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Related Experiment Videos

Presenilins are processed by caspase-type proteases

H Loetscher1, U Deuschle, M Brockhaus

  • 1Pharma Division, Preclinical Central Nervous System Research-GeneTechnology, F. Hoffmann-La Roche Ltd., Ch-4070 Basel, Switzerland.

The Journal of Biological Chemistry
|August 15, 1997
PubMed
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Presenilin 1 (PS1) and Presenilin 2 (PS2) undergo caspase-mediated cleavage in cells, generating distinct fragments. This processing is crucial for understanding presenilin function and potential roles in neurodegenerative diseases.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Presenilin 1 (PS1) and Presenilin 2 (PS2) are endoproteolytically processed in vivo.
  • This processing yields N-terminal and C-terminal fragments of specific molecular weights.

Purpose of the Study:

  • To investigate the cleavage mechanisms of PS1 and PS2.
  • To identify the proteases responsible for PS1 and PS2 processing.

Main Methods:

  • Immunoblot and pulse-chase experiments in transfected cells.
  • Affinity chromatography, SDS-PAGE, and sequencing of C-terminal fragments.
  • Use of caspase inhibitors and cleavage site mutations.

Main Results:

  • Identified processing sites in PS1 (Asp345/Ser346) and PS2 (Asp329/Ser330) characteristic of caspase proteases.

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  • Confirmed caspase involvement in PS1 and PS2 processing using inhibitors and mutations.
  • Demonstrated cleavage of PS-derived peptide substrates by mouse brain proteolytic activity and human caspase-3.

    • Conclusions:

    • Caspase-dependent proteolysis is a key mechanism for processing Presenilin 1 and Presenilin 2.
    • Specific cleavage sites suggest a role for caspases in regulating presenilin function.
    • Additional non-caspase proteases may also contribute to PS2 processing.