Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors

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Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors. / Nielsen, B S; Banke, T G; Schousboe, A; Pickering, Darryl.

In: European Journal of Pharmacology, Vol. 360, No. 2-3, 1998, p. 227-38.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Nielsen, BS, Banke, TG, Schousboe, A & Pickering, D 1998, 'Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors', European Journal of Pharmacology, vol. 360, no. 2-3, pp. 227-38.

APA

Nielsen, B. S., Banke, T. G., Schousboe, A., & Pickering, D. (1998). Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors. European Journal of Pharmacology, 360(2-3), 227-38.

Vancouver

Nielsen BS, Banke TG, Schousboe A, Pickering D. Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors. European Journal of Pharmacology. 1998;360(2-3):227-38.

Author

Nielsen, B S ; Banke, T G ; Schousboe, A ; Pickering, Darryl. / Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors. In: European Journal of Pharmacology. 1998 ; Vol. 360, No. 2-3. pp. 227-38.

Bibtex

@article{4321aa706e9011df928f000ea68e967b,
title = "Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors",
abstract = "Homomeric and heteromeric alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunits GluR1o and GluR3o were expressed in Spodoptera frugiperda (Sf9) insect cells. Membranes containing the recombinant receptors showed a doublet of bands of the expected size (99-109 kDa) after western immunoblotting which was shifted to a single band upon deglycosylation. In (R,S)-[3H]AMPA binding experiments, high expression was seen (Bmax = 0.8-3.8 pmol/mg protein) along with high affinity binding to a single site (Kd, nM+/-S.D.): GluR1o, 32.5+/-2.7; GluR3o, 23.7+/-2.4; GluR1o + GluR3o, 18.1+/-2.9. The pharmacological profiles of these receptors resembled that of native rat brain AMPA receptors: AMPA analogues > L-glutamate > quinoxaline-2,3-diones > kainate. In the Xenopus oocyte expression system we had previously shown that the agonist (R,S)-2-amino-3-(3-carboxy-5-methyl-4-isoxazolyl)propionate (ACPA) exhibited an 11-fold selectivity for GluR3o vs. GluR1o. In this study, it was found that ACPA has 3-fold higher affinity at homomeric GluR3o and heteromeric receptors than at homomeric GluR1o, suggesting that its efficacy and/or desensitisation properties are different at GluR1o vs. GluR3o.",
author = "Nielsen, {B S} and Banke, {T G} and A Schousboe and Darryl Pickering",
note = "Keywords: Animals; Baculoviridae; Binding, Competitive; Blotting, Western; Glutamic Acid; Glycosylation; Mutagenesis; Radioligand Assay; Receptors, AMPA; Recombinant Proteins; Spodoptera; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid",
year = "1998",
language = "English",
volume = "360",
pages = "227--38",
journal = "European Journal of Pharmacology",
issn = "0014-2999",
publisher = "Elsevier",
number = "2-3",

}

RIS

TY - JOUR

T1 - Pharmacological properties of homomeric and heteromeric GluR1o and GluR3o receptors

AU - Nielsen, B S

AU - Banke, T G

AU - Schousboe, A

AU - Pickering, Darryl

N1 - Keywords: Animals; Baculoviridae; Binding, Competitive; Blotting, Western; Glutamic Acid; Glycosylation; Mutagenesis; Radioligand Assay; Receptors, AMPA; Recombinant Proteins; Spodoptera; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid

PY - 1998

Y1 - 1998

N2 - Homomeric and heteromeric alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunits GluR1o and GluR3o were expressed in Spodoptera frugiperda (Sf9) insect cells. Membranes containing the recombinant receptors showed a doublet of bands of the expected size (99-109 kDa) after western immunoblotting which was shifted to a single band upon deglycosylation. In (R,S)-[3H]AMPA binding experiments, high expression was seen (Bmax = 0.8-3.8 pmol/mg protein) along with high affinity binding to a single site (Kd, nM+/-S.D.): GluR1o, 32.5+/-2.7; GluR3o, 23.7+/-2.4; GluR1o + GluR3o, 18.1+/-2.9. The pharmacological profiles of these receptors resembled that of native rat brain AMPA receptors: AMPA analogues > L-glutamate > quinoxaline-2,3-diones > kainate. In the Xenopus oocyte expression system we had previously shown that the agonist (R,S)-2-amino-3-(3-carboxy-5-methyl-4-isoxazolyl)propionate (ACPA) exhibited an 11-fold selectivity for GluR3o vs. GluR1o. In this study, it was found that ACPA has 3-fold higher affinity at homomeric GluR3o and heteromeric receptors than at homomeric GluR1o, suggesting that its efficacy and/or desensitisation properties are different at GluR1o vs. GluR3o.

AB - Homomeric and heteromeric alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunits GluR1o and GluR3o were expressed in Spodoptera frugiperda (Sf9) insect cells. Membranes containing the recombinant receptors showed a doublet of bands of the expected size (99-109 kDa) after western immunoblotting which was shifted to a single band upon deglycosylation. In (R,S)-[3H]AMPA binding experiments, high expression was seen (Bmax = 0.8-3.8 pmol/mg protein) along with high affinity binding to a single site (Kd, nM+/-S.D.): GluR1o, 32.5+/-2.7; GluR3o, 23.7+/-2.4; GluR1o + GluR3o, 18.1+/-2.9. The pharmacological profiles of these receptors resembled that of native rat brain AMPA receptors: AMPA analogues > L-glutamate > quinoxaline-2,3-diones > kainate. In the Xenopus oocyte expression system we had previously shown that the agonist (R,S)-2-amino-3-(3-carboxy-5-methyl-4-isoxazolyl)propionate (ACPA) exhibited an 11-fold selectivity for GluR3o vs. GluR1o. In this study, it was found that ACPA has 3-fold higher affinity at homomeric GluR3o and heteromeric receptors than at homomeric GluR1o, suggesting that its efficacy and/or desensitisation properties are different at GluR1o vs. GluR3o.

M3 - Journal article

VL - 360

SP - 227

EP - 238

JO - European Journal of Pharmacology

JF - European Journal of Pharmacology

SN - 0014-2999

IS - 2-3

ER -

ID: 20122784