Your browser doesn't support javascript.
loading
Influence of proteolytic cleavage of ENaC's γ subunit upon Na+ and K+ handling.
Ray, Evan C; Nickerson, Andrew; Sheng, Shaohu; Carrisoza-Gaytan, Rolando; Lam, Tracey; Marciszyn, Allison; Zhang, Lei; Jordahl, Alexa; Bi, Chunming; Winfrey, Aaliyah; Kou, Zhaohui; Gingras, Sebastien; Kirabo, Annet; Satlin, Lisa M; Kleyman, Thomas R.
Afiliación
  • Ray EC; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Nickerson A; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Sheng S; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Carrisoza-Gaytan R; Department of Pediatrics, Icahn School of Medicine at Mount Sinai, New York City, New York, United States.
  • Lam T; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Marciszyn A; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Zhang L; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Jordahl A; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Bi C; Department of Immunology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Winfrey A; Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Kou Z; Department of Immunology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Gingras S; Department of Immunology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States.
  • Kirabo A; Department of Medicine, Vanderbilt University, Nashville, Tennessee, United States.
  • Satlin LM; Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee, United States.
  • Kleyman TR; Department of Pediatrics, Icahn School of Medicine at Mount Sinai, New York City, New York, United States.
Am J Physiol Renal Physiol ; 326(6): F1066-F1077, 2024 Jun 01.
Article en En | MEDLINE | ID: mdl-38634134
ABSTRACT
The epithelial Na+ channel (ENaC) γ subunit is essential for homeostasis of Na+, K+, and body fluid. Dual γ subunit cleavage before and after a short inhibitory tract allows dissociation of this tract, increasing channel open probability (PO), in vitro. Cleavage proximal to the tract occurs at a furin recognition sequence (143RKRR146, in the mouse γ subunit). Loss of furin-mediated cleavage prevents in vitro activation of the channel by proteolysis at distal sites. We hypothesized that 143RKRR146 mutation to 143QQQQ146 (γQ4) in 129/Sv mice would reduce ENaC PO, impair flow-stimulated flux of Na+ (JNa) and K+ (JK) in perfused collecting ducts, reduce colonic amiloride-sensitive short-circuit current (ISC), and impair Na+, K+, and body fluid homeostasis. Immunoblot of γQ4/Q4 mouse kidney lysates confirmed loss of a band consistent in size with the furin-cleaved proteolytic fragment. However, γQ4/Q4 male mice on a low Na+ diet did not exhibit altered ENaC PO or flow-induced JNa, though flow-induced JK modestly decreased. Colonic amiloride-sensitive ISC in γQ4/Q4 mice was not altered. γQ4/Q4 males, but not females, exhibited mildly impaired fluid volume conservation when challenged with a low Na+ diet. Blood Na+ and K+ were unchanged on a regular, low Na+, or high K+ diet. These findings suggest that biochemical evidence of γ subunit cleavage should not be used in isolation to evaluate ENaC activity. Furthermore, factors independent of γ subunit cleavage modulate channel PO and the influence of ENaC on Na+, K+, and fluid volume homeostasis in 129/Sv mice, in vivo.NEW & NOTEWORTHY The epithelial Na+ channel (ENaC) is activated in vitro by post-translational proteolysis. In vivo, low Na+ or high K+ diets enhance ENaC proteolysis, and proteolysis is hypothesized to contribute to channel activation in these settings. Using a mouse expressing ENaC with disruption of a key proteolytic cleavage site, this study demonstrates that impaired proteolytic activation of ENaC's γ subunit has little impact upon channel open probability or the ability of mice to adapt to low Na+ or high K+ diets.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sodio / Canales Epiteliales de Sodio / Proteolisis Límite: Animals Idioma: En Revista: Am J Physiol Renal Physiol Asunto de la revista: FISIOLOGIA / NEFROLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sodio / Canales Epiteliales de Sodio / Proteolisis Límite: Animals Idioma: En Revista: Am J Physiol Renal Physiol Asunto de la revista: FISIOLOGIA / NEFROLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos