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Research Article Free access | 10.1172/JCI4074

Cl- absorption across the thick ascending limb is not altered in cystic fibrosis mice. A role for a pseudo-CFTR Cl- channel.

P Marvão, M C De Jesus Ferreira, C Bailly, M Paulais, M Bens, R Guinamard, R Moreau, A Vandewalle, and J Teulon

INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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INSERM CJF 95-07, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, Paris, France.

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Published December 1, 1998 - More info

Published in Volume 102, Issue 11 on December 1, 1998
J Clin Invest. 1998;102(11):1986–1993. https://doi.org/10.1172/JCI4074.
© 1998 The American Society for Clinical Investigation
Published December 1, 1998 - Version history
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Abstract

The cortical thick ascending limb (CTAL) absorbs Cl- via a Na+-K+-Cl- cotransport at the apical membrane and several Cl- channels at the basolateral membrane, including a 9-pS channel having several properties of the cystic fibrosis transmembrane conductance regulator (CFTR). Having checked that CFTR mRNA is present in the mouse CTAL, we investigated whether this channel is a CFTR molecule by applying the patch-clamp technique to CTALs microdissected from CFTR knockout mice (cftrm1Unc). The 9-pS channel was active in cell-attached patches from tubules of mice homozygous for the disrupted cftr gene [CFTR (-/-)] at the same frequency and with the same activity (NPo) as in normal [CFTR (+/+)] or heterozygous [CFTR (+/-)] mice. The conductive properties of the channel, studied on inside-out patches, were identical in CFTR (-/-), CFTR (+/+), and CFTR (+/-) tubules, as were the sensitivities to internal pH and internal ATP, two typical features of this channel. In addition, the Cl- absorption in isolated, microperfused CTALs and the Na+-K+-Cl- cotransport activity were identical in CFTR (-/-), CFTR (+/+), and CFTR (+/-) mice. These results show that the 9-pS Cl- channel is distinct from CFTR, and that the CFTR protein has no influence on the Cl- absorption in this part of the renal tubule.

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