Gamma secretase
Gamma Secretase
Gamma secretase (pronunciation: /ˈɡæmə sɪˈkriːteɪz/) is an intramembrane-cleaving protease, which plays a crucial role in various cellular activities, including the pathogenesis of Alzheimer's disease.
Etymology
The term "Gamma secretase" is derived from the Greek letter gamma (γ), referring to its position in the series of secretases, and the Latin word "secretase", which is a type of enzyme that cleaves proteins.
Function
Gamma secretase is a multi-subunit protease complex, catalyzing the intramembrane cleavage of single-pass transmembrane proteins. It is involved in the processing of the amyloid precursor protein (APP), a process that generates amyloid beta peptides, the main components of amyloid plaques found in the brains of Alzheimer's disease patients.
Structure
The Gamma secretase complex is composed of four essential proteins: presenilin, nicastrin, APH-1 (anterior pharynx-defective 1), and PEN-2 (presenilin enhancer 2). Presenilin is the catalytic core of the complex, while the other three proteins are necessary for its proper assembly and activity.
Clinical Significance
Alterations in Gamma secretase activity have been linked to the development of Alzheimer's disease. Mutations in the presenilin genes, which result in altered gamma secretase activity, are the most common cause of early-onset familial Alzheimer's disease.
In addition, gamma secretase is also involved in the regulation of the Notch signaling pathway, which plays a key role in cell differentiation, proliferation, and apoptosis. Abnormal Notch signaling due to alterations in gamma secretase activity has been implicated in several types of cancer.
Related Terms
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