Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate

Hans H. Schiffer; Geoffrey T. Swanson; Stephen F. Heinemann

doi:10.1016/S0896-6273(00)80404-3

Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate

Hans H. Schiffer, Geoffrey T. Swanson^*, Stephen F. Heinemann

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Article › peer-review

161 Scopus citations

Abstract

Glutamate receptors of the kainate-preferring subtype have recently been shown to mediate synaptic transmission in the hippocampus. The tow-affinity kainate receptor subunit GluR7 was found to be nonfunctional in previous studies. We report here that the GluR7 subunit and a novel carboxy-terminal splice variant, GluR7b, are functional glutamate receptors with unique pharmacological properties. In particular, glutamate exhibits a 10-fold lower potency for (non-desensitized) GluR7-mediated currents as compared to other non-NMDA receptor channels. These data will facilitate understanding of the distinct role played by GluR7 receptors in synaptic transmission.

Original language	English (US)
Pages (from-to)	1141-1146
Number of pages	6
Journal	Neuron
Volume	19
Issue number	5
DOIs	https://doi.org/10.1016/S0896-6273(00)80404-3
State	Published - Nov 1997

Funding

The authors would like to thank Jim Boulter for the GluR7, KA-1, and KA-2 cDNAs. We also thank Cheryl Rogers and Bob Petroski for subcloning of the cDNAs into pCI-neo. Doug Vetter, Robert Gereau, and Tim Green provided helpful discussions and comments on the manuscript. We are also grateful to Matt Winkler and Mariana Goldrick from Ambion (Austin, TX) for supplying the Mismatch Detect II kit and for supporting the project. Melissa Hartley and the Core Sequencing Facility at the Salk Institute carried out the DNA sequencing. This work was supported by a Deutsche Forschungsgemeinschaft fellowship to H. H. S., an NRSA fellowship (#1 F32 GM 18717–01) to G. T. S., a National Institute for Neurological Diseases and Stroke grant (#2 RO1 NS 28709–06) to S. F. H., and a McKnight Endowment Fund for Neuroscience grant to S. F. H.

ASJC Scopus subject areas

General Neuroscience

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10.1016/S0896-6273(00)80404-3

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title = "Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate",

abstract = "Glutamate receptors of the kainate-preferring subtype have recently been shown to mediate synaptic transmission in the hippocampus. The tow-affinity kainate receptor subunit GluR7 was found to be nonfunctional in previous studies. We report here that the GluR7 subunit and a novel carboxy-terminal splice variant, GluR7b, are functional glutamate receptors with unique pharmacological properties. In particular, glutamate exhibits a 10-fold lower potency for (non-desensitized) GluR7-mediated currents as compared to other non-NMDA receptor channels. These data will facilitate understanding of the distinct role played by GluR7 receptors in synaptic transmission.",

author = "Schiffer, {Hans H.} and Swanson, {Geoffrey T.} and Heinemann, {Stephen F.}",

note = "Funding Information: The authors would like to thank Jim Boulter for the GluR7, KA-1, and KA-2 cDNAs. We also thank Cheryl Rogers and Bob Petroski for subcloning of the cDNAs into pCI-neo. Doug Vetter, Robert Gereau, and Tim Green provided helpful discussions and comments on the manuscript. We are also grateful to Matt Winkler and Mariana Goldrick from Ambion (Austin, TX) for supplying the Mismatch Detect II kit and for supporting the project. Melissa Hartley and the Core Sequencing Facility at the Salk Institute carried out the DNA sequencing. This work was supported by a Deutsche Forschungsgemeinschaft fellowship to H. H. S., an NRSA fellowship (#1 F32 GM 18717–01) to G. T. S., a National Institute for Neurological Diseases and Stroke grant (#2 RO1 NS 28709–06) to S. F. H., and a McKnight Endowment Fund for Neuroscience grant to S. F. H. ",

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doi = "10.1016/S0896-6273(00)80404-3",

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AU - Swanson, Geoffrey T.

AU - Heinemann, Stephen F.

N1 - Funding Information: The authors would like to thank Jim Boulter for the GluR7, KA-1, and KA-2 cDNAs. We also thank Cheryl Rogers and Bob Petroski for subcloning of the cDNAs into pCI-neo. Doug Vetter, Robert Gereau, and Tim Green provided helpful discussions and comments on the manuscript. We are also grateful to Matt Winkler and Mariana Goldrick from Ambion (Austin, TX) for supplying the Mismatch Detect II kit and for supporting the project. Melissa Hartley and the Core Sequencing Facility at the Salk Institute carried out the DNA sequencing. This work was supported by a Deutsche Forschungsgemeinschaft fellowship to H. H. S., an NRSA fellowship (#1 F32 GM 18717–01) to G. T. S., a National Institute for Neurological Diseases and Stroke grant (#2 RO1 NS 28709–06) to S. F. H., and a McKnight Endowment Fund for Neuroscience grant to S. F. H.

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AB - Glutamate receptors of the kainate-preferring subtype have recently been shown to mediate synaptic transmission in the hippocampus. The tow-affinity kainate receptor subunit GluR7 was found to be nonfunctional in previous studies. We report here that the GluR7 subunit and a novel carboxy-terminal splice variant, GluR7b, are functional glutamate receptors with unique pharmacological properties. In particular, glutamate exhibits a 10-fold lower potency for (non-desensitized) GluR7-mediated currents as compared to other non-NMDA receptor channels. These data will facilitate understanding of the distinct role played by GluR7 receptors in synaptic transmission.

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Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate

Abstract

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