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Updated: Dec 28, 2025

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments
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Paraoxonase 3 functions as a chaperone to decrease functional expression of the epithelial sodium channel.

Shujie Shi1, Nicolas Montalbetti2, Xueqi Wang2,3

  • 1Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261 shs117@pitt.edu.

The Journal of Biological Chemistry
|February 22, 2020
PubMed
Summary
This summary is machine-generated.

Paraoxonase 3 (PON3) regulates epithelial sodium channel (ENaC) function by reducing its abundance and surface expression. This finding suggests PON3 plays a role in kidney sodium transport.

Keywords:
MEC-6PON3aldosteronechaperonedegenerinepithelial sodium channel (ENaC)hypertensionkidney

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • The paraoxonase (PON) family, including PON1, PON2, and PON3, are orthologs of MEC-6, an endoplasmic reticulum chaperone.
  • MEC-6 and PON2 are known to negatively regulate the epithelial sodium channel (ENaC).
  • PON3 is specifically expressed in aldosterone-sensitive distal tubules of the kidney.

Purpose of the Study:

  • To investigate the role of PON3 in modulating ion channel expression, specifically ENaC.
  • To determine if PON3's chaperone function is conserved in regulating ENaC.
  • To elucidate the mechanism by which PON3 affects ENaC function and expression.

Main Methods:

  • Knockdown of endogenous PON3 in mouse cortical collecting duct cells.
  • Heterologous expression systems: Fisher rat thyroid cells and Xenopus oocytes.
  • Co-immunoprecipitation assays to assess protein interactions.
  • Western blotting to determine protein abundance (whole-cell and surface).
  • Electrophysiological recordings to measure ENaC-mediated currents.

Main Results:

  • Knocking down PON3 in kidney cells enhanced sodium transport and increased gamma (γ) ENaC abundance.
  • PON3 co-immunoprecipitated with all three ENaC subunits in Fisher rat thyroid cells.
  • PON3 reduced the abundance of alpha (α) and γ ENaC subunits at both the whole-cell and surface levels.
  • In oocytes, PON3 inhibited ENaC currents by reducing ENaC surface expression.
  • PON3 did not affect ENaC channel open probability or activation by proteolysis or chemical means.

Conclusions:

  • PON3 negatively regulates ENaC expression and function.
  • PON3 likely inhibits ENaC biogenesis and/or trafficking.
  • PON3 plays a significant role in controlling sodium transport in the kidney.