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ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction
The effect of intracellular adenosine triphosphate (ATP) on the “common gating” of the CLC-1 chloride channel has been studied by several laboratories with controversial results. Our previous study on the channel expressed in Xenopus oocytes using excised inside-out patch-clamp methods showed a robu...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2553389/ https://www.ncbi.nlm.nih.gov/pubmed/18824589 http://dx.doi.org/10.1085/jgp.200810023 |
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author | Zhang, Xiao-Dong Tseng, Pang-Yen Chen, Tsung-Yu |
author_facet | Zhang, Xiao-Dong Tseng, Pang-Yen Chen, Tsung-Yu |
author_sort | Zhang, Xiao-Dong |
collection | PubMed |
description | The effect of intracellular adenosine triphosphate (ATP) on the “common gating” of the CLC-1 chloride channel has been studied by several laboratories with controversial results. Our previous study on the channel expressed in Xenopus oocytes using excised inside-out patch-clamp methods showed a robust effect of ATP in shifting the open probability curve of the common gate toward more depolarizing voltages (Tseng, P.Y., B. Bennetts, and T.Y. Chen. 2007. J. Gen. Physiol. 130:217–221). The results were consistent with those from studying the channel expressed in mammalian cells using whole cell recording methods (Bennetts, B., M.W. Parker, and B.A. Cromer. 2007. J. Biol. Chem. 282:32780–32791). However, a recent study using excised-patch recording methods for channels expressed in Xenopus oocytes reported that ATP had no direct effect on CLC-1 (Zifarelli, G., and M. Pusch. 2008. J. Gen. Physiol. 131:109–116). Here, we report that oxidation of CLC-1 may be the culprit underlying the controversy. When patches were excised from mammalian cells, the sensitivity to ATP was lost quickly—within 2–3 min. This loss of ATP sensitivity could be prevented or reversed by reducing agents. On the other hand, CLC-1 expressed in Xenopus oocytes lost the ATP sensitivity when patches were treated with oxidizing reagents. These results suggest a novel view in muscle physiology that the mechanisms controlling muscle fatigability may include the oxidation of CLC-1. |
format | Text |
id | pubmed-2553389 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-25533892009-04-01 ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction Zhang, Xiao-Dong Tseng, Pang-Yen Chen, Tsung-Yu J Gen Physiol Articles The effect of intracellular adenosine triphosphate (ATP) on the “common gating” of the CLC-1 chloride channel has been studied by several laboratories with controversial results. Our previous study on the channel expressed in Xenopus oocytes using excised inside-out patch-clamp methods showed a robust effect of ATP in shifting the open probability curve of the common gate toward more depolarizing voltages (Tseng, P.Y., B. Bennetts, and T.Y. Chen. 2007. J. Gen. Physiol. 130:217–221). The results were consistent with those from studying the channel expressed in mammalian cells using whole cell recording methods (Bennetts, B., M.W. Parker, and B.A. Cromer. 2007. J. Biol. Chem. 282:32780–32791). However, a recent study using excised-patch recording methods for channels expressed in Xenopus oocytes reported that ATP had no direct effect on CLC-1 (Zifarelli, G., and M. Pusch. 2008. J. Gen. Physiol. 131:109–116). Here, we report that oxidation of CLC-1 may be the culprit underlying the controversy. When patches were excised from mammalian cells, the sensitivity to ATP was lost quickly—within 2–3 min. This loss of ATP sensitivity could be prevented or reversed by reducing agents. On the other hand, CLC-1 expressed in Xenopus oocytes lost the ATP sensitivity when patches were treated with oxidizing reagents. These results suggest a novel view in muscle physiology that the mechanisms controlling muscle fatigability may include the oxidation of CLC-1. The Rockefeller University Press 2008-10 /pmc/articles/PMC2553389/ /pubmed/18824589 http://dx.doi.org/10.1085/jgp.200810023 Text en © 2008 Zhang et al. 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.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Articles Zhang, Xiao-Dong Tseng, Pang-Yen Chen, Tsung-Yu ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title | ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title_full | ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title_fullStr | ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title_full_unstemmed | ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title_short | ATP Inhibition of CLC-1 Is Controlled by Oxidation and Reduction |
title_sort | atp inhibition of clc-1 is controlled by oxidation and reduction |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2553389/ https://www.ncbi.nlm.nih.gov/pubmed/18824589 http://dx.doi.org/10.1085/jgp.200810023 |
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