Presenilins are processed by caspase-type proteases.

@article{Loetscher1997PresenilinsAP,
  title={Presenilins are processed by caspase-type proteases.},
  author={Hansruedi Loetscher and Ulrich Deuschle and Manfred Brockhaus and Didier Reinhardt and Peter Nelboeck and Jan Mous and J{\"u}rgen Gr{\"u}nberg and Christian Haass and Helmut Jacobsen},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 33},
  pages={20655-9}
}
Presenilin 1 (PS1) and presenilin 2 (PS2) are endoproteolytically processed in vivo and in cell transfectants to yield 27-35-kDa N-terminal and 15-24-kDa C-terminal fragments. We have studied the cleavage of PS1 and PS2 in transiently and stably transfected hamster kidney and mouse and human neuroblastoma cells by immunoblot and pulse-chase experiments. C-terminal fragments were isolated by affinity chromatography and SDS-polyacrylamide gel electrophoresis and sequenced. The processing sites… CONTINUE READING

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