Ca2+-dependent modulation of GABAA and NMDA receptors by extracellular ATP: implication for function of tripartite synapse. Biochem Soc Trans 2009 Dec;37(Pt 6):1407-11
Date
11/17/2009Pubmed ID
19909286DOI
10.1042/BST0371407Scopus ID
2-s2.0-70450170577 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
The importance of communication between neuronal and glial cells for brain function is recognized by a modern concept of 'tripartite synapse'. Astrocytes enwrap synapses and can modulate their activity by releasing gliotransmitters such as ATP, glutamate and D-serine. One of the regulatory pathways in the tripartite synapse is mediated by P2X purinoreceptors. Release of ATP from synaptic terminals and astrocytes activates Ca(2+) influx via P2X purinoreceptors which co-localize with NMDA (N-methyl-D-aspartate) and GABA (gamma-aminobutyric acid) receptors and can modulate their activity via intracellular cascades which involve phosphatase II and PKA (protein kinase A).
Author List
Lalo U, Andrew J, Palygin O, Pankratov YMESH terms used to index this publication - Major topics in bold
Adenosine TriphosphateAnimals
Astrocytes
Calcium
Humans
Mice
Neurons
Presynaptic Terminals
Receptors, GABA-A
Receptors, N-Methyl-D-Aspartate
Receptors, Purinergic P2
Signal Transduction
Synapses
