Mitochondrial and cell-surface F0F1ATPsynthase in innate and acquired cardioprotection

J Bioenerg Biomembr. 2009 Apr;41(2):151-7. doi: 10.1007/s10863-009-9208-8.

Abstract

Mitochondria are central to heart function and dysfunction, and the pathways activated by different cardioprotective interventions mostly converge on mitochondria. In a context of perspectives in innate and acquired cardioprotection, we review some recent advances in F(0)F(1)ATPsynthase structure/function and regulation in cardiac cells. We focus on three topics regarding the mitochondrial F(0)F(1)ATPsynthase and the plasma membrane enzyme, i.e.: i) the crucial role of cardiac mitochondrial F(0)F(1)ATPsynthase regulation by the inhibitory protein IF(1) in heart preconditioning strategies; ii) the structure and function of mitochondrial F(0)F(1)ATPsynthase oligomers in mammalian myocardium as possible endogenous factors of mitochondria resistance to ischemic insult; iii) the external location and characterization of plasma membrane F(0)F(1) ATP synthase in search for possible actors of its regulation, such as IF(1) and calmodulin, at cell surface.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ATPase Inhibitory Protein
  • Animals
  • Calmodulin / chemistry
  • Calmodulin / metabolism
  • Cell Membrane / chemistry
  • Cell Membrane / enzymology*
  • Cell Membrane / pathology
  • Humans
  • Mitochondria, Heart / chemistry
  • Mitochondria, Heart / enzymology*
  • Mitochondria, Heart / pathology
  • Myocardial Ischemia / enzymology*
  • Myocardial Ischemia / pathology
  • Myocardium / enzymology*
  • Myocardium / pathology
  • Protein Structure, Quaternary
  • Proteins / chemistry
  • Proteins / metabolism
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / metabolism*
  • Structure-Activity Relationship

Substances

  • Calmodulin
  • Proteins
  • Proton-Translocating ATPases