Amyloid-β peptides are generated in mitochondria-associated endoplasmic reticulum membranes

J Alzheimers Dis. 2015;43(2):369-74. doi: 10.3233/JAD-132543.

Abstract

Extracellular aggregates of amyloid-β peptides (Aβ) are a hallmark in Alzheimer's disease (AD) brains. Recent findings suggest that Aβ is generated intracellularly and potential production sites include endosomes and trans-Golgi network. We determined the production of Aβ in subcellular fractions isolated from mouse brain. We found that a considerable amount of Aβ is produced at mitochondria-endoplasmic reticulum (ER) contact sites including outer mitochondrial membrane and mitochondria-associated ER membranes. Enhanced Aβ production at this site may disturb ER, mitochondrial and mitochondria-ER contact site function. This may be one key step in the cascade of events eventually leading to neurodegeneration in AD.

Keywords: Alzheimer's disease; endoplasmic reticulum (ER); intracellular amyloid-β peptides; mitochondria; mitochondria-ER contact sites; mitochondria-associated ER membranes (MAM).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Brain / ultrastructure*
  • Cation Transport Proteins / metabolism
  • Electron Transport Complex IV / metabolism
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure
  • Enzyme-Linked Immunosorbent Assay
  • Female
  • Mice
  • Mice, Inbred C57BL
  • Mitochondria / metabolism*
  • Mitochondria / ultrastructure
  • Subcellular Fractions / ultrastructure

Substances

  • Amyloid beta-Peptides
  • Cation Transport Proteins
  • Electron Transport Complex IV
  • cytochrome c oxidase subunit I, mouse
  • Adenosine Triphosphatases
  • sodium-translocating ATPase