γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting

  • Authors:
    • Hideaki Kume
    • Yoshiki Sekijima
    • Kei Maruyama
    • Fuyuki Kametani
  • View Affiliations

  • 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.

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July 2003
Volume 12 Issue 1

Print ISSN: 1107-3756
Online ISSN:1791-244X

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Spandidos Publications style
Kume H, Sekijima Y, Maruyama K and Kametani F: γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting. Int J Mol Med 12: 57-60, 2003.
APA
Kume, H., Sekijima, Y., Maruyama, K., & Kametani, F. (2003). γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting. International Journal of Molecular Medicine, 12, 57-60. https://doi.org/10.3892/ijmm.12.1.57
MLA
Kume, H., Sekijima, Y., Maruyama, K., Kametani, F."γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting". International Journal of Molecular Medicine 12.1 (2003): 57-60.
Chicago
Kume, H., Sekijima, Y., Maruyama, K., Kametani, F."γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting". International Journal of Molecular Medicine 12, no. 1 (2003): 57-60. https://doi.org/10.3892/ijmm.12.1.57