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Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation

Author

Listed:
  • Setsuko Sahara

    (Biomedical Research Center
    CREST of Japan Science and Technology Corporation (JST))

  • Mamoru Aoto

    (Biomedical Research Center
    CREST of Japan Science and Technology Corporation (JST))

  • Yutaka Eguchi

    (Biomedical Research Center
    CREST of Japan Science and Technology Corporation (JST))

  • Naoko Imamoto

    (Department of Anatomy and Cell Biology, Osaka University Medical School)

  • Yoshihiro Yoneda

    (Department of Anatomy and Cell Biology, Osaka University Medical School)

  • Yoshihide Tsujimoto

    (Biomedical Research Center
    CREST of Japan Science and Technology Corporation (JST))

Abstract

Apoptosis is defined by several unique morphological nuclear changes, such as chromatin condensation and nuclear fragmentation1. These changes are triggered by the activation of a family of cysteine proteases called caspases2,3, and caspase-activated DNase (CAD/DFF40)4,5 and lamin protease (caspase-6)6,7 have been implicated in some of these changes. CAD/DFF40 induces chromatin condensation in purified nuclei, but distinct caspase-activated factor(s) may be responsible for chromatin condensation8. Here we use an in vitro system to identify a new nuclear factor, designated Acinus, which induces apoptotic chromatin condensation after cleavage by caspase-3 without inducing DNA fragmentation. Immunodepletion experiments showed that Acinus is essential for apoptotic chromatin condensation in vitro, and an antisense study revealed that Acinus is also important in the induction of apoptotic chromatin condensation in cells.

Suggested Citation

  • Setsuko Sahara & Mamoru Aoto & Yutaka Eguchi & Naoko Imamoto & Yoshihiro Yoneda & Yoshihide Tsujimoto, 1999. "Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation," Nature, Nature, vol. 401(6749), pages 168-173, September.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6749:d:10.1038_43678
    DOI: 10.1038/43678
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