Molecular determinants of D-serine-mediated gliotransmission: from release to function.
Glia. 2006-01-01; 54(7): 726-737
DOI: 10.1002/glia.20356
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1. Glia. 2006 Nov 15;54(7):726-37.
Molecular determinants of D-serine-mediated gliotransmission: from release to
function.
Oliet SH(1), Mothet JP.
Author information:
(1)INSERM U378 and Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat,
33077 Bordeaux, France.
Since the late 80s, it is recognized that functional activation of N-methyl
D-aspartate receptors (NMDARs) requires the binding of both glutamate and
glycine. However, the surprising discovery that the wrong isomer of serine,
D-serine, is present in mammals has profoundly challenged this dogmatic model of
NMDARs activation. Indeed, there are accumulating evidence indicating that
D-serine is the endogenous ligand for the glycine modulatory binding site in many
brain areas. D-Serine is synthesized in glial cells by serine racemase (SR) and
released upon activation of glutamate receptors. Here, we will provide an
overview of recent findings on the molecular and cellular mechanisms involved in
the synthesis and release of this gliotransmitter. We will also emphasize the
function of this novel messenger in regulating synaptic excitatory transmission
and plasticity in different brain areas. Because it fulfils all criteria for a
gliotransmitter, D-serine regulatory action on glutamatergic transmission further
illustrates the emerging concept of the « tripartite synapse ».
DOI: 10.1002/glia.20356
PMID: 17006901 [Indexed for MEDLINE]