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Structure and pharmacological properties of a molluscan glutamate-gated cation channel and its likely role in feeding behavior.

ABSTRACT: We describe the isolation of a molluscan (Lymnaea stagnalis) full-length complementary DNA that encodes a mature polypeptide (which we have named Lym-eGluR2) with a predicted molecular weight of 105 kDa that exhibits 44-48% identity to the mammalian kainate-selective glutamate receptor GluR5, GluR6, and GluR7 subunits. Injection of in vitro-transcribed RNA from this clone into Xenopus laevis oocytes results in the robust expression of homo-oligomeric cation channels that can be gated by L-glutamate (EC50 = 1.2 +/- 0.3 micron) and several other glutamate receptor agonists; rank order of potency: glutamate >> kainate > ibotenate > AMPA. These currents can be blocked by the mammalian non-NMDA receptor antagonists 6,7-dinitroquinoxaline-2,3-dione, 6-cyano-7-nitroquinoxaline-2,3-dione, and 1-(4-chlorobenzoyl)piperazine-2,3-dicarboxylic acid. Ionic-replacement experiments have shown that the agonist-induced current is carried entirely by sodium and potassium ions. In situ hybridization has revealed that the Lym-eGluR2 transcript is present in all 11 ganglia of the Lymnaea CNS, including the 4-cluster motorneurons within the paired buccal ganglia. The pharmacological properties and deduced location of Lym-eGluR2 are entirely consistent with it being (a component of) the receptor, which has been identified previously on buccal motorneurons, that mediates the excitatory effects of glutamate released from neurons within the feeding central pattern generator.

SUBMITTER: Stuhmer T

PROVIDER: S-EPMC6579067 | biostudies-literature | 1996 May

REPOSITORIES: biostudies-literature

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Structure and pharmacological properties of a molluscan glutamate-gated cation channel and its likely role in feeding behavior.

Stühmer T T Amar M M Harvey R J RJ Bermudez I I van Minnen J J Darlison M G MG

The Journal of neuroscience : the official journal of the Society for Neuroscience 19960501 9

We describe the isolation of a molluscan (Lymnaea stagnalis) full-length complementary DNA that encodes a mature polypeptide (which we have named Lym-eGluR2) with a predicted molecular weight of 105 kDa that exhibits 44-48% identity to the mammalian kainate-selective glutamate receptor GluR5, GluR6, and GluR7 subunits. Injection of in vitro-transcribed RNA from this clone into Xenopus laevis oocytes results in the robust expression of homo-oligomeric cation channels that can be gated by L-glutam ...[more]

PMID: 8622118

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Project description:The glutamate-gated chloride channel (GluCl) is a highly sensitive insecticide target of the avermectin class of insecticides. As an alternative to using chemical insecticides to kill mosquitoes, we tested the effects of purified immunoglobulin G (IgG) targeting the extracellular domain of GluCl from Anopheles gambiae (AgGluCl) on the survivorship of three key mosquito disease vectors: Anopheles gambiae s.s., Aedes aegypti and Culex tarsalis. When administered through a single blood meal, anti-AgGluCl IgG reduced the survivorship of A. gambiae in a dose-dependent manner (LC50: 2.82 mg ml(-1), range 2.68-2.96 mg ml(-1)) but not A. aegypti or C. tarsalis. We previously demonstrated that AgGluCl is only located in tissues of the head and thorax of A. gambiae. To verify that AgGluCl IgG is affecting target antigens found outside the midgut, we injected it directly into the hemocoel via intrathoracic injection. A single, physiologically relevant concentration of anti-AgGluCl IgG injected into the hemocoel equally reduced mosquito survivorship of all three species. To test whether anti-AgGluCl IgG was entering the hemocoel of each of these mosquitoes, we fed mosquitoes a blood meal containing anti-AgGluCl IgG and subsequently extracted their hemolymph. We only detected IgG in the hemolymph of A. gambiae, suggesting that resistance of A. aegypti and C. tarsalis to anti-AgGluCl IgG found in blood meals is due to deficient IgG translocation across the midgut. We predicted that anti-AgGluCl IgG's mode of action is by antagonizing GluCl activity. To test this hypothesis, we fed A. gambiae blood meals containing anti-AgGluCl IgG and the GluCl agonist ivermectin (IVM). Anti-AgGluCl IgG attenuated the mosquitocidal effects of IVM, suggesting that anti-AgGluCl IgG antagonizes IVM-induced activation of GluCl. Lastly, we stained adult, female A. aegypti and C. tarsalis for GluCl expression. Neuronal GluCl expression in these mosquitoes was similar to previously reported A. gambiae GluCl expression; however, we also discovered GluCl staining on the basolateral surface of their midgut epithelial cells, suggesting important physiological differences in Culicine and Anopheline mosquitoes.

Dataset Information

Structure and pharmacological properties of a molluscan glutamate-gated cation channel and its likely role in feeding behavior.

Publications

Structure and pharmacological properties of a molluscan glutamate-gated cation channel and its likely role in feeding behavior.

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