A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing.

@article{Weidemann2002ANE,
  title={A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing.},
  author={Andreas Weidemann and Simone Eggert and Friedrich B M Reinhard and Markus Vogel and Krzysztof Paliga and Gottfried Baier and Colin L. Masters and Konrad Beyreuther and Genevieve Evin},
  journal={Biochemistry},
  year={2002},
  volume={41 8},
  pages={2825-35}
}
Proteolytic processing of the transmembrane domain of the amyloid precursor protein (APP) is a key component of Alzheimer's disease pathogenesis. Using C-terminally tagged APP derivatives, we have identified by amino-terminal sequencing a novel cleavage site of APP, at Leu-49, distal to the gamma-secretase site. This was termed -cleavage. Brefeldin A treatment and pulse-chase experiments indicate that this cleavage occurs late in the secretory pathway. The level of -cleavage is decreased by… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 101 extracted citations

Biological function of Presenilin and its role in AD pathogenesis

Translational Neurodegeneration • 2013
View 7 Excerpts
Highly Influenced

Physiological functions of APP family proteins.

Cold Spring Harbor perspectives in medicine • 2012
View 10 Excerpts
Highly Influenced

Trafficking and proteolytic processing of APP.

Cold Spring Harbor perspectives in medicine • 2012
View 8 Excerpts
Highly Influenced

Interactions between APP secretases and inflammatory mediators

Journal of Neuroinflammation • 2008
View 7 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…