Mitochondrial dysfunction in the type 2 diabetic heart is associated with alterations in spatially distinct mitochondrial proteomes

Am J Physiol Heart Circ Physiol. 2010 Aug;299(2):H529-40. doi: 10.1152/ajpheart.00267.2010. Epub 2010 Jun 11.

Abstract

Cardiac complications and heart failure are the leading cause of death in type 2 diabetic patients. Mitochondrial dysfunction is central in the pathogenesis of the type 2 diabetic heart. However, it is unclear whether this dysfunction is specific for a particular subcellular region. The purpose of this study was to determine whether mitochondrial dysfunction in the type 2 diabetic heart is specific to a spatially distinct subset of mitochondria. We investigated mitochondrial morphology, function, and proteomic composition of subsarcolemmal mitochondria (SSM) and interfibrillar mitochondria (IFM) in 18-wk-old db/db mice. Oxidative damage was assessed in subpopulations through the measurement of lipid peroxidation byproducts and nitrotyrosine residues. Proteomic profiles and posttranslational modifications were assessed in mitochondrial subpopulations using iTRAQ and multi-dimensional protein identification technologies, respectively. SSM from db/db hearts had altered morphology, including a decrease in size and internal complexity, whereas db/db IFM were increased in internal complexity. Db/db SSM displayed decreased state 3 respiration rates, electron transport chain activities, ATP synthase activities, and mitochondrial membrane potential and increased oxidative damage, with no change in IFM. Proteomic assessment revealed a greater impact on db/db SSM compared with db/db IFM. Inner mitochondrial membrane proteins, including electron transport chain, ATP synthesis, and mitochondrial protein import machinery, were predominantly decreased. We provide evidence that mitochondrial dysfunction in the type 2 diabetic heart is associated with a specific subcellular locale. Furthermore, mitochondrial morphological and functional indexes are impacted differently during type 2 diabetic insult and may result from the modulation of spatially distinct mitochondrial proteomes.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antioxidants / metabolism
  • Cell Respiration
  • Diabetes Mellitus, Type 2 / genetics
  • Diabetes Mellitus, Type 2 / metabolism*
  • Diabetes Mellitus, Type 2 / pathology
  • Disease Models, Animal
  • Electron Transport
  • Electron Transport Chain Complex Proteins / metabolism
  • Ion Channels / metabolism
  • Lipid Peroxidation
  • Male
  • Membrane Potential, Mitochondrial
  • Mice
  • Mitochondria, Heart / metabolism*
  • Mitochondria, Heart / pathology
  • Mitochondrial ADP, ATP Translocases / metabolism
  • Mitochondrial Proteins / metabolism*
  • Mitochondrial Proton-Translocating ATPases / metabolism
  • Mitochondrial Size
  • Oxidative Stress
  • Protein Processing, Post-Translational
  • Proteome*
  • Proteomics / methods
  • Tyrosine / analogs & derivatives
  • Tyrosine / metabolism
  • Uncoupling Protein 3

Substances

  • Antioxidants
  • Electron Transport Chain Complex Proteins
  • Ion Channels
  • Mitochondrial Proteins
  • Proteome
  • Uncoupling Protein 3
  • 3-nitrotyrosine
  • Tyrosine
  • Mitochondrial ADP, ATP Translocases
  • Mitochondrial Proton-Translocating ATPases