Mitochondrial loss, dysfunction and altered dynamics in Huntington's disease

Hum Mol Genet. 2010 Oct 15;19(20):3919-35. doi: 10.1093/hmg/ddq306. Epub 2010 Jul 21.

Abstract

Although a direct causative pathway from the gene mutation to the selective neostriatal neurodegeneration remains unclear in Huntington's disease (HD), one putative pathological mechanism reported to play a prominent role in the pathogenesis of this neurological disorder is mitochondrial dysfunction. We examined mitochondria in preferentially vulnerable striatal calbindin-positive neurons in moderate-to-severe grade HD patients, using antisera against mitochondrial markers of COX2, SOD2 and cytochrome c. Combined calbindin and mitochondrial marker immunofluorescence showed a significant and progressive grade-dependent reduction in the number of mitochondria in spiny striatal neurons, with marked alteration in size. Consistent with mitochondrial loss, there was a reduction in COX2 protein levels using western analysis that corresponded with disease severity. In addition, both mitochondrial transcription factor A, a regulator of mtDNA, and peroxisome proliferator-activated receptor-co-activator gamma-1 alpha, a key transcriptional regulator of energy metabolism and mitochondrial biogenesis, were also significantly reduced with increasing disease severity. Abnormalities in mitochondrial dynamics were observed, showing a significant increase in the fission protein Drp1 and a reduction in the expression of the fusion protein mitofusin 1. Lastly, mitochondrial PCR array profiling in HD caudate nucleus specimens showed increased mRNA expression of proteins involved in mitochondrial localization, membrane translocation and polarization and transport that paralleled mitochondrial derangement. These findings reveal that there are both mitochondrial loss and altered mitochondrial morphogenesis with increased mitochondrial fission and reduced fusion in HD. These findings provide further evidence that mitochondrial dysfunction plays a critical role in the pathogenesis of HD.

Publication types

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

MeSH terms

  • Calbindins
  • Cytochromes c / analysis
  • Cytochromes c / immunology
  • DNA, Mitochondrial / genetics
  • DNA, Mitochondrial / metabolism
  • DNA-Binding Proteins / metabolism
  • Dynamins
  • Electron Transport Complex IV / analysis
  • Energy Metabolism
  • Fluorescent Antibody Technique
  • GTP Phosphohydrolases / metabolism
  • Gene Expression
  • Gene Expression Profiling
  • Humans
  • Huntingtin Protein
  • Huntington Disease / genetics
  • Huntington Disease / metabolism*
  • Huntington Disease / pathology*
  • Membrane Potential, Mitochondrial
  • Membrane Transport Proteins / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Mitochondria / genetics
  • Mitochondria / metabolism*
  • Mitochondria / pathology*
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins / metabolism
  • Neostriatum / metabolism*
  • Neostriatum / ultrastructure*
  • Nerve Tissue Proteins / genetics
  • Neurons / chemistry
  • Neurons / pathology
  • Nuclear Proteins / genetics
  • Peroxisome Proliferator-Activated Receptors / metabolism
  • Polymerase Chain Reaction
  • S100 Calcium Binding Protein G / analysis
  • Superoxide Dismutase / analysis
  • Superoxide Dismutase / immunology
  • Transcription Factors / metabolism

Substances

  • Calbindins
  • DNA, Mitochondrial
  • DNA-Binding Proteins
  • HTT protein, human
  • Huntingtin Protein
  • Membrane Transport Proteins
  • Microtubule-Associated Proteins
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Peroxisome Proliferator-Activated Receptors
  • S100 Calcium Binding Protein G
  • Transcription Factors
  • mitochondrial transcription factor A
  • Cytochromes c
  • Superoxide Dismutase
  • superoxide dismutase 2
  • cytochrome C oxidase subunit II
  • Electron Transport Complex IV
  • GTP Phosphohydrolases
  • Mfn1 protein, human
  • DNM1L protein, human
  • Dynamins