2. Academic Validation
  3. Amyloid precursor protein processing and bioenergetics

Amyloid precursor protein processing and bioenergetics

  • Brain Res Bull. 2017 Jul;133:71-79. doi: 10.1016/j.brainresbull.2016.08.009.
Heather M Wilkins 1,  Russell H Swerdlow 2
Affiliations

Affiliations

  • 1 Department of Neurology University of Kansas Medical Center, Kansas City, KS, USA; University of Kansas Alzheimer's Disease Center, Kansas City, KS, USA.
  • 2 Department of Neurology University of Kansas Medical Center, Kansas City, KS, USA; University of Kansas Alzheimer's Disease Center, Kansas City, KS, USA; Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS, USA; Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS USA. Electronic address: rswerdlow@kumc.edu.
PMID: 27545490 DOI: 10.1016/j.brainresbull.2016.08.009
Abstract

The processing of amyloid precursor protein (APP) to amyloid beta (Aβ) is of great interest to the Alzheimer's disease (AD) field. Decades of research define how APP is altered to form Aβ, and how Aβ generates oligomers, protofibrils, and fibrils. Numerous signaling pathways and changes in cell physiology are known to influence APP processing. Existing data additionally indicate a relationship exists between mitochondria, bioenergetics, and APP processing. Here, we review data that address whether mitochondrial function and bioenergetics modify APP processing and Aβ production.

Keywords

Alpha secretase; Alzheimer's disease; Amyloid beta; Amyloid precursor protein; BACE1; Bioenergetics; Gamma secretase; Mitochondria.

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