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'secretase' can also refer to...







Molecular mechanism of intramembrane proteolysis by γ-secretase

Structural Features of Human Memapsin 2 (β-Secretase) and their Biological and Pathological Implications

Gamma-secretase subunits associate in intracellular membrane compartments in Arabidopsis thaliana

Enhanced β-secretase processing alters APP axonal transport and leads to axonal defects

Phosphatidylethanolamine plasmalogen enhances the inhibiting effect of phosphatidylethanolamine on γ-secretase activity

A reporter for amyloid precursor protein γ-secretase activity in Drosophila

Modulation of beta-secretase gene expression by action of catalytic nucleic acids

Thimet Oligopeptidase Cleaves the Full-Length Alzheimer Amyloid Precursor Protein at a β-Secretase Cleavage Site in COS Cells

Presenilin 1/γ-secretase modulates P-cadherin processing and influences cell adhesion in oral squamous cell carcinoma cell lines

Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate α-secretase activity

Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific γ secretase

The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts

Pathogenic APP mutations near the γ-secretase cleavage site differentially affect Aβ secretion and APP C-terminal fragment stability


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A family of peptidases involved in processing of membrane-bound precursor molecules. α-Secretase (ADAM10, EC, 748 aa) cleaves amyloid precursor protein (APP) to produce the soluble nonamyloidogenic product sAPPα; this prevents the formation of amyloid (beta peptide. It also has TNF-convertase activity. (Beta-Secretase (BACE-1, beta-site APP cleaving enzyme 1, EC, 501 aa) is an integral membrane aspartic peptidase that generates the N-terminus of the β-amyloid protein from APP. Further cleavage is then carried out by γ-secretase, a multiprotein complex responsible for the intramembranous cleavage of the amyloid precursor protein (APP) and other type I transmembrane proteins such as notch and E-cadherin. There are four components, presenilin, nicastrin, APH-1, and PEN-2, all of which are required for activity; a fifth component, CD147, seems to have a regulatory role. Mutations in presenilin are a risk factor for Alzheimer's disease.

Subjects: Medicine and Health — Chemistry.

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