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XB-ART-9804
Cell Physiol Biochem 2000 Jan 01;105-6:329-34. doi: 10.1159/000016374.
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Structure and function of the ion channel ICln.

Fürst J , Jakab M , König M , Ritter M , Gschwentner M , Rudzki J , Danzl J , Mayer M , Burtscher CM , Schirmer J , Maier B , Nairz M , Chwatal S , Paulmichl M .


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Normal function of organs and cells is tightly linked to the cytoarchitecture. Control of the cell volume is therefore vital for the organism. A widely established strategy of cells to counteract swelling is the activation of chloride and potassium channels, which leads to a net efflux of salt followed by water - a process termed regulatory volume decrease. Since there is evidence for swelling-dependent chloride channels (IClswell) being activated also during pathological processes, the identification of the molecular entity underlying IClswell is of utmost importance. Several proteins are discussed as the channel forming IClswell, i.e. phospholemman, p-glycoprotein, CLC-3 and ICln. In this review we would like to focus on the properties of ICln, a protein cloned from a Madin Darby canine kidney (MDCK) cell library whose expression in Xenopus laevis oocytes resulted in a nucleotide sensitive outwardly rectifying chloride current closely resembling the biophysical properties of IClswell.

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Species referenced: Xenopus laevis
Genes referenced: clns1a fxyd1