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Neuron-glia interactions in glutamatergic neurotransmission: roles of oxidative and glycolytic adenosine triphosphate as energy source.
Schousboe, A; Sickmann, H M; Bak, L K; Schousboe, I; Jajo, F S; Faek, S A A; Waagepetersen, H S.
Afiliación
  • Schousboe A; Department of Pharmacology and Pharmacotherapy, Faculty of Pharmaceutical Sciences, University of Copenhagen, Copenhagen, Denmark.
J Neurosci Res ; 89(12): 1926-34, 2011 Dec.
Article en En | MEDLINE | ID: mdl-21919035
Glutamatergic neurotransmission accounts for a considerable part of energy consumption related to signaling in the brain. Chemical energy is provided by adenosine triphosphate (ATP) formed in glycolysis and tricarboxylic acid (TCA) cycle combined with oxidative phosphorylation. It is not clear whether ATP generated in these pathways is equivalent in relation to fueling of the energy-requiring processes, i.e., vesicle filling, transport, and enzymatic processing in the glutamatergic tripartite synapse (the astrocyte and pre- and postsynapse). The role of astrocytic glycogenolysis in maintaining theses processes also has not been fully elucidated. Cultured astrocytes and neurons were utilized to monitor these processes related to glutamatergic neurotransmission. Inhibitors of glycolysis and TCA cycle in combination with pathway-selective substrates were used to study glutamate uptake and release monitored with D-aspartate. Western blotting of glyceraldehyde-3-P dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) was performed to determine whether these enzymes are associated with the cell membrane. We show that ATP formed in glycolysis is superior to that generated by oxidative phosphorylation in providing energy for glutamate uptake both in astrocytes and in neurons. The neuronal vesicular glutamate release was less dependent on glycolytic ATP. Dependence of glutamate uptake on glycolytic ATP may be at least partially explained by a close association in the membrane of GAPDH and PGK and the glutamate transporters. It may be suggested that these enzymes form a complex with the transporters and the Na(+) /K(+) -ATPase, the latter providing the sodium gradient required for the transport process.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Comunicación Celular / Adenosina Trifosfato / Neuroglía / Transmisión Sináptica / Ácido Glutámico / Neuronas Límite: Animals / Humans Idioma: En Revista: J Neurosci Res Año: 2011 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Comunicación Celular / Adenosina Trifosfato / Neuroglía / Transmisión Sináptica / Ácido Glutámico / Neuronas Límite: Animals / Humans Idioma: En Revista: J Neurosci Res Año: 2011 Tipo del documento: Article País de afiliación: Dinamarca Pais de publicación: Estados Unidos