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Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology
The Drosophila para sodium channel α subunit was expressed in Xenopus oocytes alone and in combination with tipE, a putative Drosophila sodium channel accessory subunit. Coexpression of tipE with para results in elevated levels of sodium currents and accelerated current decay. Para/TipE sodium chann...
Autores principales: | , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1997
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2233785/ https://www.ncbi.nlm.nih.gov/pubmed/9236205 |
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author | Warmke, Jeffrey W. Reenan, Robert A.G. Wang, Peiyi Qian, Su Arena, Joseph P. Wang, Jixin Wunderler, Denise Liu, Ken Kaczorowski, Gregory J. der Ploeg, Lex H.T. Van Ganetzky, Barry Cohen, Charles J. |
author_facet | Warmke, Jeffrey W. Reenan, Robert A.G. Wang, Peiyi Qian, Su Arena, Joseph P. Wang, Jixin Wunderler, Denise Liu, Ken Kaczorowski, Gregory J. der Ploeg, Lex H.T. Van Ganetzky, Barry Cohen, Charles J. |
author_sort | Warmke, Jeffrey W. |
collection | PubMed |
description | The Drosophila para sodium channel α subunit was expressed in Xenopus oocytes alone and in combination with tipE, a putative Drosophila sodium channel accessory subunit. Coexpression of tipE with para results in elevated levels of sodium currents and accelerated current decay. Para/TipE sodium channels have biophysical and pharmacological properties similar to those of native channels. However, the pharmacology of these channels differs from that of vertebrate sodium channels: (a) toxin II from Anemonia sulcata, which slows inactivation, binds to Para and some mammalian sodium channels with similar affinity (K (d) ≅ 10 nM), but this toxin causes a 100-fold greater decrease in the rate of inactivation of Para/TipE than of mammalian channels; (b) Para sodium channels are >10-fold more sensitive to block by tetrodotoxin; and (c) modification by the pyrethroid insecticide permethrin is >100-fold more potent for Para than for rat brain type IIA sodium channels. Our results suggest that the selective toxicity of pyrethroid insecticides is due at least in part to the greater affinity of pyrethroids for insect sodium channels than for mammalian sodium channels. |
format | Text |
id | pubmed-2233785 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1997 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22337852008-04-22 Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology Warmke, Jeffrey W. Reenan, Robert A.G. Wang, Peiyi Qian, Su Arena, Joseph P. Wang, Jixin Wunderler, Denise Liu, Ken Kaczorowski, Gregory J. der Ploeg, Lex H.T. Van Ganetzky, Barry Cohen, Charles J. J Gen Physiol Article The Drosophila para sodium channel α subunit was expressed in Xenopus oocytes alone and in combination with tipE, a putative Drosophila sodium channel accessory subunit. Coexpression of tipE with para results in elevated levels of sodium currents and accelerated current decay. Para/TipE sodium channels have biophysical and pharmacological properties similar to those of native channels. However, the pharmacology of these channels differs from that of vertebrate sodium channels: (a) toxin II from Anemonia sulcata, which slows inactivation, binds to Para and some mammalian sodium channels with similar affinity (K (d) ≅ 10 nM), but this toxin causes a 100-fold greater decrease in the rate of inactivation of Para/TipE than of mammalian channels; (b) Para sodium channels are >10-fold more sensitive to block by tetrodotoxin; and (c) modification by the pyrethroid insecticide permethrin is >100-fold more potent for Para than for rat brain type IIA sodium channels. Our results suggest that the selective toxicity of pyrethroid insecticides is due at least in part to the greater affinity of pyrethroids for insect sodium channels than for mammalian sodium channels. The Rockefeller University Press 1997-08-01 /pmc/articles/PMC2233785/ /pubmed/9236205 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Warmke, Jeffrey W. Reenan, Robert A.G. Wang, Peiyi Qian, Su Arena, Joseph P. Wang, Jixin Wunderler, Denise Liu, Ken Kaczorowski, Gregory J. der Ploeg, Lex H.T. Van Ganetzky, Barry Cohen, Charles J. Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title | Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title_full | Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title_fullStr | Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title_full_unstemmed | Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title_short | Functional Expression of Drosophila para Sodium Channels : Modulation by the Membrane Protein TipE and Toxin Pharmacology |
title_sort | functional expression of drosophila para sodium channels : modulation by the membrane protein tipe and toxin pharmacology |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2233785/ https://www.ncbi.nlm.nih.gov/pubmed/9236205 |
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