Glycine taken up through GLYT1 and GLYT2 heterotransporters into glutamatergic axon terminals of mouse spinal cord elicits release of glutamate by homotransporter reversal and through anion channels
作者： Luca Raiteri , Sara Stigliani , Antonella Siri , Mario Passalacqua , Edon Melloni
DOI: 10.1016/J.BCP.2004.08.029
关键词:
摘要: Glycine concentration-dependently elicited [3H]D-aspartate ([3H]D-ASP) release from superfused mouse spinal cord synaptosomes. effect was insensitive to strychnine or 5,7-dichlorokynurenic acid, but prevented by the glycine transporter blocker glycyldodecylamide. also evoked of endogenous glutamate, which sensitive glycyldodecylamide and abolished in low-Na+ medium. Experiments with purified synaptosomes gliasomes show that glycine-evoked [3H]D-ASP largely originates glutamatergic nerve terminals. The halved NFPS, a selective GLYT1 transporters, Org 25543, GLYT2 blocker, almost mixture two, suggesting activation present on terminals triggers [3H]D-ASP. Accordingly, confocal microscopy experiments localization immuno-stained for vesicular glutamate vGLUT1. independent extra- intraterminal Ca2+ ions. It partly inhibited DL-TBOA anion channel blockers niflumic acid NPPB. To conclude, transporters (GLYT1 or/and GLYT2) coexist same Activation heterotransporters elicits homotransporter reversal through channels.
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