APP processing in Alzheimer's disease
By Yun-wu Zhang, Robert C Thompson, Han Zhang, Huaxi Xu. Molecular Brain, 2011
910 citations recorded by the source corpus.
An important pathological feature of Alzheimer's disease (AD) is the presence of extracellular senile plaques in the brain. Senile plaques are composed of aggregations of small peptides called β-amyloid (Aβ). Multiple lines of evidence demonstrate that overproduction/aggregation of Aβ in the brain is a primary cause of AD and inhibition of Aβ generation has become a hot topic in AD research. Aβ is generated from β-amyloid precursor protein (APP) through sequential cleavages first by β-secretase and then by γ-secretase complex. Alternatively, APP can be cleaved by α-secretase within the Aβ domain to release soluble APPα and preclude Aβ generation. Cleavage of APP by caspases may also contribute to AD pathologies. Therefore, understanding the metabolism/processing of APP is crucial for AD therapeutics. Here we review current knowledge of APP processing regulation as well as the patho/physiological functions of APP and its metabolites.
Subfields: Cellular and Molecular Neuroscience, Pharmacology, Physiology
View Paper: https://www.semanticscholar.org/paper/b81bb319470dbdacb05f1e5fa11e8cc23eb1232e
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In Cellular and Molecular Neuroscience
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Citations in the corpus
- Decoding Alzheimer's disease from perturbed cerebral glucose metabolism: implications for diagnostic and therapeutic strategies. (2013, background): “Both clinical and experimental studies have demonstrated that thiamine-dependent biological processes and thiamine metabolism are specifically involved in AD (Gold et al., 1998; Gold, 2005; Zhang et al., 2011a).”
- Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “In brain, BACE1 is the major β-secretase, while γ-secretase is comprised of at least four core components, including presenilins (PS1 and PS2), niacstrin, PEN2, and APH1 [27].”