A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-01-01

AUTHORS

Masato Enari, Hideki Sakahira, Hideki Yokoyama, Katsuya Okawa, Akihiro Iwamatsu, Shigekazu Nagata

ABSTRACT

The homeostasis of animals is regulated not only by the growth and differentiation of cells, but also by cell death through a process known as apoptosis. Apoptosis is mediated by members of the caspase family of proteases, and eventually causes the degradation of chromosomal DNA. A caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD) have now been identified in the cytoplasmic fraction of mouse lymphoma cells. CAD is a protein of 343 amino acids which carries a nuclear-localization signal; ICAD exists in a long and a short form. Recombinant ICAD specifically inhibits CAD-induced degradation of nuclear DNA and its DNase activity. When CAD is expressed with ICAD in COS cells or in a cell-free system, CAD is produced as a complex with ICAD: treatment with caspase 3 releases the DNase activity which causes DNA fragmentation in nuclei. ICAD therefore seems to function as a chaperone for CAD during its synthesis, remaining complexed with CAD to inhibit its DNase activity; caspases activated by apoptotic stimuli then cleave ICAD, allowing CAD to enter the nucleus and degrade chromosomal DNA. More... »

PAGES

43-50

Journal

TITLE

Nature

ISSUE

6662

VOLUME

391

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/34112

    DOI

    http://dx.doi.org/10.1038/34112

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1019010983

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9422506


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