Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1.

@article{Andreasen2006ActivationOE,
  title={Activation of epithelial sodium channels by mouse channel activating proteases (mCAP) expressed in Xenopus oocytes requires catalytic activity of mCAP3 and mCAP2 but not mCAP1.},
  author={Ditte Andreasen and Gr{\'e}goire Vuagniaux and Nicole Fowler-Jaeger and Edith Hummler and Bernard C Rossier},
  journal={Journal of the American Society of Nephrology : JASN},
  year={2006},
  volume={17 4},
  pages={
          968-76
        }
}
Mouse channel activating proteases 1, 2, and 3 (mCAP1, mCAP2, and mCAP3) were described recently as regulators of the epithelial sodium channel (ENaC). The mCAP are membrane-bound serine proteases that are synthesized as inactive proenzymes. To mature into active proteases, they undergo intramolecular cleavage by auto- and/or heterocatalytic processing. Specific antibodies against each mCAP were developed to distinguish between proenzyme and active protease by Western blot analysis. Various… CONTINUE READING

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