The initiation and progression of Alzheimer disease (AD) is a complex process not yet fully understood. While many hypotheses have been provided as to the cause of the disease, the exact mechanisms remain elusive and difficult to verify. Proteomic applications in disease models of AD have provided valuable insights into the molecular basis of this disorder, demonstrating that on a protein level, disease progression impacts numerous cellular processes such as energy production, cellular structure, signal transduction, synaptic function, mitochondrial function, cell cycle progression, and proteasome function. Each of these cellular functions contributes to the overall health of the cell, and the dysregulation of one or more could contribute to the pathology and clinical presentation in AD. In this review, foci reside primarily on the amyloid β-peptide (Aβ) induced oxidative stress hypothesis and the proteomic studies that have been conducted by our laboratory and others that contribute to the overall understanding of this devastating neurodegenerative disease. This article is part of a Special Issue entitled: Misfolded Proteins, Mitochondrial Dysfunction, and Neurodegenerative Diseases.
|Number of pages||10|
|Journal||Biochimica et Biophysica Acta - Molecular Basis of Disease|
|State||Published - Aug 1 2014|
Bibliographical noteFunding Information:
This work was supported in part by a NIH grant to D.A.B. [ AG-05119 ].
- Alzheimer disease
- Oxidative stress
- Redox proteomics
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology