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Expression and function of epithelial anoctamins.

Rainer Schreiber¹, Inna Uliyakina, Patthara Kongsuphol

¹Institut für Physiologie, Universität Regensburg, Universitätsstrasse 31, D-93053 Regensburg, Germany.

The Journal of Biological Chemistry

|January 9, 2010

Summary

The anoctamin (ANO) protein family, including ANO1, plays a crucial role in epithelial function. Different ANO members are expressed in specific tissues, forming unique calcium-dependent chloride channels.

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Area of Science:

Cell Biology
Physiology
Molecular Biology

Background:

The calcium-activated chloride channel anoctamin1 (ANO1; TMEM16A) is vital for epithelial organ function.
ANO1 deficiency in mice causes transport defects resembling cystic fibrosis and general epithelial electrolyte transport issues.

Purpose of the Study:

To analyze the expression patterns of all ten anoctamin (ANO1-ANO10) members across various murine tissues.
To investigate the functional properties of ANO proteins, specifically their ability to form calcium-activated chloride channels.

Main Methods:

Analysis of ANO gene expression in a wide range of murine tissues.
Heterologous expression of ANO proteins in Fisher Rat Thyroid (FTR) cells.
Assessment of plasma membrane localization and chloride channel activity using ATP-induced iodide quenching of YFP fluorescence and patch clamping.

Main Results:

Predominant expression of ANO1, 6, 7, 8, 9, and 10 was found in epithelial tissues, while ANO2, 3, 4, and 5 were prevalent in neuronal and muscle tissues.
ANO1, 2, 6, and 7 exhibited calcium-activated chloride (Cl-) conductance when expressed in FTR cells.
ANO9 and ANO10 suppressed baseline Cl- conductance, with ANO9 inhibiting ANO1 activity. ANO6 and ANO10 also produced chloride currents with distinct calcium sensitivities.

Conclusions:

Each tissue expresses a specific set of anoctamins.
These anoctamins form cell- and tissue-specific calcium-dependent chloride channels, highlighting their diverse physiological roles.