European Journal of Pharmacology: Molecular Pharmacology
Differential effects of lectins on recombinant glutamate receptors
References (36)
- et al.
Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop
Neuron
(1995) - et al.
The effect of lectins on desensitization of locust muscle glutamate receptors
Brain Res.
(1985) - et al.
Concanavalin A potentiates NMDA-evoked responses in the Xenopus oocyte expression system
Eur. J. Pharmacol.
(1989) - et al.
The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits
Neuron
(1992) - et al.
N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
Neuron
(1994) - et al.
Characterization of the oligosaccharide side chains on kainate binding proteins and AMPA receptors
Brain Res.
(1992) - et al.
Apparent desensitization of NMDA responses in Xenopus oocytes involves calcium-dependent chloride current
Neuron
(1990) - et al.
Specific inhibition by of the interaction between soybean agglutinin and animal cell surfaces
Biochim. Biophys. Acta
(1970) - et al.
Enhancement of the biological activities of soybean agglutinin by cross-linking with glutaraldehyde
Biochem. Biophys. Res. Commun.
(1973) The interaction of lectins with animal cell surfaces
Int. Rev. Cytol.
(1974)
Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A
Neuron
Immunochemical studies on the specificity of soybean agglutinin
Carbohydr. Res.
Transmembrane topology of the glutamate receptor subunit GluR6
J. Biol. Chem.
The TINS/TIPS Lecture - The molecular biology of mammalian glutamate receptor channels
Trends Neurosci.
A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides
J. Biol. Chem.
Blockade of ionotropic quisqualate receptor desensitization in rat hippocampal neurons by wheat-germ agglutinin and other lectins
Neuroscience
Glutamate receptor desensitization and its role in synaptic transmission
Neuron
Desensitization of AMPA receptors upon multiquantal neutrotransmitter release
Neuron
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Neuropharmacological characterization of frutalin in mice: Evidence of an antidepressant-like effect mediated by the NMDA receptor/NO/cGMP pathway
2018, International Journal of Biological MacromoleculesCitation Excerpt :However, dl-serine (an NMDA agonist) had no effect on the FTL response. Other studies have shown that d-galactose-binding lectins can bind directly to NMDA receptors, modulating their activity by interacting with oligosaccharide residues in these receptors [34–36]. Further studies are needed to understand the relation between FTL and the NMDA receptor.
NRAP-1 Is a Presynaptically Released NMDA Receptor Auxiliary Protein that Modifies Synaptic Strength
2017, NeuronCitation Excerpt :We also found that addition of the lectin Con-A increased current magnitude in oocytes that expressed NMR-1, NMR-2, and NRAP-1, and restored current in oocytes that expressed only NMR-1 and NMR-2. In vertebrates, Con-A is best known for modulating desensitization of kainate and AMPARs (Partin et al., 1993), but it can also enhance currents mediated by NMDARs (Yue et al., 1995). Because NRAP-1 and Con-A both impart function to C. elegans NMDARs, we hypothesize that NRAP-1 might in part modify the rate of NMDAR desensitization, or recovery from desensitization.
Kainate receptors: Pharmacology, function and therapeutic potential
2009, NeuropharmacologyCitation Excerpt :In a study by Everts et al. (1999) the actions of con A were investigated on a range of functional GluR subunits. It was observed that con A blocked desensitisation of recombinant KARs but had a much lesser effect on AMPAR (no action on GluA2) and NMDAR subtypes (Yue et al., 1995; Everts et al., 1999). Con A potentiates the effects of agonists on GluK2 (Jones et al., 1997; Paternain et al., 1998) but has a much lesser effect on agonist potency on GluK1 (Huettner, 1990; Bleakman et al., 2002).
Correlation of the expression of kainate receptor subtypes to responses evoked in cultured cortical and spinal cord neurones
2002, Brain ResearchCitation Excerpt :Previous studies have demonstrated that GluR6 channels are insensitive to AMPA, whereas those heteromerically assembled from GluR6 and KA2 can be activated by this agonist [8,13,24]. Con A, which selectively blocks desensitization of KA receptors, while having little effect on AMPA receptors [29,49,51], potentiated responses of cortical, but not spinal cord, neurones to AMPA. This would be consonant with the expression of GluR6/KA2 receptors by cortical neurones and would moreover suggest that this combination does not occur in spinal cord neurones.