Overview
- Peptide (C)RLYVLKLSDDIGD, corresponding to amino acid residues 202-214 of rat GlyT1 (Accession P28572). 2nd extracellular loop.
- Western blot analysis of rat brain (lanes 1 and 4), mouse brain (lanes 2 and 5) and human U87-MG glioma cell (lanes 3 and 6) lysates:1-3. Anti-GlyT1 (SLC6A9) (extracellular) Antibody (#AGT-011), (1:200).
4-6. Anti-GlyT1 (SLC6A9) (extracellular) Antibody, preincubated with GlyT1/SLC6A9 (extracellular) Blocking Peptide (#BLP-GT011).
- Cell surface detection of GlyT1 by indirect flow cytometry in live intact human Jurkat T-cell leukemia cells:___ Cells.
___ Cells + goat-anti-rabbit-APC.
___ Cells + Anti-GlyT1 (SLC6A9) (extracellular) Antibody (#AGT-011), (2.5μg) + goat-anti-rabbit-APC.
- Zafra, F. et al. (2008) IUBMB Life. 60, 810.
- Chen, N. et al. (2004) Pflugers. Arch. 447, 519.
- Supplisson, S. et al. (2002) FEBS Lett. 529, 93.
- Kristensen, A.S. et al. (2011) Pharmacol. Rev. 63, 585.
- Olivares, L. et al. (1995) J. Biol. Chem. 270, 9437.
- Massari, S. et al. (2005) J. Biol. Chem. 280, 7388.
- Liu, Q.R. et al. (1993) J. Biol. Chem. 268, 22802.
- Rees, M.I. et al. (2006) Nat. Genet. 38, 801.
Apart from its obvious biochemical functions, glycine is also an important inhibitory neurotransmitter. Following depolarization, glycine is released from synaptic vesicles, binds to glycine receptors (GlyRs) on postsynaptic membranes thereby causing hyperpolarization of postsynaptic neurons due to the massive influx of Cl- ions. Glycine is then taken up from the synaptic cleft via the glycine transporters GlyT1 and GlyT21.
GlyT1 and GlyT2 belong to the SLC6, Na+/Cl- dependent transporter family, of which members include transporters for GABA, serotonin, dopamine and norepinephrine2. Like all SLC6 members, GlyT1 and GlyT2 have 12 transmembrane domains and intracellular N- and C-terminals. Both can be found in different splice variants3,4. SLC6 transporters undergo post-translational modifications. For instance, GlyT1 and GlyT2 are glycosylated, which is important for their membrane trafficking5.
Phosphorylation of these two transporters also takes place in a PKC-dependent manner, which may lead to down regulation of both transporters6. Pharmacologically, GlyT1 and GlyT2 can be differentiated by applying sarcosine which inhibits GlyT1 but not GlyT27.
GlyT1 and GlyT2 are broadly expressed in the nervous system; GlyT1 is concentrated in glial cells, while GlyT2 is present in glycenergic neurons in the spinal cord, brainstem and cerebellum1. GlyT1 can also be detected in the pancreas, uterus, stomach, spleen, liver and retina4.
GlyT1 has become a target for the treatment of schizophrenia, although a defect of the protein is not directly associated with the disorder. Inhibiting GlyT1 should lead to the increase in glutamatergic pathways, thereby decreasing psychotic effects in schizophrenic individuals. GlyT2 has been associated with hyperekplexia, a motor disorder characterized by neonatal hypertonia and startle reflex8.
Application key:
Species reactivity key:
Anti-GlyT1 (SLC6A9) (extracellular) Antibody (#AGT-011) is a highly specific antibody directed against an epitope of the rat glycine transporter 1. The antibody can be used in western blot analysis. The antibody recognizes an extracellular epitope and can thus potentially recognize GlyT1 in living cells. It has been designed to recognize GlyT1 from rat, mouse, and human samples.