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

Marvão, Pedro; Ferreira, Munique; Bailly, Claire; Paulais, Marc; Bens, Marcelle; Guinamard, Romain; Moreau, Robert A.; Vandewalle, Alain; Teulon, Jacques

doi:10.1172/jci4074

Cited by 24 publications

(26 citation statements)

References 33 publications

(53 reference statements)

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“…As observed in previous experiments on small-conductance Cl Ϫ channels (8,22,24), the closed current level was not usually visible because of the high number of channels per patch and the slow kinetics of the channel (22). The closed current level was estimated by inhibiting Cl Ϫ channel activity, taking advantage of the fact that this channel is inhibited by an acidic intracellular pH (pHi).…”

Section: Methodsmentioning

confidence: 97%

Similar chloride channels in the connecting tubule and cortical collecting duct of the mouse kidney

Nissant

Paulais²,

Lachheb³

et al. 2006

American Journal of Physiology-Renal Physiology

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Using the patch-clamp technique, we investigated Cl- channels on the basolateral membrane of the connecting tubule (CNT) and cortical collecting duct (CCD). We found a approximately 10-pS channel in CNT cell-attached patches. Substitution of sodium gluconate for NaCl in the pipette shifted the reversal potential by +25 mV, whereas N-methyl-D-gluconate chloride had no effect, indicating anion selectivity. On inside-out patches, we determined a selectivity sequence of Cl- > Br- approximately NO3(-) > F-, which is compatible with that of ClC-K2, a Cl- channel in the distal nephron. In addition, the number of open channels (NP(o)) measured in cell-attached patches was significantly increased when Ca2+ concentration or pH in the pipette was increased, which is another characteristic of ClC-K. These findings suggest that the basis for this channel is ClC-K2. A similar Cl- channel was found in CCD patches. Because CNT and CCD are heterogeneous tissues, we studied the cellular distribution of the Cl- channel using recording conditions (KCl-rich solution in the pipette) that allowed us to detect simultaneously Cl- channels and inwardly rectifying K+ channels. We detected Cl- channels alone in 45% and 42% and K+ channels alone in 51% and 58% of CNT and CCD patches, respectively. Cl- and K+ channels were recorded simultaneously from two patches (4% of patches) in the CNT and from none of the patches in the CCD. This indicates that Cl- and K+ channels are located in different cell types, which we suggest may be the intercalated cells and principal cells, respectively.

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Section: Methodsmentioning

confidence: 97%

Similar chloride channels in the connecting tubule and cortical collecting duct of the mouse kidney

Nissant

Paulais²,

Lachheb³

et al. 2006

American Journal of Physiology-Renal Physiology

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“…The reaction buffer (25 l) contained 1 to 5 l cDNA, water, 2.5 l of PCR buffer, 1.5 l of 25 mM MgCl 2 , 1 l of 10 mM dNTP mix, 0.5 l of 10 M oligonucleotide primer (each), and 0.2 l of enzyme. cDNA was amplified using the following primers and conditions: SUR1, 5Ј-ATTAACCTGAGAGGGGCGAT-3Ј (sense) and 5Ј-GAGGTGTAGA-CAGCGAAGGC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 35 cycles of 94°C ϫ 30 s, 58°C ϫ 45 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; SUR2A/B, 5Ј-TGCGACATTTGTGACA-CATG-3Ј (sense) and 5Ј-CGTAAGCCACAGAATACCTGC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 35 cycles of 94°C ϫ 30 s, 58°C ϫ 45 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; Kir6.1, 5Ј-GCAAACCCGAGTCTTCTAGG-3Ј (sense) and 5Ј-GCA-GACGTGAATGACCTGAC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 35 cycles of 94°C ϫ 30 s, 56°C ϫ 30 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; Kir6.2, 5Ј-CTGGCCATCCTCAT-TCTC-3Ј (sense) and 5Ј-GATGCCCGTGGTTTCTAC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 38 cycles of 94°C ϫ 30 s, 57°C ϫ 30 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; ABC1, 5Ј-GGAGTCTAGTCCTCTTTCTC-3Ј (sense) and 5Ј-CCATGAATC-GAGATATCGTC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 38 cycles of 94°C ϫ 30 s, 58°C ϫ 45 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; CFTR (Marvao et al, 1998), 5Ј-CAGT-CATCTCTGCCTTGTGGGA-3Ј (sense) and 5Ј-CGAACTGAAGC-TCGGACGTAGACT-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 35 cycles of 94°C ϫ 30 s, 60°C ϫ 30 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min; and ␤-actin, 5Ј-GAGACCTTCAA-CACCC-3Ј (sense) and 5Ј-GTGGTGGTGAAGCTGTAGCC-3Ј (antisense), an initial denaturation at 94°C ϫ 5 min, 30 cycles of 94°C ϫ 30 s, 58°C ϫ 45 s, 72°C ϫ 45 s, and a final dwell at 72°C ϫ 7 min. With the exception of Kir6.2, in the absence of the reverse transcription reaction, no bands were detected after the amplification.…”

Section: Methodsmentioning

confidence: 99%

“…2, neither J774 nor RAW 264 macrophages expressed CFTR mRNA. The kidney was used as a positive control, because it has been shown to contain a large number of CFTR transcripts (Marvao et al, 1998).…”

Section: Molecular Characterization Of Abc Proteins In Macrophagesmentioning

confidence: 99%

Inhibitors of ATP-Binding Cassette Transporters Suppress Interleukin-12 p40 Production and Major Histocompatibility Complex II Up-Regulation in Macrophages

Haskó¹,

Deitch²,

Németh³

et al. 2002

J Pharmacol Exp Ther

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ATP-binding cassette (ABC) transporters are a large family of proteins whose role is to translocate various substances across biological membranes. They include the Tangier disease protein ABC1, sulfonylurea receptors (SUR), multidrug resistance protein (MDR), and cystic fibrosis transmembrane regulator (CFTR). In the current study, we investigated the involvement of ABC transporters in the regulation of lipopolysaccharide (LPS) and/or interferon (IFN)-␥-induced interleukin (IL)-12 p40 and tumor necrosis factor (TNF)-␣ production, nitric oxide formation, as well as major histocompatibility complex II up-regulation in macrophages. The general ABC transporter inhibitor glibenclamide suppressed both IL-12 p40 and nitric oxide production. However, glibenclamide failed to affect the production of TNF-␣. The selective ABC1 inhibitors 4,4Ј-diisothiocyanostilbene-2,2Ј-disulfonic acid and sulfobromophthalein mimicked the suppressive effect of glibenclamide on IL-12 p40 production. On the other hand, both the MDR inhibitor verapamil and CFTR blocker 2,2Ј-iminodibenzoic acid failed to suppress the production of IL-12 p40. Furthermore, selective inhibitors and activators of SURs were without effect. In agreement with the pharmacological data, macrophages expressed mRNA for ABC1, but not SURs or CFTR. Intracellular levels of IL-12 p40 were decreased by glibenclamide, suggesting that glibenclamide does not affect IL-12 p40 secretion. The effect of glibenclamide did not involve an interference with the activation of the p38 and p42/44 mitogen-activated protein kinases or c-Jun kinase. Glibenclamide also suppressed IFN-␥-induced up-regulation of major histocompatibility complex II. Taken together, our results indicate that ABC proteins regulate LPS and/or IFN-␥-induced macrophage activation.

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“…Methods for channel current recording in inside-out patches were described previously [Marvao et al, 1998]. Bath and pipette solutions contained: 120 mM N-methyl-D-glucamine-Cl (NMDG-Cl), 0.5 mM MgCl 2 , 2 mM EGTA, 10 mM HEPES (pH 7.35 with NMDG).…”

Section: Patch-clamptechnique and Data Analysismentioning

confidence: 99%

Misprocessing of theCFTRprotein leads to mild cystic fibrosis phenotype

et al. 2005

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Cystic fibrosis (CF) is mainly caused by mutations that interfere with the biosynthetic folding of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. The aim of this study was to determine the mechanism of dysfunction of a disease-causing mutation associated with variable phenotypes. In order to attain these objectives, we studied the effect of the p.L206W mutation on CFTR protein production and function, and we examined the genotype-phenotype correlation of [p.L206W]+[p.F508del] patients. We showed that p.L206W is a processing (class II) mutation since the CFTR biosynthetic pathway was severely impaired, whereas single-channel measurements indicated ion conductance similar to the wild-type protein. These data raise the larger question of the phenotypic variability of class II mutants, including p.F508del. Since multiple potential partners could modify the processing of the CFTR protein during its course to the cell surface, environmental and other genetic factors might contribute to this variability.

show abstract

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

Cited by 24 publications

References 33 publications

Similar chloride channels in the connecting tubule and cortical collecting duct of the mouse kidney

Similar chloride channels in the connecting tubule and cortical collecting duct of the mouse kidney

Inhibitors of ATP-Binding Cassette Transporters Suppress Interleukin-12 p40 Production and Major Histocompatibility Complex II Up-Regulation in Macrophages

Misprocessing of theCFTRprotein leads to mild cystic fibrosis phenotype

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