Neuron
A single amino acid exchange alters the pharmacology of neonatal rat glycine receptor subunit
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Cited by (168)
Do in vitro assays in rat primary neurons predict drug-induced seizure liability in humans?
2018, Toxicology and Applied PharmacologyCitation Excerpt :The data from the rat primary neurons clearly demonstrated expression of the glycine receptor subunits GLRA2 and GLRB. However, a single amino acid difference in GLRA2 subunit, from glycine in the rat and in human, to glutamate in the neonatal rat cortical neurons (Becker et al., 1988) leads to lower affinity of strychnine for glycine receptors in neonatal rat cortical neurons (Becker et al., 1988; Kuhse et al., 1990; Schmieden et al., 1992), which might explain the lack of in vitro effects of strychnine in the current study. Antipsychotic or neuroleptic drugs such as chlorpromazine are known to lower the seizure threshold and induce spike-wave discharge pattern in the human EEG (Torta and Monaco, 2002).
New insights in endogenous modulation of ligand-gated ion channels: Histamine is an inverse agonist at strychnine sensitive glycine receptors
2013, European Journal of PharmacologyCitation Excerpt :Such high strychnine sensitivity is in line with the dominant role of the α1 subunit of glycine receptor. α2 homomeric receptors (neonatal type of the spinal glycine receptor) were reported to be strychnine-resistant (Kuhse et al., 1990) and recombinant α2 receptors are less sensitive to strychnine compared to the α1 receptors (Schmieden et al., 1992). Striatal neurons, lacking α1 subunit expression are less sensitive to strychnine (IC50=74 nM, see Sergeeva and Haas, 2001) than TMN neurons (IC50=10 nM).
Protein kinases regulate glycine receptor binding in brain stem auditory nuclei after unilateral cochlear ablation
2007, Brain ResearchCitation Excerpt :Receptor subunit composition, however, may change with age (Milbrandt et al., 1997; Krenning et al., 1998) and after cochlear lesions (Holt et al., 2005; Sassu et al., 2005). Since receptors containing α1, α2 and α3 subunits exhibit similar sensitivities to strychnine (Kuhse et al., 1990; Legendre, 2001; Gisselmann et al., 2002; Han et al., 2003), it is unlikely that changes in receptor subunit composition, if they occurred, directly reduced the [3H]strychnine binding activity after UCA in the present study. It is more likely that the present declines in binding reflect a net loss of whole receptors or a reduced affinity for strychnine caused by a mechanism other than a change in subunit composition.
A novel glycine receptor β subunit splice variant predicts an unorthodox transmembrane topology: Assembly into heteromeric receptor complexes
2007, Journal of Biological ChemistryPostsynaptic receptor mechanisms underlying developmental speeding of synaptic transmission
2005, Neuroscience ResearchGlycinergic inhibition in thalamus revealed by synaptic receptor blockade
2005, Neuropharmacology
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