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J Biol Chem, Vol. 274, Issue 9, 5953-5962, February 26, 1999
From the a Ottawa Regional Cancer Center Research
Laboratories, Ottawa, Ontario K1H 8L6, the b Department of
Biochemistry, University of Ottawa,
Ottawa, Ontario K1H 8M5, Canada, the d Department of
Molecular Biology, University of Geneva, 30 Quai Ernest-Ansermet,
CH-1211 Geneva, Switzerland, the g Division of Hematology,
Ottawa General Hospital, Ottawa, Ontario K1H 8L6, the
f Department of Oncology and Medicine, Lady Davis Institute for
Medical Research, Montreal, Quebec H3T 1E2, the h Department
of Microbiology and Immunology, University of Ottawa, Ottawa,
Ontario K1H 8M5, and the e Department of Biochemistry, McGill
University, Montreal, Quebec H3G 1Y6, Canada
The interferon-inducible, double-stranded
RNA-dependent protein kinase PKR has been implicated in
anti-viral, anti-tumor, and apoptotic responses. Others have attempted
to examine the requirement of PKR in these roles by targeted disruption
at the amino terminal-encoding region of the Pkr gene. By
using a strategy that aims at disruption of the catalytic domain of
PKR, we have generated mice that are genetically ablated for functional
PKR. Similar to the other mouse model of Pkr disruption, we
have observed no consequences of loss of PKR on tumor suppression.
Anti-viral response to influenza and vaccinia also appeared to be
normal in mice and in cells lacking PKR. Cytokine signaling in the type I interferon pathway is normal but may be compromised in the
erythropoietin pathway in erythroid bone marrow precursors. Contrary to
the amino-terminal targeted Pkr mouse, tumor necrosis
factor
Characterization of Transgenic Mice with Targeted Disruption of
the Catalytic Domain of the Double-stranded RNA-dependent
Protein Kinase, PKR
-induced apoptosis and the anti-viral apoptosis response to
influenza is not impaired in catalytic domain-targeted
Pkr-null cells. The observation of intact eukaryotic
initiation factor-2 phosphorylation in these Pkr-null
cells provides proof of rescue by another eukaryotic initiation
factor-2 kinase(s).
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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