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Related Experiment Video

Updated: Sep 11, 2025

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments
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Extracellular serine proteases activate amiloride-insensitive ENaC channels and decrease migration and invasion

Daria V Lysikova1, Polina I Kirillova1, Irina O Vassilieva2

  • 1Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.

American Journal of Physiology. Cell Physiology
|August 18, 2025
PubMed
Summary
This summary is machine-generated.

Extracellular serine proteases like α-chymotrypsin and plasmin activate epithelial sodium channels (ENaCs) in leukemia cells, reducing their migration and invasion. This highlights a new role for serine proteases in regulating cancer cell motility via ENaC channels.

Keywords:
human leukemia cellsmigrationplasminα-chymotrypsinδ-ENaC

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Ion Channel Physiology

Background:

  • Epithelial sodium channels (ENaCs) are implicated in cancer cell proliferation, apoptosis, and motility.
  • Previous studies showed trypsin stimulates amiloride-insensitive ENaC-like channels in leukemia K562 cells.
  • The role of various serine proteases in regulating sodium channels and cancer progression in blood cells is unclear.

Purpose of the Study:

  • To investigate the effect of serine proteases α-chymotrypsin and plasmin on sodium channels in leukemia cells.
  • To determine the functional role of protease-activated sodium channels in leukemia cell migration and invasion.
  • To elucidate the involvement of δ-ENaC in protease-induced channel activity and its impact on cancer cell behavior.

Main Methods:

  • Single-channel whole-cell patch-clamp electrophysiology to study sodium channel activity.
  • δ-ENaC knockdown (KD) in K562 cells to assess subunit involvement.
  • In vitro migration and invasion assays to evaluate cell motility.
  • Use of serine protease inhibitors (SBTI, α2-antiplasmin) to confirm the role of proteolytic activity.

Main Results:

  • α-chymotrypsin and plasmin directly activated sodium channels in K562 and U937 leukemia cell lines.
  • δ-ENaC knockdown prevented α-chymotrypsin-induced channel activation, confirming δ-ENaC's role.
  • α-chymotrypsin and plasmin significantly reduced migration and invasion of K562 cells; this effect was partially abolished by δ-ENaC KD.
  • α-chymotrypsin reduced migration in U937 and HL-60 cells but not in MOLT-4 cells lacking functional ENaCs.
  • Protease inhibitors blocked the effect on cell migration/invasion, indicating the necessity of proteolytic activity.

Conclusions:

  • Extracellular serine proteases α-chymotrypsin and plasmin activate sodium channels, involving δ-ENaC, in leukemia cells.
  • These proteases decrease leukemia cell migration and invasion, suggesting a regulatory role in cancer progression.
  • Serine proteases act as regulators of sodium permeability via ENaC, impacting the motility of transformed blood cells.