:
Alzheimer’s disease (AD) is a progressive brain disorder and one of the most common
causes of dementia and death. AD can be of two types; early-onset and late-onset, where late-onset
AD occurs sporadically while early-onset AD results from a mutation in any of the three genes that
include amyloid precursor protein (APP), presenilin 1 (PSEN 1) and presenilin 2 (PSEN 2). Biologically,
AD is defined by the presence of the distinct neuropathological profile that consists of the extracellular
β-amyloid (Aβ) deposition in the form of diffuse neuritic plaques, intraneuronal neurofibrillary
tangles (NFTs) and neuropil threads; in dystrophic neuritis, consisting of aggregated hyperphosphorylated
tau protein. Elevated levels of (Aβ), total tau (t-tau) and phosphorylated tau (ptau)
in cerebrospinal fluid (CSF) have become an important biomarker for the identification of this
neurodegenerative disease. The aggregation of Aβ peptide derived from amyloid precursor protein
initiates a series of events that involve inflammation, tau hyperphosphorylation and its deposition,
in addition to synaptic dysfunction and neurodegeneration, ultimately resulting in dementia. The
current review focuses on the role of proteomes in the pathogenesis of AD.
Critical role of mitosis in spontaneous late-onset Alzheimer’s disease; from a Shugoshin 1 cohesinopathy mouse model
