scholarly journals Voltage-dependent gating mechanism for single fast chloride channels from rat skeletal muscle.

1992 ◽  
Vol 453 (1) ◽  
pp. 279-306 ◽  
Author(s):  
D S Weiss ◽  
K L Magleby
Keyword(s):  
Skeletal Muscle ◽  
Chloride Channels ◽  
Rat Skeletal Muscle ◽  
Gating Mechanism ◽  
Voltage Dependent

scholarly journals Mechanism of voltage-dependent gating in skeletal muscle chloride channels

1996 ◽  
Vol 71 (2) ◽  
pp. 695-706 ◽  
Author(s):  
C. Fahlke ◽  
A. Rosenbohm ◽  
N. Mitrovic ◽  
A.L. George ◽  
R. Rüdel
Keyword(s):  
Skeletal Muscle ◽  
Chloride Channels ◽  
Voltage Dependent

Enantiomers of clofibric acid analogs have opposite actions on rat skeletal muscle chloride channels

1988 ◽  
Vol 413 (1) ◽  
pp. 105-107 ◽  
Author(s):  
D. Conte-Camerino ◽  
M. Mambrini ◽  
A. DeLuca ◽  
D. Tricarico ◽  
S. H. Bryant ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Chloride Channels ◽  
Clofibric Acid ◽  
Rat Skeletal Muscle

scholarly journals Stilbene derivatives inhibit the activity of the inner mitochondrial membrane chloride channels

2007 ◽  
Vol 12 (4) ◽  
Author(s):  
Izabela Koszela-Piotrowska ◽  
Katarzyna Choma ◽  
Piotr Bednarczyk ◽  
Krzysztof Dołowy ◽  
Adam Szewczyk ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Chloride Channel ◽  
Chloride Channels ◽  
Mitochondrial Membrane ◽  
Disulfonic Acid ◽  
Mitochondrial Membranes ◽  
Rat Skeletal Muscle ◽  
Inner Mitochondrial Membrane ◽  
Stilbene Derivatives ◽  
Rat Heart Mitochondria

AbstractIon channels selective for chloride ions are present in all biological membranes, where they regulate the cell volume or membrane potential. Various chloride channels from mitochondrial membranes have been described in recent years. The aim of our study was to characterize the effect of stilbene derivatives on single-chloride channel activity in the inner mitochondrial membrane. The measurements were performed after the reconstitution into a planar lipid bilayer of the inner mitochondrial membranes from rat skeletal muscle (SMM), rat brain (BM) and heart (HM) mitochondria. After incorporation in a symmetric 450/450 mM KCl solution (cis/trans), the chloride channels were recorded with a mean conductance of 155 ± 5 pS (rat skeletal muscle) and 120 ± 16 pS (rat brain). The conductances of the chloride channels from the rat heart mitochondria in 250/50 mM KCl (cis/trans) gradient solutions were within the 70–130 pS range. The chloride channels were inhibited by these two stilbene derivatives: 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid (DIDS) and 4-acetamido-4′-isothiocyanostilbene-2,2′-disulfonic acid (SITS). The skeletal muscle mitochondrial chloride channel was blocked after the addition of 1 mM DIDS or SITS, whereas the brain mitochondrial channel was blocked by 300 μM DIDS or SITS. The chloride channel from the rat heart mitochondria was inhibited by 50–100 μM DIDS. The inhibitory effect of DIDS was irreversible. Our results confirm the presence of chloride channels sensitive to stilbene derivatives in the inner mitochondrial membrane from rat skeletal muscle, brain and heart cells.

Channelopathies: Their Contribution to Our Knowledge About Voltage-Gated Ion Channels

Physiology ◽  
1997 ◽  
Vol 12 (3) ◽  
pp. 105-112
Author(s):  
F Lehmann-Horn ◽  
R Rudel
Keyword(s):  
Skeletal Muscle ◽  
Ion Channels ◽  
Ion Channel ◽  
Chloride Channels ◽  
Gene Products ◽  
Sodium Potassium ◽  
Voltage Gated ◽  
Voltage Dependent ◽  
Genes Encoding ◽  
Voltage Gated Ion Channels

Since 1990, many mutations in genes encoding voltage-dependent sodium, potassium, calcium, and chloride channels have been discovered to cause disorders of heart, skeletal muscle, brain, or kidney. Study of the defective gene products has furthered our knowledge not only of pathology but also of ion-channel function.

scholarly journals Permeation and Block of the Skeletal Muscle Chloride Channel, ClC-1, by Foreign Anions

1998 ◽  
Vol 111 (5) ◽  
pp. 653-665 ◽  
Author(s):  
G.Y. Rychkov ◽  
M. Pusch ◽  
M.L. Roberts ◽  
T.J. Jentsch ◽  
A.H. Bretag
Keyword(s):  
Skeletal Muscle ◽  
Binding Site ◽  
Chloride Channel ◽  
Chloride Channels ◽  
Single Channel ◽  
Hydrophobic Interactions ◽  
Channel Pore ◽  
Channel Opening ◽  
Voltage Dependent ◽  
Significant Block

A distinctive feature of the voltage-dependent chloride channels ClC-0 (the Torpedo electroplaque chloride channel) and ClC-1 (the major skeletal muscle chloride channel) is that chloride acts as a ligand to its own channel, regulating channel opening and so controlling the permeation of its own species. We have now studied the permeation of a number of foreign anions through ClC-1 using voltage-clamp techniques on Xenopus oocytes and Sf9 cells expressing human (hClC-1) or rat (rClC-1) isoforms, respectively. From their effect on channel gating, the anions presented in this paper can be divided into three groups: impermeant or poorly permeant anions that can not replace Cl− as a channel opener and do not block the channel appreciably (glutamate, gluconate, HCO3−, BrO3−); impermeant anions that can open the channel and show significant block (methanesulfonate, cyclamate); and permeant anions that replace Cl− at the regulatory binding site but impair Cl− passage through the channel pore (Br−, NO3−, ClO3−, I−, ClO4−, SCN−). The permeability sequence for rClC-1, SCN− ∼ ClO4− > Cl− > Br− > NO3− ∼ ClO3− > I− >> BrO3− > HCO3− >> methanesulfonate ∼ cyclamate ∼ glutamate, was different from the sequence determined for blocking potency and ability to shift the Popen curve, SCN− ∼ ClO4− > I− > NO3− ∼ ClO3− ∼ methanesulfonate > Br− > cyclamate > BrO3− > HCO3− > glutamate, implying that the regulatory binding site that opens the channel is different from the selectivity center and situated closer to the external side. Channel block by foreign anions is voltage dependent and can be entirely accounted for by reduction in single channel conductance. Minimum pore diameter was estimated to be ∼4.5 Å. Anomalous mole-fraction effects found for permeability ratios and conductance in mixtures of Cl− and SCN− or ClO4− suggest a multi-ion pore. Hydrophobic interactions with the wall of the channel pore may explain discrepancies between the measured permeabilities of some anions and their size.

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