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 William Bunnett, Christoph Korbmacher

Research output: Contribution to journalArticleResearchpeer-review

21 Citations (Scopus)

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
Pages (from-to)19067 - 19078
Number of pages12
JournalThe Journal of Biological Chemistry
Volume289
Issue number27
DOIs
Publication statusPublished - 2014

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