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Updated: May 27, 2026
07:55
Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
Published on: October 17, 2015
Proteolytic processing of Alzheimer's β-amyloid precursor protein
Han Zhang1,2, Qilin Ma3, Yun-Wu Zhang1
1Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, College of Medicine, Xiamen University, Xiamen, Fujian, China.
Journal of Neurochemistry
|November 30, 2011
Summary
Alzheimer's disease involves amyloid precursor protein (APP) processing, generating toxic β-amyloid (Aβ) peptides and neuroprotective sAPP-α. Understanding APP metabolism is key to AD pathogenesis.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Alzheimer's disease (AD) pathogenesis is linked to amyloid precursor protein (APP).
- APP processing generates β-amyloid (Aβ) peptides, implicated in AD hallmarks like plaques.
- APP also yields the APP intracellular domain and neuroprotective sAPP-α via different pathways.
Purpose of the Study:
- To review mechanisms of APP metabolism.
- To elucidate functions of APP's proteolytic products.
- To enhance understanding of APP's patho/physiological roles in AD.
Main Methods:
- Literature review of APP processing pathways.
- Analysis of secretase-mediated APP cleavage.
- Examination of Aβ and sAPP-α functions.
Main Results:
- APP cleavage by β- and γ-secretase produces neurotoxic Aβ.
- Aβ aggregation and deposition are key pathological features of AD.
- α-secretase cleavage yields neuroprotective sAPP-α.
Conclusions:
- APP metabolism is a complex process with implications for AD.
- Dysregulated APP processing contributes to AD pathology.
- Targeting APP pathways may offer therapeutic strategies for AD.
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