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| Content Provider | PubMed Central |
|---|---|
| Author | Jung, Jinsei Nam, Joo Hyun Park, Hyun Woo Oh, Uhtaek Yoon, Joo-heon Lee, Min Goo |
| Abstract | Anoctamin 1 (ANO1)/transmembrane protein 16A (TMEM16A) is a calcium-activated anion channel that may play a role in HCO3 − secretion in epithelial cells. Here, we report that the anion selectivity of ANO1 is dynamically regulated by the Ca2+/calmodulin complex. Whole-cell current measurements in HEK 293T cells indicated that ANO1 becomes highly permeable to HCO3 − at high [Ca2+]i. Interestingly, this result was not observed in excised patches, indicating the involvement of cytosolic factors in this process. Further studies revealed that the direct association between ANO1 and calmodulin at high [Ca2+]i is responsible for changes in anion permeability. Calmodulin physically interacted with ANO1 in a [Ca2+]i-dependent manner, and addition of recombinant calmodulin to the cytosolic side of excised patches reversibly increased PHCO3/PCl. In addition, the high [Ca2+]i-induced increase in HCO3 − permeability was reproduced in mouse submandibular gland acinar cells, in which ANO1 plays a critical role in fluid secretion. These results indicate that the HCO3 − permeability of ANO1 can be dynamically modulated and that ANO1 may play an important role in cellular HCO3 − transport, especially in transepithelial HCO3 − secretion. |
| Related Links | http://dx.doi.org/10.1073/pnas.1211594110 |
| Ending Page | 365 |
| Page Count | 6 |
| Starting Page | 360 |
| File Format | |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 1 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-01-02 |
| Access Restriction | Open |
| Rights Holder | National Academy of Sciences |
| Subject Keyword | General Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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