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
UR - https://www.scopus.com/pages/publications/84903823511
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 -