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J. Biol. Chem., Vol. 276, Issue 8, 5992-5999, February 23, 2001
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From the Cellular and Molecular Biochemistry Research Laboratory
(151), Department of Laboratory Medicine and Pathology and
University of Minnesota Cancer Center, University of Minnesota and
the Department of Veterans Affairs Medical Center, Minneapolis,
Minnesota 55417 and the § Transgenic Oncogenesis Group,
Laboratory of Cell Regulation and Carcinogenesis, NCI, National
Institutes of Health, Bethesda, Maryland 20892
Protein kinase CK2 (CK2) has long been implicated
in the regulation of cell growth and proliferation. Its activity is
generally elevated in rapidly proliferating tissues, and nuclear matrix (NM) is an important subnuclear locale of its functional signaling. In
the prostate, nuclear CK2 is rapidly lost commensurate with induction
of receptor-mediated apoptosis after growth stimulus withdrawal. By
contrast, chemical-induced apoptosis in prostate cancer and other cells
(by etoposide and diethylstilbestrol) evokes an enhancement in CK2
associated with the NM that appears to be because of translocation of
CK2 from the cytoplasmic to the nuclear compartment. This shuttling of
CK2 to the NM may reflect a protective response to chemical-mediated
apoptosis. Supporting evidence for this was obtained by employing cells
that were transiently transfected with various expression plasmids of
CK2 (thereby expressing additional CK2) prior to treatment with
etoposide or diethylstilbestrol. Cells transfected with the CK2
A Potential Role of Nuclear Matrix-associated Protein Kinase CK2
in Protection against Drug-induced Apoptosis in Cancer Cells*
,
or
CK2
showed significant resistance to chemical-mediated
apoptosis commensurate with the corresponding elevation in
CK2 in the NM. Transfection with CK2 did not demonstrate this
effect. These results suggest, for the first time, that besides the
commonly appreciated function of CK2 in cell growth, it may also have a
role in protecting cells against apoptosis.
*
This work was supported in part by United States Public
Health Service Research Grant CA-15062 awarded by the NCI, DHHS,
National Institutes of Health and by the Medical Research Fund of the
Department of Veterans Affairs.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.
Present address: Duke University Medical Center, Durham, NC.
¶
To whom correspondence should be addressed: Cellular and
Molecular Biochemistry Research Laboratory (151), Veterans Affairs Medical Center, One Veterans Dr., Minneapolis, MN 55417. Tel.: 612-725-2000 (ext. 2594); Fax: 612-725-2093; E-mail:
ahmedk@tc.umn.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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