furthermore, two additional GroP metabolites not previously identified in eukaryotic cells, glycerophosphoserine (GroPSer) and glycerophosphoglycerate (GroPGate), were also highly elevated in GDE1(-/-) brains. Enzyme assays with synthetic GroP metabolites confirmed that GroPSer and GroPGate are direct substrates of GDE1. Interestingly, our metabolomic profiles also revealed that serine (both L-and D-) levels were significantly reduced in brains of GDE1(-/-) mice. These findings designate GroPSer as a previously unappreciated reservoir for free serine in the nervous system and suggest that GDE1, through recycling serine from GroPSer, may impact D-serine-dependent neural signaling processes in vivo.
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