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

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 William Bunnett, Christoph Korbmacher

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

29 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 language	English
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
Publication status	Published - 2014

Access to Document

10.1074/jbc.M113.538470

Cite this

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

@article{892aa5c98d924636a5a604fb855cd8e5,

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 William} and Christoph Korbmacher",

year = "2014",

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

language = "English",

volume = "289",

pages = "19067 -- 19078",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology",

number = "27",

}

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

TY - JOUR

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 William

AU - Korbmacher, Christoph

PY - 2014

Y1 - 2014

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.

UR - http://www.jbc.org/content/289/27/19067.full.pdf+html

U2 - 10.1074/jbc.M113.538470

DO - 10.1074/jbc.M113.538470

M3 - Article

SN - 0021-9258

VL - 289

SP - 19067

EP - 19078

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 27

ER -

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

Abstract

Access to Document

Other files and links

Cite this