Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin i involves distinct cleavage sites

Silke Haerteis, Annabel Krappitz, Matteus Krappitz, Jane E. Murphy, Marko Bertog, Bettina Krueger, Regina Nacken, Hyunjae Chung, Morley D. Hollenberg, Wolfgang Knecht, Nigel W. Bunnett, Christoph Korbmacher

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)19067-19078
Number of pages12
JournalJournal of Biological Chemistry
Volume289
Issue number27
DOIs
StatePublished - Jul 4 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin i involves distinct cleavage sites'. Together they form a unique fingerprint.

Cite this