Small conductance chloride channels in the apical membrane of thyroid cells

Champigny, Guy; Verrier, Bernard; Gérard, Céline; Mauchamp, Jean; Lazdunski, Michel

doi:10.1016/0014-5793(90)80024-d

Cited by 49 publications

(32 citation statements)

References 20 publications

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“…A similar sensitivity to stilbene derivatives was observed in the outwardly rectifying Cl-channel (Tabeharani, Low, Elie & Hanrahan, 1990;Tilmann, Kunzelmann, Frobe, Cabantchik, Lang, Englert & Greger, 1991) and in the Ca2"-activated Cl-channel but not in the cyclic AMPactivated ohmic Cl-channel (Tabeharani et al 1990;. Similarly, NPPB blocks the outwardly rectifying Cl-channel (Hayslett, Gogelein, Kunzelmann & Greger, 1987;Kunzelmann, Pavenstadt & Greger, 1989;Li et al 1990;McCann et al 1989;Giraldez et al 1989;Sepulveda et al 1991;Tilmann et al 1991) but not the cyclic AMP-activated ohmic Cl-channel (Champigny, Verrier, Gerard, Mauchamp & Lazdunski, 1990).…”

Section: Direct Inhibition By Arachidonic Acidmentioning

confidence: 64%

Volume‐regulatory Cl‐ channel currents in cultured human epithelial cells.

Kubo

Okada

1992

The Journal of Physiology

180

158

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SUMMARY1. During osmotic swelling, cultured human small intestinal epithelial cells (Intestine 407) exhibited activation of large Cl-currents under the patch-clamp whole-cell configuration. The volume-sensitive Cl-conductance was independent of intracellular Ca2+ and cyclic AMP.2. The anion permeability sequence of the current was SCN-> I-> Br-> Cl-> F-> gluconate-, corresponding to Eisenman's sequence I. 3. Cl-currents were instantaneously activated by command pulses in a range of -120 to + 45 mV. At potentials more positive than + 50 mV the current showed a time-dependent inactivation. This inactivation was accelerated by increased depolarization. The instantaneous current-voltage relationship rectified in the outward direction.4. A stilbene-derivative Cl-channel blocker, 4-acetamido-4'-isothiocyanostilbene (SITS), inhibited the Cl-current at micromolar concentrations. SITS facilitated inactivation at positive potentials. Outward currents were more prominently suppressed by SITS than inward currents. The concentrations required for 50% inhibition (IC50) of outward and inward currents were 1-5 and 6 EM, respectively. The outward and inward currents were equally inhibited by a carboxylate analogue Clchannel blocker, 5-nitro-2-(3-phenylpropylamino)-benzoate (NPPB)

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Section: Direct Inhibition By Arachidonic Acidmentioning

confidence: 64%

Volume‐regulatory Cl‐ channel currents in cultured human epithelial cells.

Kubo

Okada

1992

The Journal of Physiology

180

158

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“…The deactivated excised channel could not be reactivated by pulsing the voltage to high positive or negative values. Cl-selective channels found in immortalized airway cell lines [ 181, human pancreatic duct [30], thyroid [31] and T84 cells [32]. Expression of the cystic fibrosis gene produced a CAMP-regulated Cl-channel with a cell-attached conductance of 8 pS in the nonepithelial Sf9 cells [6], 4 pS in Vero cells [9], 9 pS in CHO cells [8] and 10 pS in HeLa cells [7].…”

Section: Resultsmentioning

confidence: 99%

Characterization of cAMP dependent CFTR‐chloride channels in human trache gland cells

Becq¹,

Merten²,

Voelckel³

et al. 1993

FEBS Letters

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Human tracheal gland cells are believed to be a major site at the origin of cystic fibrosis. Since this disease is due to mutations in a protein called CFTR, we looked for the activity of CFTR in human tracheal gland cells in culture. We have identified CFTR‐like chloride‐selective channels as having a linear current‐voltage relationship and unitary conductance of 7 pS in these cells. In cell‐attached patches, theophylline (1 mM), IBMX (1 mM), or a cocktail of dibutyryl cAMP (1 mM) and IBMX (0.1 mM) promoted the opening of channels. The unitary current had a reversal potential close to the cell resting potential. Replacement of choline by K+ or Na+ in the pipette solution was without effect on the current‐voltage relationship, the reversal potential or the unitary conductance, which is consistent with the chloride selectivity of the channel. Channels were always found clustered and their opening probability was not noticeably dependent on membrane potential. This work therefore represents the first observation of a CFTR‐like channel activity in submucosal gland cells.

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“…Expression of the CFTR gene generates a novel cAMP-stimulated conductance (6), which is mediated by chloride channels with relatively low unitary conductance, a nonrectifying currentvoltage relationship (7), and other features typical of epithelial chloride channels (8)(9)(10). They have characteristic gating kinetics at physiological potentials (open bursts that are interrupted by rapid flickering, separated by relatively long closures) and are only weakly inhibited by external 4,4'diisothiocyanatostilbene-2,2'-disulfonic acid, an inhibitor of many anion transporters (7,11,12).…”

Section: Cftr Is An Atp-dependent Chloride Channel That Is Tightly Rementioning

confidence: 99%

Revisiting Cystic Fibrosis Transmembrane Conductance Regulator Structure and Function

Hanrahan

Wioland²

2004

Proceedings of the American Thoracic Society

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The cystic fibrosis transmembrane conductance regulator (CFTR) is a channel/enzyme which mediates passive diffusion of chloride and bicarbonate through epithelial cell membranes. It is expressed in many cell types throughout the body, but in the airways it is found mainly in secretory serous cells of the submucosal glands. CFTR belongs to a large super-family of ATP binding cassette transporters that have two nucleotide binding domains with characteristic sequences or "motifs". Although most other ATP binding cassette transporters consume ATP to actively transport various substrates, in CFTR the interactions of ATP with nucleotide binding domains control opening and closing of the channel pore (i.e., channel gating). Recent high resolution structures of bacterial nucleotide binding domains combined with new biochemical and electrophysiological studies of CFTR itself have led to major advances in our understanding of CFTR gating. For example, it is now clear that the ATPase activity of CFTR is not strictly required for its channel activity. CFTR has at least two distinct gating modes; one dependent on hydrolysis and the other requiring only stable ATP binding. In this article we discuss a working hypothesis for CFTR that incorporates these recent findings and discuss some interesting implications of the paradigm shift for other aspects of CFTR function and dysfunction.

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Small conductance chloride channels in the apical membrane of thyroid cells

Cited by 49 publications

References 20 publications

Volume‐regulatory Cl‐ channel currents in cultured human epithelial cells.

Volume‐regulatory Cl‐ channel currents in cultured human epithelial cells.

Characterization of cAMP dependent CFTR‐chloride channels in human trache gland cells

Revisiting Cystic Fibrosis Transmembrane Conductance Regulator Structure and Function

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