Regulation of the cardiac sodium pump

W. Fuller*, Lindsay Tulloch, M. J. Shattock, S. C. Calaghan, J. Howie, K. J. Wypijewski

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

40 Citations (Scopus)

Abstract

In cardiac muscle, the sarcolemmal sodium/potassium ATPase is the principal quantitative means of active transport at the myocyte cell surface, and its activity is essential for maintaining the trans-sarcolemmal sodium gradient that drives ion exchange and transport processes that are critical for cardiac function. The 72-residue phosphoprotein phospholemman regulates the sodium pump in the heart: unphosphorylated phospholemman inhibits the pump, and phospholemman phosphorylation increases pump activity. Phospholemman is subject to a remarkable plethora of post-translational modifications for such a small protein: the combination of three phosphorylation sites, two palmitoylation sites, and one glutathionylation site means that phospholemman integrates multiple signaling events to control the cardiac sodium pump. Since misregulation of cytosolic sodium contributes to contractile and metabolic dysfunction during cardiac failure, a complete understanding of the mechanisms that control the cardiac sodium pump is vital. This review explores our current understanding of these mechanisms.

Original languageEnglish
Pages (from-to)1357-1380
Number of pages24
JournalCellular and Molecular Life Sciences
Volume70
Issue number8
DOIs
Publication statusPublished - Apr 2013

Keywords

  • Heart
  • Protein kinase C
  • Protein kinase A
  • Sodium pump
  • BETA-ADRENERGIC STIMULATION
  • PHOSPHOLEMMAN-INDUCED MODULATION
  • MITOCHONDRIAL CA2+ UPTAKE
  • SITE-DIRECTED MUTAGENESIS
  • Palmitoylation
  • CURRENT-VOLTAGE RELATIONSHIP
  • Phospholemman
  • PIG VENTRICULAR MYOCYTES
  • Ion transport
  • FXYD
  • Intracellular sodium
  • PROTEIN-KINASE-C
  • OXIDANT-INDUCED ACTIVATION
  • NA+-K+ PUMP
  • NA+-CA2+ EXCHANGE CURRENT

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