Endogenous d-serine exists in the mammalian brain independent of synthesis by serine racemase

• Published in: Biochemical and biophysical research communications Vol. 641; pp. 186 - 191
• Main Authors: Osaki, Akina, Aoyama, Marie, Mita, Masashi, Hamase, Kenji, Yasui, Masato, Sasabe, Jumpei
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.01.2023
• Subjects: And d-amino acids; Animals; Brain - metabolism; d-serine; GluN1; Mammals - metabolism; Mice; Mice, Knockout; NMDAR; Racemases and Epimerases - genetics; Racemases and Epimerases - metabolism; Receptors, N-Methyl-D-Aspartate - metabolism; Serine - metabolism; Serine racemase; GluN1; NMDAR; And d-amino acids; Serine racemase; d-serine; (d)(-)serine; And (d)(-)amino acids

Activation of N-methyl-d-aspartate receptors (NMDARs) requires binding of a co-agonist in addition to l-glutamate. d-serine binds to the co-agonist site on GluN1 subunits of NMDARs and modulates glutamatergic neurotransmission. While loss of GluN1 subunits in mice results in neonatal death due to re...