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

doi:10.1074/jbc.M113.538470

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

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

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)
Pages (from-to)	19067-19078
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	289
Issue number	27
DOIs	https://doi.org/10.1074/jbc.M113.538470
State	Published - Jul 4 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Haerteis, S., Krappitz, A., Krappitz, M., Murphy, J. E., Bertog, M., Krueger, B., Nacken, R., Chung, H., Hollenberg, M. D., Knecht, W., Bunnett, N. W., & Korbmacher, C. (2014). Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin i involves distinct cleavage sites. Journal of Biological Chemistry, 289(27), 19067-19078. https://doi.org/10.1074/jbc.M113.538470

Haerteis, S, Krappitz, A, Krappitz, M, Murphy, JE, Bertog, M, Krueger, B, Nacken, R, Chung, H, Hollenberg, MD, Knecht, W, Bunnett, NW & Korbmacher, C 2014, 'Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin i involves distinct cleavage sites', Journal of Biological Chemistry, vol. 289, no. 27, pp. 19067-19078. https://doi.org/10.1074/jbc.M113.538470

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

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.",

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

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doi = "10.1074/jbc.M113.538470",

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T1 - Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin i involves distinct cleavage sites

AU - Haerteis, Silke

AU - Krappitz, Annabel

AU - Krappitz, Matteus

AU - Murphy, Jane E.

AU - Bertog, Marko

AU - Krueger, Bettina

AU - Nacken, Regina

AU - Chung, Hyunjae

AU - Hollenberg, Morley D.

AU - Knecht, Wolfgang

AU - Bunnett, Nigel W.

AU - Korbmacher, Christoph

PY - 2014/7/4

Y1 - 2014/7/4

N2 - 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.

AB - 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.

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

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