Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production.

@article{Benjannet2001PosttranslationalPO,
  title={Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production.},
  author={Suzanne Benjannet and Aram Elagoz and Louise Wickham and Maya A Mamarbachi and Jon Scott Munzer and Amit Basak and Claude Lazure and James A. Cromlish and Sangram S. Sisodia and Fr{\'e}d{\'e}ric Checler and Michel Chr{\'e}tien and Nabil G Seidah},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 14},
  pages={10879-87}
}
Processing of the beta-amyloid precursor protein (betaAPP) by beta- and gamma-secretases generates the amyloidogenic peptide Abeta, a major factor in the etiology of Alzheimer's disease. Following the recent identification of the beta-secretase beta-amyloid-converting enzyme (BACE), we herein investigate its zymogen processing, molecular properties, and cellular trafficking. Our data show that among the proprotein convertase family members, furin is the major converting enzyme of pro-BACE into… CONTINUE READING
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