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• W2890631218 endingPage "469" @default.
• W2890631218 startingPage "461" @default.
• W2890631218 abstract "Sodium influx is tightly regulated in the cells of blood origin. Amiloride-insensitive sodium channels were identified as one of the main sodium-transporting pathways in leukemia cells. To date, all known regulatory pathways of these channels are coupled with intracellular actin cytoskeleton dynamics. Here, to search for physiological mechanisms controlling epithelial Na+ channel (ENaC)-like channels, we utilized leukemia K562 cells as a unique model to examine single channel behavior in a whole-cell patch-clamp experiments. We have shown for the first time that extracellular serine protease trypsin directly activates sodium channels in plasma membrane of K562 cells. The whole-cell single current recordings clearly demonstrate no inhibition of trypsin-activated channels by amiloride or benzamil. Involvement of proteolytic cleavage in channel opening was confirmed in experiments with soybean trypsin inhibitor. More importantly, stabilization of F-actin with intracellular phalloidin did not prevent trypsin-induced channel activation indicating no implication of cytoskeleton rearrangements in stimulatory effect of extracellular protease. Our data reveals a novel mechanism modulating amiloride-insensitive ENaC-like channel activity and integral sodium permeability in leukemia cells." @default.
• W2890631218 created "2018-09-27" @default.
• W2890631218 creator A5009804972 @default.
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• W2890631218 date "2018-09-11" @default.
• W2890631218 modified "2023-09-27" @default.
• W2890631218 title "Extracellular protease trypsin activates amiloride‐insensitive sodium channels in human leukemia cells" @default.
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• W2890631218 doi "https://doi.org/10.1002/jcb.27402" @default.
• W2890631218 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30203535" @default.
• W2890631218 hasPublicationYear "2018" @default.
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