1998
DOI: 10.1085/jgp.111.5.653
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Permeation and Block of the Skeletal Muscle Chloride Channel, ClC-1, by Foreign Anions

Abstract: 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. … Show more

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Cited by 145 publications
(170 citation statements)
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“…This selectivity mechanism requires that binding sites within the hClC-1 pore exhibit only a low affinity for permeating anions to allow a measurable ion flow per unit of time. In agreement with this prediction, an evaluation of the blocking action of iodide in hClC-1 revealed dissociation constants in the millimolar range (8,10). Because iodide binds more tightly than chloride, this value represents a lower limit for the chloride dissociation constant and demonstrates that ClC-type channels bind anions with affinities that are more than an order of magnitude lower than the values with which potassium (11) and calcium channels (12) interact with their respective permeant ions.…”
Section: The Clc Family Of Voltage-gated CLsupporting
confidence: 54%
See 1 more Smart Citation
“…This selectivity mechanism requires that binding sites within the hClC-1 pore exhibit only a low affinity for permeating anions to allow a measurable ion flow per unit of time. In agreement with this prediction, an evaluation of the blocking action of iodide in hClC-1 revealed dissociation constants in the millimolar range (8,10). Because iodide binds more tightly than chloride, this value represents a lower limit for the chloride dissociation constant and demonstrates that ClC-type channels bind anions with affinities that are more than an order of magnitude lower than the values with which potassium (11) and calcium channels (12) interact with their respective permeant ions.…”
Section: The Clc Family Of Voltage-gated CLsupporting
confidence: 54%
“…Human ClC-1 (hClC-1) 1 exhibits at least two functionally distinct ion binding sites within the pore (8,10), both preferring large and polyatomic anions over chloride. The tighter binding of these anions reduces their turnover, resulting in lower permeability and conductivity, thus making chloride the most permeant anion (8,9).…”
Section: The Clc Family Of Voltage-gated CLmentioning
confidence: 99%
“…Crystal structure and electrophysiological data from ClC channels clearly exclude permeation of ATP. The large organic anion ATP is much too big to pass through the ClC pore [62,63]. Likewise, high-resolution structural data from water and K + channels confirm that the narrow conductive pore is a general feature of ion channels [64,65].…”
Section: Suggested Mechanisms For Cellular Nucleotide Releasementioning
confidence: 87%
“…2B). As a control, SCN -and I -were tested as known inhibitors of transport in ClC chloride channels (20), and both anions did not inhibit formate transport (SI Appendix, Fig. S2).…”
mentioning
confidence: 99%