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Glycine is the major inhibitory neurotransmitter in the spinal cord and brainstem and is also required for the activation of NMDA receptors. The extracellular concentration of this neuroactive amino acid is regulated by at least two glycine transporters (GLYT1 and GLYT2). To study the localization and properties of these proteins, sequence-specific(More)
The high-affinity glycine transporter in neurons and glial cells is the primary means of inactivating synaptic glycine. Previous molecular cloning studies have indicated heterogeneity of glycine transporters in the CNS. Here the distribution of glycine transporter GLYT1 and GLYT2 transcripts and proteins in different regions and developmental stages of the(More)
Previously we demonstrated the existence of a physical and functional interaction between the glycine transporters and the SNARE protein syntaxin 1. In the present report the physiological role of the syntaxin 1-glycine transporter 2 (GLYT2) interaction has been investigated by using a brain-derived preparation. Previous studies, focused on syntaxin(More)
We examined the effects of nine different tricyclic antidepressant drugs on the glycine uptake mediated by the glycine transporter 1b (GLYT1b) and glycine transporter 2a (GLYT2a) stably expressed in human embryonic kidney 293 cells. Desipramine, imipramine, clomipramine, nomifensine and mianserin had no effect on the activity of the glycine transporters.(More)
Glycine exerts multiple functions in the central nervous system, as an inhibitory neurotransmitter through activation of specific, Cl--permeable, ligand-gated ionotropic receptors and as an obligatory co-agonist with glutamate on the activation of N-methyl-D-aspartate (NMDA) receptors. In some areas of the central nervous system, glycine seems to be(More)
High affinity sodium- and potassium-coupled L-glutamate transport into presynaptic nerve terminals and fine glial processes removes the neurotransmitter from the synaptic cleft, thereby terminating glutamergic transmission. This report describes that the purified L-glutamate transporter from pig brain is phosphorylated by protein kinase C, predominantly at(More)
Glycine is a major inhibitory neurotransmitter in the spinal cord and brainstem of vertebrates. Glycine is accumulated into synaptic vesicles by a proton-coupled transport system and released to the synaptic cleft after depolarization of the presynaptic terminal. The inhibitory action of glycine is mediated by pentameric glycine receptors (GlyR) that belong(More)
The synaptic action of many neurotransmitters is terminated by specific transporters that remove the molecules from the synaptic cleft and help to replenish the transmitter supply. Here, we have investigated the spatiotemporal distribution of the glycine transporter GLYT2 in the central auditory system of rats, where glycinergic synapses are abundant. In(More)
To elucidate the role of N-glycosylation in the function of the high affinity glycine transporter GLYT1, we have investigated the effect of the glycosylation inhibitor tunicamycin as well as the effect of the disruption of the putative glycosylation sites by site-directed mutagenesis. SDS-polyacrylamide gel electrophoresis of proteins from GLYT1-transfected(More)
The effects of arachidonic acid on glycine uptake, exchange and efflux in C6 glioma cells were investigated. Arachidonic acid produced a dose-dependent inhibition of high-affinity glycine uptake. This effect was not due to a simple detergent-like action on membranes, as the inhibition of glycine transport was most pronounced with cis-unsaturated long-chain(More)