ClC-1 chloride channel: Matching its properties to a role in skeletal muscle

dc.contributor.authorAromataris, E.
dc.contributor.authorRychkov, G.
dc.date.issued2006
dc.descriptionThe definitive version is available at www.blackwell-synergy.com
dc.description.abstract1. ClC-1 is a Cl- channel in mammalian skeletal muscle that plays an important role in membrane repolarization following muscular contraction. Reduction of ClC-1 conductance results in myotonia, a state characterized by muscle hyperexcitability. 2. As is the case for other members of the ClC family, ClC-1 exists as a dimer that forms a double-barrelled channel. Each barrel, or pore, of ClC-1 is gated by its own gate ('fast' or 'single pore' gate), whereas both pores are gated simultaneously by another mechanism ('slow' or 'common' gate). 3. Comparison of the biophysical and pharmacological properties of heterologously expressed ClC-1 with the properties of the Cl- conductance measured in skeletal muscle strongly suggests that ClC-1 is the major Cl- channel responsible for muscle repolarization. However, not all results obtained in experiments on whole muscle or muscle fibres support this notion. 4. In the present review we attempt to bring together the current knowledge of ClC-1 with the physiology of skeletal muscle.
dc.description.statementofresponsibilityEdoardo C Aromataris and Grigori Y Rychkov
dc.identifier.citationClinical and Experimental Pharmacology and Physiology, 2006; 33(11):1118-1123
dc.identifier.doi10.1111/j.1440-1681.2006.04502.x
dc.identifier.issn0305-1870
dc.identifier.issn1440-1681
dc.identifier.orcidAromataris, E. [0000-0001-7238-5833]
dc.identifier.orcidRychkov, G. [0000-0002-2788-2977]
dc.identifier.urihttp://hdl.handle.net/2440/24087
dc.language.isoen
dc.publisherBlackwell Publishing Asia
dc.source.urihttps://doi.org/10.1111/j.1440-1681.2006.04502.x
dc.subjectCl- conductance
dc.subjectClC-1
dc.subjectgating
dc.subjectmuscle excitability
dc.subjectmyotonia congenita
dc.subjectskeletal muscle
dc.titleClC-1 chloride channel: Matching its properties to a role in skeletal muscle
dc.typeJournal article
pubs.publication-statusPublished

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