Literature summary for 3.4.21.4 extracted from

Haerteis, S.; Krappitz, A.; Krappitz, M.; Murphy, J.; Bertog, M.; Krueger, B.; Nacken, R.; Chung, H.; Hollenberg, M.; Knecht, W.; Bunnett, N.; Korbmacher, C.
Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin I involves distinct cleavage sites (2014), J. Biol. Chem., 289, 19067-19078.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
epithelial cell	isoform trypsin IV is expressed in human renal epithelial cells and can increase epithelial sodium channel-mediated sodium transport in cultured human airway epithelial cells	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
epithelial sodium channel + H2O	-	Homo sapiens	?	epithelial sodium channel cleavage and activation by isoform trypsin IV but not by trypsin I requires a critical cleavage site, i.e. Lys189 in the extracellular domain of the gamma-subunit	?
N-(p-tosyl)-Gly-Pro-Arg 4-nitroanilide + H2O	-	Homo sapiens	N-(p-tosyl)-Gly-Pro-Arg + 4-nitroaniline	-	?

General Information

General Information	Comment	Organism
physiological function	isoforms trypsin IV and trypsin I can stimulate epithelial sodium channel heterologously expressed in Xenopus oocytes. Epithelial sodium channel cleavage and activation by trypsin IV but not by trypsin I requires a critical cleavage site, i.e. Lys189 in the extracellular domain of the gamma-subunit. Channel activation by trypsin I is prevented by mutating three putative cleavage sites (Lys168, Lys170, and Arg172) in addition to mutating previously described prostasin (RKRK178), plasmin (Lys189), and neutrophil elastase (Val182 and Val193) sites	Homo sapiens

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Release 2023.1 (January 2023)