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. 2023 Mar 30;21(4):764–776. doi: 10.2174/1570159X21666230216094353

Fig. (1).

Fig. (1)

The amyloid precursor protein (APP) is a transmembrane protein, and during normal physiological condition, 90% of the APP is cleaved through α and γ-secretase and forms soluble p3 and APP intracellular domain (AICD) fragments. When a small percentage of APP molecules enter the β-secretase route, APP is cleaved by β-secretase. It results in the formation of β-APPs and membrane-bound C99 peptides. The γ-secretase cleaves the C-terminal membrane-bound C99 peptide within the transmembrane domain to produce two primary isoforms of Αβ with 40 and 42 amino acid lengths which are responsible for Αβ plaques formation.