PMID- 21856347
OWN - NLM
STAT- MEDLINE
DCOM- 20130129
LR  - 20211203
IS  - 1872-9754 (Electronic)
IS  - 0197-0186 (Linking)
VI  - 59
IP  - 6
DP  - 2011 Nov
TI  - Signaling through EAAT-1/GLAST in cultured Bergmann glia cells.
PG  - 871-9
LID - 10.1016/j.neuint.2011.07.015 [doi]
AB  - Glutamate, the major excitatory amino acid, activates a wide variety of signal 
      transduction cascades. Synaptic plasticity relies on activity-dependent 
      differential protein expression. Ionotropic and metabotropic glutamate receptors 
      have been critically involved in long-term synaptic changes, although recent 
      findings suggest that the electrogenic Na(+)-dependent glutamate transporters, 
      responsible of its removal from the synaptic cleft, participate in 
      glutamate-induced signaling. Transporter proteins are expressed in neurons and 
      glia cells albeit most of the glutamate uptake occurs in the glial compartment. 
      Within the cerebellum, Bergmann glial cells are close to glutamatergic synapses 
      and participate actively in the recycling of glutamate through the 
      glutamate/glutamine shuttle. In this context, we decided to investigate a 
      plausible role of Bergmann glia glutamate transporters as signaling entities. To 
      this end, primary cultures of chick cerebellar Bergmann glial cells were exposed 
      to d-aspartate (D-Asp) and other transporter ligands and the serine 2448 
      phosphorylation pattern of the master regulator of protein synthesis, namely the 
      mammalian target of rapamycin (mTOR), determined. An increase in mTOR 
      phosphorylation and activity was detected. The signaling cascade included Ca(2+) 
      influx, activation of the phosphatidylinositol 3-kinase and protein kinase B. 
      Furthermore, transporter signaling resulted also in an increase in activator 
      protein-1 (AP-1) binding to DNA and the up-regulation of the transcription of an 
      AP-1 driven gene construct. These results add a novel mediator of the glutamate 
      effects at the translational and transcriptional levels and further strengthen 
      the notion of the critical involvement of glia cells in synaptic function.
CI  - Copyright A(c) 2011 Elsevier B.V. All rights reserved.
FAU - Martinez-Lozada, Zila
AU  - Martinez-Lozada Z
AD  - Departamento de Genetica y Biologia Molecular, Centro de Investigacion y de 
      Estudios Avanzados del Instituto Politecnico Nacional, Apartado Postal 14-740, 
      Mexico DF 07000, Mexico.
FAU - Hernandez-Kelly, Luisa C
AU  - Hernandez-Kelly LC
FAU - Aguilera, Jose
AU  - Aguilera J
FAU - Lopez-Bayghen, Esther
AU  - Lopez-Bayghen E
FAU - Ortega, Arturo
AU  - Ortega A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110810
PL  - England
TA  - Neurochem Int
JT  - Neurochemistry international
JID - 8006959
RN  - 0 (Cations, Divalent)
RN  - 0 (Excitatory Amino Acid Transporter 1)
RN  - 30KYC7MIAI (Aspartic Acid)
RN  - 3KX376GY7L (Glutamic Acid)
RN  - EC 2.7.1.137 (Phosphatidylinositol 3-Kinase)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Aspartic Acid/physiology
MH  - Calcium/metabolism
MH  - Cations, Divalent
MH  - Chick Embryo
MH  - Chickens
MH  - Excitatory Amino Acid Transporter 1/genetics/*physiology
MH  - Glutamic Acid/metabolism
MH  - Neuroglia/*classification/enzymology/*metabolism
MH  - Phosphatidylinositol 3-Kinase/physiology
MH  - Phosphatidylinositol 3-Kinases/metabolism
MH  - Primary Cell Culture
MH  - Signal Transduction/*physiology
MH  - TOR Serine-Threonine Kinases/metabolism
EDAT- 2011/08/23 06:00
MHDA- 2013/01/30 06:00
CRDT- 2011/08/23 06:00
PHST- 2011/02/15 00:00 [received]
PHST- 2011/07/26 00:00 [revised]
PHST- 2011/07/29 00:00 [accepted]
PHST- 2011/08/23 06:00 [entrez]
PHST- 2011/08/23 06:00 [pubmed]
PHST- 2013/01/30 06:00 [medline]
AID - S0197-0186(11)00270-1 [pii]
AID - 10.1016/j.neuint.2011.07.015 [doi]
PST - ppublish
SO  - Neurochem Int. 2011 Nov;59(6):871-9. doi: 10.1016/j.neuint.2011.07.015. Epub 2011 
      Aug 10.