Regulation of the glutamate uptake by extracellular calcium

Inhibition of L-glutamate and GABA synaptosome uptake by crotoxin, the major neurotoxin from Crotalus durissus terrificus venom

“…After 45 min, the cells were already recovered with full ability to been one of the explanations for convulsive diseases (39). Our results show that extracellular Ca 2+ does not significantly interfere in L-Glu ( Figure 5) or GABA uptake (data not shown), in disagreement with Zhu et al (64) and Mafra et al data (35). We have to point out that L-Glu or GABA uptake indeed slightly decreases in the absence of external Ca 2+ , which was not An important aspect of neurotransmitter transport is that they are potentially electrogenic.…”

Involvement of calcium-dependent mechanisms in T3-induced phosphorylation of vimentin of immature rat testis

“…This reagent exchanges Ca 2+ more than 100 times faster than other agents such as EGTA, because of the faster rates of association and dissociation. Therefore, BAPTA is an important tool to control fast changes in Ca 2+ concentration (Mafra et al, 2002). Our results showed that when the intracellular calcium was chelated with BAPTA, the effect of T 3 on vimentin phosphorylation was totally prevented.…”

Evidence that intracellular Ca2+ mediates the effect of α-ketoisocaproic acid on the phosphorylating system of cytoskeletal proteins from cerebral cortex of immature rats

“…4), suggesting that Ca 2+ entry via voltage-and ligand-gated channels are involved in the ability of KIC to alter the phosphorylating/dephosphorylating equilibrium of the cytoskeletal proteins studied. To further investigate the role of intracellular Ca 2+ in this process we used BAPTA-AM, the membrane-permeable form of BAPTA, as the active Ca 2+ chelator [22]. Tissue slices were incubated with 1 mM KIC plus 50 AM BAPTA-AM, a concentration that does not alter the phosphorylating system.…”