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J Biol Chem, Vol. 274, Issue 13, 8437-8444, March 26, 1999
From the Department of Pharmacology, University of Michigan, School
of Medicine, Ann Arbor, Michigan 48109-0632
1,25-Dihydroxyvitamin D3
(1,25-(OH)2D3) suppresses c-myc
expression during differentiation of HL-60 cells along the monocytic pathway by blocking transcriptional elongation at the first exon/intron border of the c-myc gene. In the present study, the
physiological relevance of three putative regulatory protein binding
sites found within a 280-base pair region in intron 1 of the
c-myc gene was explored. HL-60 promyelocytic leukemia cells
were transiently transfected with three different c-myc
promoter constructs cloned upstream of a chloramphenicol
acetyltransferase (CAT) reporter gene. With the wild-type
c-myc promoter construct (pMPCAT), which contains MIE1,
MIE2, and MIE3 binding sites, 1,25-(OH)2D3 was able to decrease CAT activity by 45.4 ± 7.9% (mean ± S.E.,
n = 8). The ability of
1,25-(OH)2D3 to inhibit CAT activity was
significantly decreased to 18.5 ± 4.3% (59.3% reversal,
p < 0.02) when examined with a MIE1 deletion
construct (pMPCAT-MIE1). Moreover, 1,25-(OH)2D3 was completely ineffective at suppressing CAT activity in cells transfected with pMPCAT-287, a construct without MIE1, MIE2, and MIE3
binding sites (
c-myc Intron Element-binding Proteins Are Required
for 1,25-Dihydroxyvitamin D3 Regulation of
c-myc during HL-60 Cell Differentiation and the
Involvement of HOXB4
6.5 ± 10.9%, p < 0.002).
MIE1- and MIE2-binding proteins induced by
1,25-(OH)2D3 had similar gel shift mobilities, while MIE3-binding proteins migrated differently. Furthermore, chelerythrine chloride, a selective protein kinase C (PKC) inhibitor, and a PKC
antisense oligonucleotide completely blocked the binding of nuclear proteins induced by 1,25-(OH)2D3 to
MIE1, MIE2, and MIE3. A 1,25-(OH)2D3-inducible
MIE1-binding protein was identified to be HOXB4. HOXB4 levels were
significantly increased in response to
1,25-(OH)2D3. Taken together, these results
indicate that HOXB4 is one of the nuclear phosphoproteins involved in
c-myc transcription elongation block during HL-60 cell
differentiation by 1,25-(OH)2D3.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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