Differential effects of lectins on recombinant glutamate receptors

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Abstract

The effects of the lectins concanavalin A, succinyl concanavalin A, wheat-germ agglutinin and soybean agglutinin were studied at recombinant ionotropic glutamate receptors expressed in Xenopus oocytes. Homomeric and heteromeric receptors from each of the three major classes of ionotropic glutamate receptors (N-methyl-D-aspartate (NMDA), α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and kainate) were studied. The lectins potentiated homomeric configurations of kainate, AMPA and NMDA receptors to a greater degree than the corresponding heteromeric configurations although the rank order of the lectin potentiating effects was the same for both homomeric and heteromeric receptors within a given glutamate receptor class. The most profound effects of the lectins were observed with the kainate receptors; the rank order of potentiating effects of the lectins at the homo- and heteromeric kainate receptors (Glu6 and Glu6/KA-2) was concanavalin A > succinyl concanavalin A > wheat-germ agglutinin > soybean agglutinin. At the recombinant Glu3 and Glu23 AMPA receptor complexes, wheat-germ agglutinin and concanavalin A produced the largest enhancements of the glutamate-activated currents followed by succinyl concanavalin A; soybean agglutinin had no significant potentiating effect. Agonist-evoked currents recorded from oocytes expressing the homo- and heteromeric NMDA receptors were only slightly enhanced by concanavalin A and succinyl concanavalin A but not by wheat-germ agglutinin or soybean agglutinin. These results demonstrate that kainate, AMPA and NMDA receptors display dramatic differences in their responses to lectins, and suggest that the receptor-bound oligosaccharide side chains may play different roles in the functional responses mediated by the three major classes of ionotropic glutamate receptors.

References (36)

Cited by (38)

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    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.

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    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

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    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).

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    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.

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