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Passer B, Pellegrini L, Russo C, et al. Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. J Alzheimers Dis. 2000;2(3):289-301doi: 10.3233/jad-2000-23-408.
Passer, B., Pellegrini, L., Russo, C., Siegel, R. M., Lenardo, M. J., Schettini, G., Bachmann, M., Tabaton, M., & D'Adamio, L. (2000). Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. Journal of Alzheimer's disease : JAD, 2(3), 289-301. https://doi.org/10.3233/jad-2000-23-408
Passer, B, et al. "Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor." Journal of Alzheimer's disease : JAD vol. 2,3 (2000): 289-301. doi: https://doi.org/10.3233/jad-2000-23-408
Passer B, Pellegrini L, Russo C, Siegel RM, Lenardo MJ, Schettini G, Bachmann M, Tabaton M, D'Adamio L. Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. J Alzheimers Dis. 2000 Nov;2(3):289-301. doi: 10.3233/jad-2000-23-408. PMID: 12214090.
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J Alzheimers Dis. 2000 Nov;2(3):289-301. doi: 10.3233/jad-2000-23-408.

Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor.

Journal of Alzheimer's disease : JAD

B Passer, L Pellegrini, C Russo, R M Siegel, M J Lenardo, G Schettini, M Bachmann, M Tabaton, L D'Adamio

Affiliations

  1. T-cell apoptosis Unit, Laboratory of Cellular and Molecular Immunology, NIAID, National Institutes of Health, Bethesda, MD 20892, USA.

PMID: 12214090 DOI: 10.3233/jad-2000-23-408

Abstract

The amyloid beta protein precursor (AbetaPP) is sequentially processed by beta- and gamma-secretases to generate the Abeta peptide. The biochemical path leading to Abeta formation has been extensively studied since extracellular aggregates of amyloidogenic forms of Abeta peptide (Abeta42) are considered the culprit of Alzheimer's disease. Aside from its pathological relevance, the biological role of AbetaPP proteolysis is unknown. Although never previously described, cleavage of AbetaPP by gamma-secretase should release, together with Abeta, a COOH-terminal AbetaPP Intracellular Domain, herein termed AID. We have now identified AID-like peptides in brain tissue of normal control and patients with sporadic Alzheimer's disease and demonstrate that AID acts as a positive regulator of apoptosis. Thus, overproduction of AID may add to the toxic effect of Abeta42 aggregates and further accelerate neurodegeneration.

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