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The calcium-activated chloride channel anoctamin1 (ANO1; TMEM16A) is fundamental for the function of epithelial organs. Mice lacking ANO1 expression exhibit transport defects and a pathology similar to cystic fibrosis. They also show a general defect of epithelial electrolyte transport. Here we analyzed expression of all ten members (ANO1-ANO10) in a broad range of murine tissues and detected predominant expression of ANO1, 6, 7, 8, 9, 10 in epithelial tissues, while ANO2, 3, 4, 5 are common in neuronal and muscle tissues. When expressed in Fisher Rat Thyroid (FTR) cells, all ANO proteins localized to the plasma membrane but only ANO1, 2, 6, and 7 produced Ca(2+)-activated Cl(-) conductance, as analyzed by ATP-induced iodide quenching of YFP fluorescence. In contrast ANO9 and ANO10 suppressed baseline Cl(-) conductance and coexpression of ANO9 with ANO1 inhibited ANO1 activity. Patch clamping of ANO-expressing FRT cells indicated that apart from ANO1 also ANO6 and 10 produced chloride currents, albeit with very different Ca(2+) sensitivity and activation time. We conclude that each tissue expresses a set of anoctamins that form cell- and tissue-specific Ca(2+)-dependent Cl(-) channels.

Original publication

DOI

10.1074/jbc.M109.065367

Type

Journal article

Journal

J Biol Chem

Publication Date

05/03/2010

Volume

285

Pages

7838 - 7845

Keywords

Animals, Biological Transport, Calcium, Cell Line, Cell Membrane, Chloride Channels, Chlorides, Epithelium, Humans, Ion Channel Gating, Ionomycin, Ionophores, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Molecular Sequence Data, Patch-Clamp Techniques, Protein Isoforms, Rats, Tissue Distribution