Treating cystic fibrosis infection, inflammation and ion channels

Therapy ◽  
2011 ◽  
Vol 8 (6) ◽  
pp. 583-585
Author(s):  
J Stuart Elborn
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels

scholarly journals Small-molecule ion channels increase host defences in cystic fibrosis airway epithelia

Nature ◽  
2019 ◽  
Vol 567 (7748) ◽  
pp. 405-408 ◽  
Author(s):  
Katrina A. Muraglia ◽  
Rajeev S. Chorghade ◽  
Bo Ram Kim ◽  
Xiao Xiao Tang ◽  
Viral S. Shah ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Small Molecule ◽  
Airway Epithelia ◽  
Cystic Fibrosis Airway

scholarly journals Regulation of ion channels in cystic fibrosis (869.8)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Katherine Henry ◽  
Eric Schiffhauer ◽  
Seakwoo Lee ◽  
Pamela Zeitlin
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels

Role of CFTR and Other Ion Channels in Cystic Fibrosis

2007 ◽  
pp. 23-41
Author(s):  
Karl Kunzelmann ◽  
Tanja Bachhuber ◽  
Gabriele Adam ◽  
Thilo Voelcker ◽  
Bettina Murle ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels

scholarly journals Ion channels as targets to treat cystic fibrosis lung disease

2018 ◽  
Vol 17 (2) ◽  
pp. S22-S27 ◽  
Author(s):  
S. Lorraine Martin ◽  
Vinciane Saint-Criq ◽  
Tzyh-Chang Hwang ◽  
László Csanády
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Lung Disease ◽  
Cystic Fibrosis Lung ◽  
Cystic Fibrosis Lung Disease

scholarly journals Pharmacological Modulation of Ion Channels for the Treatment of Cystic Fibrosis

2021 ◽  
Vol Volume 13 ◽  
pp. 693-723
Author(s):  
Madalena C Pinto ◽  
Iris AL Silva ◽  
Miriam F Figueira ◽  
Margarida D Amaral ◽  
Miquéias Lopes-Pacheco
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Pharmacological Modulation

Ion channels in normal human and cystic fibrosis sweat gland cells

1989 ◽  
Vol 257 (1) ◽  
pp. C129-C140 ◽  
Author(s):  
M. E. Krouse ◽  
G. Hagiwara ◽  
J. Chen ◽  
N. J. Lewiston ◽  
J. J. Wine
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Sweat Gland ◽  
Single Channel ◽  
Cell Types ◽  
Cation Channels ◽  
Secretory Cells ◽  
Anion Channels ◽  
Current Voltage ◽  
Normal Human

Single-channel patch-clamp techniques were used to study the population of apical membrane ion channels in cultured sweat gland secretory cells from normal and cystic fibrosis subjects. Four types of anion channels and two types of cation channels were found. At physiological voltages, anion channels had chord conductances of 10, 18, 24, and greater than 200 pS. All had linear current-voltage relations except the 24 pS channel, which showed outward rectification. Cation channels had chord conductances of 5 and 18 pS, were linear, and were nonselective for a variety of cations. Channel types and proportions were equivalent in control, cystic fibrosis, and cystic fibrosis heterozygote cells. Beyond showing that the distribution of channel types remains unchanged in cystic fibrosis cells, the data provide a basis for comparison with cells cultured under different conditions, with other cell types, and with native tissues.

scholarly journals Catalyst-like modulation of transition states for CFTR channel opening and closing: New stimulation strategy exploits nonequilibrium gating

2014 ◽  
Vol 143 (2) ◽  
pp. 269-287 ◽  
Author(s):  
László Csanády ◽  
Beáta Töröcsik
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Single Channel ◽  
Transition States ◽  
Chloride Ion ◽  
Open Probability ◽  
Gating Mechanism ◽  
Channel Opening ◽  
The Stability ◽  
Opening And Closing

Cystic fibrosis transmembrane conductance regulator (CFTR) is the chloride ion channel mutated in cystic fibrosis (CF) patients. It is an ATP-binding cassette protein, and its resulting cyclic nonequilibrium gating mechanism sets it apart from most other ion channels. The most common CF mutation (ΔF508) impairs folding of CFTR but also channel gating, reducing open probability (Po). This gating defect must be addressed to effectively treat CF. Combining single-channel and macroscopic current measurements in inside-out patches, we show here that the two effects of 5-nitro-2-(3-phenylpropylamino)benzoate (NPPB) on CFTR, pore block and gating stimulation, are independent, suggesting action at distinct sites. Furthermore, detailed kinetic analysis revealed that NPPB potently increases Po, also of ΔF508 CFTR, by affecting the stability of gating transition states. This finding is unexpected, because for most ion channels, which gate at equilibrium, altering transition-state stabilities has no effect on Po; rather, agonists usually stimulate by stabilizing open states. Our results highlight how for CFTR, because of its unique cyclic mechanism, gating transition states determine Po and offer strategic targets for potentiator compounds to achieve maximal efficacy.

Regulation of epithelial ion channels by the cystic fibrosis transmembrane conductance regulator

1996 ◽  
Vol 74 (9) ◽  
pp. 527-534 ◽  
Author(s):  
R. Greger ◽  
M. Mall ◽  
M. Bleich ◽  
D. Ecke ◽  
R. Warth ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Cystic Fibrosis Transmembrane

Physiology of apoptosis

2000 ◽  
Vol 279 (4) ◽  
pp. F605-F615 ◽  
Author(s):  
E. Gulbins ◽  
A. Jekle ◽  
K. Ferlinz ◽  
H. Grassmé ◽  
F. Lang
Keyword(s):  
Cystic Fibrosis ◽  
Ion Channels ◽  
Chloride Channel ◽  
Mitochondrial Permeability Transition Pore ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Volume Changes ◽  
Mitochondrial Permeability ◽  
Type K

Ion fluxes and volume changes of the whole cell as well as of organelles belong to the hallmarks of apoptosis; however, the molecular mechanism regulating these changes is only poorly characterized. Several ion channels in the plasma membrane, in particular the N-type K+channel, the chloride channel cystic fibrosis conductance regulator, and an outward rectifying chloride channel, as well as the mitochondrial permeability transition pore, have been implicated to be involved in signal transduction cascades regulating apoptosis. Furthermore, Bcl-2-like proteins have been suggested to function, at least in part, as ion channels, because they display some homology to bacterial pore-forming toxins. In contrast to the demonstration of the involvement of these different ion channels in apoptosis, the molecular consequences regulated by these ion channels, and finally triggering apoptosis, are almost completely unknown.

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