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The ?-secretase complex: from structure to function.

ABSTRACT: One of the most critical pathological features of Alzheimer's disease (AD) is the accumulation of ?-amyloid (A?) peptides that form extracellular senile plaques in the brain. A? is derived from ?-amyloid precursor protein (APP) through sequential cleavage by ?- and ?-secretases. ?-secretase is a high molecular weight complex minimally composed of four components: presenilins (PS), nicastrin, anterior pharynx defective 1 (APH-1), and presenilin enhancer 2 (PEN-2). In addition to APP, ?-secretase also cleaves many other type I transmembrane (TM) protein substrates. As a crucial enzyme for A? production, ?-secretase is an appealing therapeutic target for AD. Here, we summarize current knowledge on the structure and function of ?-secretase, as well as recent progress in developing ?-secretase targeting drugs for AD treatment.

SUBMITTER: Zhang X 

PROVIDER: S-EPMC4263104 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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The γ-secretase complex: from structure to function.

Zhang Xian X   Li Yanfang Y   Xu Huaxi H   Zhang Yun-Wu YW  

Frontiers in cellular neuroscience 20141211

One of the most critical pathological features of Alzheimer's disease (AD) is the accumulation of β-amyloid (Aβ) peptides that form extracellular senile plaques in the brain. Aβ is derived from β-amyloid precursor protein (APP) through sequential cleavage by β- and γ-secretases. γ-secretase is a high molecular weight complex minimally composed of four components: presenilins (PS), nicastrin, anterior pharynx defective 1 (APH-1), and presenilin enhancer 2 (PEN-2). In addition to APP, γ-secretase  ...[more]

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