Pharmacological properties of glycine uptake in the developing rat retina

  title={Pharmacological properties of glycine uptake in the developing rat retina},
  author={Roc{\'i}o Salceda},
  journal={Neurochemistry International},
  • R. Salceda
  • Published 1 September 2006
  • Biology, Medicine
  • Neurochemistry International
A pharmacological characterization of glycine transport was performed in the rat retina at different postnatal ages. The uptake of 3H-glycine increased during the first 2 weeks of postnatal age, reaching maximum values at 12 days; then it decreased sharply to the adult values. We found a Na+ -dependent and high-affinity transport system with a Km of 100 microM. The Na+ Hill coefficient for glycine uptake was 1.76 +/- 0.07. Although glycine uptake was insensitive to staurosporine and phorbol… Expand
Characteristics of glycine transport across the inner blood–retinal barrier
GlyT1 most likely mediates glycine transport at the inner BRB and is expected to play an important role in regulating the glycine concentration in the neural retina. Expand
Differential distribution of glycine transporters in Müller cells and neurons in amphibian retinas
The results indicated that GlyT1- and GlyT2-like transporters were present in Müller cells and neurons, respectively, which is consistent with the general pattern that Gly T1-liketransporters are present in Muller cells and Gly T2- like transportters in neurons in amphibian retinas. Expand
Glycine transporters (glycine transporter 1 and glycine transporter 2) are expressed in retina
In-situ hybridization signals were observed in the ganglionar and inner nuclear layer as well as in the outer nuclear layer of the frog and rat retinas and accumulation of 3H-glycine was observed in isolated photoreceptor cells. Expand
Glycine transport accounts for the differential role of glycine vs. d‐serine at NMDA receptor coagonist sites in the salamander retina
In this study, we demonstrate that d‐serine interacts with N‐methyl‐d‐aspartate receptor (NMDAR) coagonist sites of retinal ganglion cells of the tiger salamander retina by showing that exogenousExpand
Glycine and l-arginine transport in cultured Müller glial cells (TR-MUL)
GlyT1 and CAT1 most likely mediate glycine and L-arginine uptake, respectively, by Müller cells and are expected to play an important role in supplying precursors for creatine biosynthesis in Müllers cells. Expand
Glycine receptor subunits expression in the developing rat retina
These results revealed the expression of GlyR at early postnatal ages, supporting its role in retina development and indicated that the adult retina expressed a high proportion of the &agr;2 subunit, suggesting the expressionof monomeric and/or heteromeric receptors. Expand
D-serine: A study of its function and regulation in the retina
University of Minnesota Ph.D. dissertation. Major: Neuroscience. Advisor: Robert F. Miller, MD. 1 computer file (PDF); v, 130 pages. Ill. (some col.)
Identification of The Cell Type Expressing The Glycine Transporter 1 (GLYT1) in The Thalamus
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Pharmacological Properties of Glycine Transport in the Frog Retina
The results indicate the presence of different glycine transporter isoforms in the frog retina, acting mainly through the classical inhibitory glycine system. Expand
Expression of glycine and the glycine transporter Glyt-1 in the developing rat retina
Diverse mechanisms and transient roles for glycine in the developing rat retina are suggested, including a subpopulation of amacrine cells are prominently immunoreactive for both glycine and glyt-1 in the adult rat retina. Expand
Pharmacological assessment of the role of the glycine transporter GlyT-1 in mediating high-affinity glycine uptake by rat cerebral cortex and cerebellum synaptosomes
It is indicated that high-affinity glycine uptake in cerebral cortex occurs predominantly via GlyT-1, however, in cerebellum, only a part of the high-Affinity uptake is mediated by GlyT -1, with the remaining NFPS-insensitive component most likely mediated by glyT-2. Expand
Uptake and K+-stimulated release of [14C]glycine from frog retinal synaptosomal fractions
  • R. Salceda
  • Chemistry, Medicine
  • Neurochemical Research
  • 2004
The uptake of [14C]glycine in retina and synaptosomal fractions was found to be saturable as well as energy and Na+-dependent, and the K+-stimulated release of glycine from P2 fraction was significantly reduced in the presence of TTX. Expand
Regulation by phorbol esters of the glycine transporter (GLYT1) in glioblastoma cells.
Incubation of C6 cells with TPA led to concentration- and time-dependent decrease in the glycine transport that could be completely suppressed by the addition of the PKC inhibitor staurosporine, and the TPA effect could be mimicked by oleoylacetylglycerol and exogenous phospholipase C. Expand
Glycine transport into plasma-membrane vesicles derived from rat brain synaptosomes.
The existence of a high-affinity, Na+-dependent glycine-uptake system in membrane vesicles derived from rat brain suggests that this amino acid may have a transmitter role in some areas of the rat brain. Expand
Glycine transporters are differentially expressed among CNS cells
Immunoblots show that GLYT1 is expressed at the highest concentrations in the spinal cord, brainstem, diencephalon, and retina, and, in a lesser degree, to the olfactory bulb and brain hemispheres, whereas it is not detected in peripheral tissues. Expand
Cloning and expression of a spinal cord- and brain-specific glycine transporter with novel structural features.
The experimental data suggests GLYT2 might play a major role in the termination of the inhibitory effect of glycine in the brain stem and spinal cord of vertebrates. Expand
Distribution of the glycine transporter glyt-1 in mammalian and nonmammalian retinae.
In monkeys, cats, and rats, populations of cells which the authors interpret as being glycine-containing interplexiform cells expressed glyt-1: these cells lacked a content of glutamate, suggesting they are not bipolar cells. Expand
Cloning, expression, and localization of a rat brain high-affinity glycine transporter.
The primary structure and hydropathicity profile of GLYT1 protein reveal that this protein is a member of the sodium- and chloride-dependent superfamily of transporters that utilize neurotransmitters and related substances as substrates. Expand