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J Biol Chem, Vol. 274, Issue 31, 21651-21658, July 30, 1999
From the AML2 is a member of the acute myelogenous
leukemia, AML family of transcription factors. The biologic functions
of AML1 and AML3 have been well characterized; however, the functional
role of AML2 remains unknown. In this study, we found that AML2 protein expressed predominantly in cells of hematopoietic origin is a nuclear
serine phosphoprotein associated with the nuclear matrix, and its
expression is not cell cycle-related. In HL-60 cells AML2 expression
can be induced by all three natural retinoids,
all-trans-retinoic acid (RA), 13-cis-RA, and
9-cis-RA in a dose-dependent manner. A
synthetic retinoic acid derivative, 4HPR, which neither activates RA
receptor (RAR)
Regulation of AML2/CBFA3 in Hematopoietic Cells through the
Retinoic Acid Receptor
-Dependent Signaling Pathway
,,
,, and
Division of Pathology and Laboratory
Medicine and the Departments of ¶ Hematology, Clinical
Investigation3, ** Bioimmunotherapy, and
Molecular Pathology, the University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 and
§ Department of Molecular Genetics, the Weizmann Institute
of Science, Rehovot, Israel
nor retinoic X receptor was unable to induce the
expression of AML2. A RAR-selective activator, TTNPB, induced AML2
expression similar to RA. Our study further showed that AGN193109, a
potent RAR antagonist, suppressed AML2 expression induced by RA and
that a retinoic X receptor pan agonist AGN194204 had no effect on its
expression. Taken together, these studies conclusively demonstrated
that the expression of AML2 in HL-60 cells is regulated through the
RAR-specific signaling pathway. Our study further showed that after
all-trans-retinoic acid priming, AML2 expression could be
augmented by vitamin D3. Based on these studies we
hypothesize that AML2 expression is normally regulated by
retinoid/vitamin D nuclear receptors mainly through the
RAR-dependent signaling pathway and that it may play a
role in hematopoietic cell differentiation.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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