Protein Carbonylation of an Amino Acid Residue of the Na/K-ATPase α1 Subunit Determines Na/K-ATPase Signaling and Sodium Transport in Renal Proximal Tubular Cells Article (Faculty180)

cited authors

  • Yan, Yanling; Shapiro, Anna P; Mopidevi, B R; Chaudhry, Muh A; Maxwell, Kyle; Haller, S T; Drummond, Christopher A; Kennedy, David J; Tian, Jiang; Malhotra, Deepak; Xie, Zi- J; Shapiro, Joseph I; Liu, Jiang

description

  • We have demonstrated that cardiotonic steroids, such as ouabain, signaling through the Na/K-ATPase, regulate sodium reabsorption in the renal proximal tubule. By direct carbonylation modification of the Pro222 residue in the actuator (A) domain of pig Na/K-ATPase α1 subunit, reactive oxygen species are required for ouabain-stimulated Na/K-ATPase/c-Src signaling and subsequent regulation of active transepithelial (22)Na(+) transport. In the present study we sought to determine the functional role of Pro222 carbonylation in Na/K-ATPase signaling and sodium handling.

authors

publication date

  • 2016

published in

volume

  • 5