Hypoxia-up-regulated mitochondrial movement regulator does not contribute to the APP/PS1 double transgenic mouse model of Alzheimer's disease

Dement Geriatr Cogn Disord. 2013;36(3-4):137-45. doi: 10.1159/000351669. Epub 2013 Jul 27.

Abstract

Background/aims: It has been demonstrated that mitochondrial dysfunction is associated with Alzheimer's disease (AD); meanwhile, hypoxia-up-regulated mitochondrial movement regulator (HUMMR) plays an important role in regulating mitochondrial function. The present study aimed to confirm the association between HUMMR and mitochondrial function in AD.

Methods: We detected the expression of HUMMR at transcriptional and translational levels in APP/PS1 double transgenic mice using real-time quantitative RT-PCR and Western blotting. Age- and gender-matched wild-type (WT) littermates were used as controls. Mitochondrial morphology was observed in the hippocampus and cortex of APP/PS1 double transgenic mice using transmission electron microscopy.

Results: Damage to mitochondrial morphology in the hippocampus and cortex of APP/PS1 double transgenic mice was found, including swelling and cavitations. Our analysis showed no statistical differences in the expression of HUMMR between APP/PS1 double transgenic mice and WT littermates (p > 0.05). These results showed that there was no association between HUMMR and mitochondrial dysfunction in APP/PS1 transgenic mice.

Conclusion: These results indicate that HUMMR does not play a key role in mitochondrial dysfunction in the APP/PS1 double transgenic AD mouse.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / genetics*
  • Alzheimer Disease / psychology
  • Amyloid beta-Protein Precursor / genetics*
  • Amyloid beta-Protein Precursor / physiology*
  • Animals
  • Blotting, Western
  • Cerebral Cortex / pathology
  • Cerebral Cortex / ultrastructure
  • Exons / genetics
  • Eye Proteins
  • Female
  • Hippocampus / pathology
  • Hippocampus / ultrastructure
  • Humans
  • Male
  • Membrane Proteins / genetics*
  • Membrane Proteins / physiology*
  • Mice
  • Mice, Transgenic
  • Microscopy, Electron
  • Mitochondria / physiology
  • Mitochondria / ultrastructure
  • Mitochondrial Proteins
  • Presenilin-1 / genetics*
  • Presenilin-1 / physiology*
  • Real-Time Polymerase Chain Reaction
  • Transgenes

Substances

  • Amyloid beta-Protein Precursor
  • Eye Proteins
  • MGARP protein, mouse
  • Membrane Proteins
  • Mitochondrial Proteins
  • Presenilin-1