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J. Biol. Chem., Vol. 276, Issue 5, 3683-3690, February 2, 2001
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From The cytotoxic T lymphocyte protease granzyme A
induces caspase-independent cell death in which DNA single-strand
nicking is observed instead of oligonucleosomal fragmentation. Granzyme
A is a specific tryptase that concentrates in the nucleus of targeted cells and synergistically enhances DNA fragmentation induced by the
caspase activator granzyme B. Here we show that granzyme A treatment of
isolated nuclei enhances DNA accessibility to exogenous endonucleases.
In vitro and after cell loading with perforin, GrnA
completely degrades histone H1 and cleaves core histones into ~16-kDa
fragments. Histone digestion provides a mechanism for unfolding
compacted chromatin and facilitating endogenous DNase access to DNA
during T cell and natural killer cell granule-mediated apoptosis.
Induction of Rapid Histone Degradation by the Cytotoxic T
Lymphocyte Protease Granzyme A*
§,§,
, and§**
The Center for Blood Research,
¶ Massachusetts General Hospital and § Department of
Pediatrics, Harvard Medical School, Boston, Massachusetts 02115 and
Manitoba Institute of Cell Biology, University of Manitoba,
Winnipeg, R3E OV9 Canada
*
This work was supported by National Institutes of Health
Grant AI45587.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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