Abstract
Alzheimer’s disease (AD) is the most prevalent form of dementia, and the numbers of AD patients are expected to increase as human life expectancy improves. Deposition of β-amyloid protein (Aβ) in the extracellular matrix and intracellular neurofibrillary tangles are molecular hallmarks of the disease. Since the precise pathophysiology of AD has not been elucidated yet, effective treatment is not available. Thus, understanding the disease pathology, as well as identification and development of valid biomarkers, is imperative for early diagnosis as well as for monitoring disease progression and therapeutic responses. Keeping this goal in mind several studies using quantitative proteomics platform have been carried out on both clinical specimens including the brain, cerebrospinal fluid (CSF), plasma and on animal models of AD. In this review, we summarize the mass spectrometry (MS)-based proteomics studies on AD and discuss the discovery as well as validation stages in brief to identify candidate biomarkers.
Highlights
Alzheimer’s disease (AD) is the most common progressive neurodegenerative disorder with memory loss, cognitive impairment, disorientation, and psychiatric symptoms
The proteomic analysis methods can be divided into discovery and targeted mass-spectrometry-based methods
Several quantitative proteomics methods including label-free, isobaric labelling based in the discovery platform and multiple-reaction monitoring (MRM), PRM and data-independent analysis (DIA) in the targeted platform have been employed for AD biomarker discover and understanding AD pathogenesis
Summary
Alzheimer’s disease (AD) is the most common progressive neurodegenerative disorder with memory loss, cognitive impairment, disorientation, and psychiatric symptoms. Munsunuri et al used dimethyl labeling to compare proteome changes in temporal neocortex in Alzheimer’s disease (AD) patients and non-AD individuals They observed significant alterations in 69 proteins involved in several pathways including energy metabolism, glycolysis, oxidative stress, apoptosis, signal transduction, and synaptic functioning [10]. Bai et al performed a deep proteome analysis of detergentinsoluble protein aggregates from brain tissue and identified ~4000 proteins, including U1–70K and other U1 small nuclear ribonucleoprotein (U1 snRNP) spliceosome components in AD as well as MCI samples [22] Such insights underscore the need for further functional studies to probe the exact role of aggregate-associated proteins in AD, and mass-spectrometry-based proteomics may prove to be an invaluable tool
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