Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from gamma-secretase.

@article{Campbell2003PresenilinEM,
  title={Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from gamma-secretase.},
  author={William A. Campbell and Megan L O Reed and Jennifer M. Strahle and Michael S Wolfe and Weiming Xia},
  journal={Journal of neurochemistry},
  year={2003},
  volume={85 6},
  pages={1563-74}
}
Presenilin (PS)-dependent gamma-secretase cleavage is the final proteolytic step in generating amyloid beta protein (A beta), a key peptide involved in the pathogenesis of Alzheimer's disease. PS undergoes endoproteolysis by an unidentified 'presenilinase' to generate the functional N-terminal and C-terminal fragment heterodimers (NTF/CTF) that may harbor the gamma-secretase active site. To better understand the relationship between presenilinase and gamma-secretase, we characterized the… CONTINUE READING

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