γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting
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- Published online on: July 1, 2003 https://doi.org/10.3892/ijmm.12.1.57
- Pages: 57-60
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Abstract
Aβ is the major component of amyloid in the brain in Alzheimer's disease and is derived from an amyloid precursor protein (APP) by the sequential proteolytic processing of two putative proteases, called β- and γ-secretase. To clarify the mechanism of γ-secretase processing, we created constructs contained the C-terminal domain of APP and analyzed the processing in COS-1 cells. We found that C-terminal fragments (CTFs) containing a short extra N-terminal region before the β-secretase cleavage site were directly processed at γ-secretase cleavage site. This suggests that γ-secretase cleavage occurs independently and is not dependent on α- and β-secretase cleavage.
