The phospholipid base-exchange system as a possible modulator of γ-aminobutyric acid transport in brain cells

1977 ◽  
Vol 2 (5) ◽  
pp. 469-484 ◽  
Author(s):  
Gianna Evelina De Medio ◽  
Anders Hamberger ◽  
Åke Sellström ◽  
Giuseppe Porcellati
Keyword(s):  
Aminobutyric Acid ◽  
Brain Cells ◽  
Acid Transport ◽  
Exchange System ◽  
Base Exchange

scholarly journals Agonist-induced inhibition of phosphatidylserine synthesis is secondary to the emptying of intracellular Ca2+ stores in Jurkat T-cells

1992 ◽  
Vol 288 (3) ◽  
pp. 785-789 ◽  
Author(s):  
C Pelassy ◽  
J P Breittmayer ◽  
C Aussel
Keyword(s):  
T Cells ◽  
Exchange System ◽  
Jurkat T Cells ◽  
Experimental Conditions ◽  
Intact Cells ◽  
Base Exchange ◽  
Permeabilized Cells ◽  
Atpase Inhibitors ◽  
Storage Organelle ◽  
Intracellular Compartments

The biosynthesis of phosphatidylserine (PtdSer) by the serine base-exchange enzyme system, in Jurkat T-lymphocytes, was inhibited in intact cells maintained in low-Ca(2+)-containing buffer (< 10 microM-Ca2+) by using Ca2+ ionophores (A23187 or ionomycin). The rise in cytosolic Ca2+ concentration under these experimental conditions was only due to the release of Ca2+ from intracellular compartments, suggesting that the inhibition of PtdSer synthesis was correlated with the emptying of intracellular Ca2+ pools. This was further studied in saponin-permeabilized cells, in which PtdSer synthesis was found to be inhibited by EGTA, Ca2+ ionophores (A23187 or ionomycin) and Ca(2+)-ATPase inhibitors [thapsigargin or 2,5-di-(t-butyl)-benzohydroquinone]. Since Ca(2+)-ATPase inhibitors impaired refilling of the Ca2+ stores with Ca2+, and since in CD3-activated Jurkat T-cells the Ca2+ stores remained empty after 1 h of treatment with anti-CD3 monoclonal antibodies, we suggest that PtdSer synthesis is mainly regulated by the level of Ca2+ in the intracellular compartments and that the Ca(2+)-dependent serine base-exchange system responsible for PtdSer synthesis is probably located within or close to a Ca(2+)-storage organelle.

A novel selective γ-aminobutyric acid transport inhibitor demonstrates a functional role for GABA transporter subtype GAT2/BGT-1 in the CNS

2006 ◽  
Vol 48 (6-7) ◽  
pp. 637-642 ◽  
Author(s):  
Rasmus P. Clausen ◽  
Bente Frølund ◽  
Orla M. Larsson ◽  
Arne Schousboe ◽  
Povl Krogsgaard-Larsen ◽  
...  
Keyword(s):  
Functional Role ◽  
Aminobutyric Acid ◽  
Acid Transport ◽  
Gaba Transporter ◽  
Transport Inhibitor
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