First Author | Ehmsen JT | Year | 2013 |
Journal | J Neurosci | Volume | 33 |
Issue | 30 | Pages | 12464-9 |
PubMed ID | 23884950 | Mgi Jnum | J:199792 |
Mgi Id | MGI:5505320 | Doi | 10.1523/JNEUROSCI.4914-12.2013 |
Citation | Ehmsen JT, et al. (2013) D-Serine in Glia and Neurons Derives from 3-Phosphoglycerate Dehydrogenase. J Neurosci 33(30):12464-12469 |
abstractText | 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. |