Cathepsin B is secreted apically from Xenopus 2F3 cells and cleaves the epithelial sodium channel (ENaC) to increase its activity.

@article{Alli2012CathepsinBI,
  title={Cathepsin B is secreted apically from Xenopus 2F3 cells and cleaves the epithelial sodium channel (ENaC) to increase its activity.},
  author={Abdel A Alli and Junfeng Song and Otor K Al-Khalili and Hui-Fang Bao and He-ping Ma and Alia A Alli and Douglas C. Eaton},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 36},
  pages={30073-83}
}
The epithelial sodium channel (ENaC) plays an important role in regulating sodium balance, extracellular volume, and blood pressure. Evidence suggests the α and γ subunits of ENaC are cleaved during assembly before they are inserted into the apical membranes of epithelial cells, and maximal activity of ENaC depends on cleavage of the extracellular loops of α and γ subunits. Here, we report that Xenopus 2F3 cells apically express the cysteine protease cathepsin B, as indicated by two-dimensional… CONTINUE READING

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