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Blood, Vol. 92 No. 7 (October 1), 1998:
pp. 2450-2460
Regulation of the c-jun Gene in p210 BCR-ABL Transformed
Cells Corresponds With Activity of JNK, the c-jun N-Terminal
Kinase
Gem S. Burgess,
Elizabeth A. Williamson,
Larry D. Cripe,
Sara Litz-Jackson,
Jay A. Bhatt,
Kurt Stanley,
Mark J. Stewart,
Andrew
S. Kraft,
Harikrishna Nakshatri, and
H. Scott Boswell
From the Walther Cancer Institute, and the Hematology/Oncology
Division, the Departments of Medicine, and Surgery, Indiana University
School of Medicine, Indianapolis, IN; and the Division of Medical
Oncology, University of Colorado Health Sciences Center, Denver.
Activity of the c-jun N-terminal kinase (JNK)
has been shown in hematopoietic cells transformed by p210
BCR-ABL. However, analysis has not been reported for
hematopoietic cells on the consequences of this activity for
c-jun promoter regulation within its distinctive proximal
8-base consensus CRE-like element, an element linked to JNK-mediated
increase in c-jun transcription. In the present study,
regulation of the proximal c-jun promoter was studied in murine
myeloid cells transformed by p210 BCR-ABL. Promoter regulation in p210
BCR-ABL transformed cells was compared with regulation of the promoter
in nontransformed interleukin-3 (IL-3)-dependent parental cells. The
composition of nuclear AP-1 proteins contained within cells with p210
BCR-ABL, and their binding to the c-jun promoter proximal
CRE-like element, was compared with the composition and binding of AP-1
proteins in IL-3-treated parental cells without p210 BCR-ABL. The
present analysis found fivefold increased c-jun transcription
occurring in p210 BCR-ABL transformed murine myeloid cells possessing a
corresponding magnitude of increased kinase activity of JNK, compared
with IL-3-stimulated parental cells. Augmented JNK activity was
accompanied by increased nuclear abundance of c-jun and
c-fos proteins that bound specifically to the proximal
c-jun promoter CRE element. Also, representative human leukemic
cell lines expressing p210 BCR-ABL and possessing abundant kinase
activity of JNK, when compared with parental cells that were deficient
in JNK activity, had increased c-jun and c-fos proteins. Finally, to show the relevance of these observations in model
systems, we studied blast cells from patients with Philadelphia chromosome-positive acute leukemic transformation, and observed comparable activities of JNK catalysis and c-jun/AP-1 protein relative to the cell lines that possessed p210 BCR-ABL and JNK activity. These studies provide a basis for investigating the set of
downstream genes which augmented c-jun/AP-1 activity enlists in
the process of transformation by p210 BCR-ABL.
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