Abstract
Background: Proteolysis is required for ENaC activity, but the proteases activating ENaC in epithelial tissues are unknown. Results: Human trypsin IV and trypsin I activate ENaC by cleavage at distinct sites in the channel's -subunit. Conclusion: Cleavage at distinct sites may provide a mechanism for differential ENaC regulation by tissue-specific proteases. Significance: ENaC activation by trypsin IV may contribute to ENaC regulation in vivo.
Original language | English (US) |
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Pages (from-to) | 19067-19078 |
Number of pages | 12 |
Journal | Journal of Biological Chemistry |
Volume | 289 |
Issue number | 27 |
DOIs | |
State | Published - Jul 4 2014 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology