Block of CFTR-dependent chloride currents by inhibitors of multidrug resistance-associated proteins

Tullia Diena; Raffaella Melani; Emanuela Caci; Nicoletta Pedemonte; Elvira Sondo; Olga Zegarra-Moran; Luis J V Galietta

doi:10.1016/j.ejphar.2007.01.051

Block of CFTR-dependent chloride currents by inhibitors of multidrug resistance-associated proteins

Tullia Diena, Raffaella Melani, Emanuela Caci, Nicoletta Pedemonte, Elvira Sondo, Olga Zegarra-Moran, Luis J V Galietta

Istituto "Giannina Gaslini"

Research output: Contribution to journal › Article › peer-review

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein that belongs to the same family as multidrug resistance-associated proteins whose main function is to expel xenobiotics and physiological organic anions from the cell interior. Despite the overall structural similarity with these membrane proteins, CFTR is not an active transporter but is instead a Cl^- channel. We have tested the ability of known inhibitors of multidrug resistance-associated proteins to affect CFTR Cl^- currents. We have found that sulfinpyrazone, probenecid, and benzbromarone are also inhibitors of CFTR activity, with a mechanism involving blockage of the channel pore.

Original language	English
Pages (from-to)	127-131
Number of pages	5
Journal	European Journal of Pharmacology
Volume	560
Issue number	2-3
DOIs	https://doi.org/10.1016/j.ejphar.2007.01.051
Publication status	Published - Apr 10 2007

Keywords

CFTR
Channel blocker
Chloride channel
Multidrug resistance protein

ASJC Scopus subject areas

Cellular and Molecular Neuroscience
Pharmacology

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10.1016/j.ejphar.2007.01.051

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Block of CFTR-dependent chloride currents by inhibitors of multidrug resistance-associated proteins. / Diena, Tullia; Melani, Raffaella; Caci, Emanuela; Pedemonte, Nicoletta ; Sondo, Elvira; Zegarra-Moran, Olga; Galietta, Luis J V.

In: European Journal of Pharmacology, Vol. 560, No. 2-3, 10.04.2007, p. 127-131.

Research output: Contribution to journal › Article › peer-review

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title = "Block of CFTR-dependent chloride currents by inhibitors of multidrug resistance-associated proteins",

abstract = "The cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein that belongs to the same family as multidrug resistance-associated proteins whose main function is to expel xenobiotics and physiological organic anions from the cell interior. Despite the overall structural similarity with these membrane proteins, CFTR is not an active transporter but is instead a Cl- channel. We have tested the ability of known inhibitors of multidrug resistance-associated proteins to affect CFTR Cl- currents. We have found that sulfinpyrazone, probenecid, and benzbromarone are also inhibitors of CFTR activity, with a mechanism involving blockage of the channel pore.",

keywords = "CFTR, Channel blocker, Chloride channel, Multidrug resistance protein",

author = "Tullia Diena and Raffaella Melani and Emanuela Caci and Nicoletta Pedemonte and Elvira Sondo and Olga Zegarra-Moran and Galietta, {Luis J V}",

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AU - Diena, Tullia

AU - Melani, Raffaella

AU - Caci, Emanuela

AU - Pedemonte, Nicoletta

AU - Sondo, Elvira

AU - Zegarra-Moran, Olga

AU - Galietta, Luis J V

PY - 2007/4/10

Y1 - 2007/4/10

N2 - The cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein that belongs to the same family as multidrug resistance-associated proteins whose main function is to expel xenobiotics and physiological organic anions from the cell interior. Despite the overall structural similarity with these membrane proteins, CFTR is not an active transporter but is instead a Cl- channel. We have tested the ability of known inhibitors of multidrug resistance-associated proteins to affect CFTR Cl- currents. We have found that sulfinpyrazone, probenecid, and benzbromarone are also inhibitors of CFTR activity, with a mechanism involving blockage of the channel pore.

AB - The cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein that belongs to the same family as multidrug resistance-associated proteins whose main function is to expel xenobiotics and physiological organic anions from the cell interior. Despite the overall structural similarity with these membrane proteins, CFTR is not an active transporter but is instead a Cl- channel. We have tested the ability of known inhibitors of multidrug resistance-associated proteins to affect CFTR Cl- currents. We have found that sulfinpyrazone, probenecid, and benzbromarone are also inhibitors of CFTR activity, with a mechanism involving blockage of the channel pore.

KW - CFTR

KW - Channel blocker

KW - Chloride channel

KW - Multidrug resistance protein

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EP - 131

JO - European Journal of Pharmacology

JF - European Journal of Pharmacology

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ER -

Block of CFTR-dependent chloride currents by inhibitors of multidrug resistance-associated proteins

Abstract

Keywords

ASJC Scopus subject areas

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