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Stat1 is induced and activated by all-trans retinoic acid in acute
promyelocytic leukemia cells
M Gianni, M Terao, I Fortino, M LiCalzi, V Viggiano, T Barbui, A Rambaldi and E Garattini
Molecular Biology Unit, Centro Catullo e Daniela Borgomainerio, Istituto di
Ricerche Farmacologiche Mario Negri, Milan, Italy.
Treatment of freshly isolated acute promyelocytic leukemia (APL) cells and
the myelogenous leukemia cell lines, NB4, HL-60, and U937, with all- trans
retinoic acid (ATRA) results in a remarkable elevation in the amounts of
Stat1 alpha and Stat2 proteins. Stat1 alpha protein levels are augmented by
ATRA as a consequence of elevated amounts of the corresponding transcripts.
The retinoid increases the levels of nuclear complexes that are capable of
binding to interferon (IFN)-regulated consensus sequences and contain Stat1
and/or Stat2 proteins, and causes a rapid and long-lasting elevation in
Stat1 alpha tyrosine phosphorylation. Transient transfection experiments
show that ATRA enhances the transactivating properties of Stat1 alpha
observed on an appropriate reporter gene, in the presence of the RAR alpha
retinoic acid receptor, but not in the presence of the PML-RAR protein.
Treatment of NB4 cells with ATRA is associated with a remarkable
upregulation of the two IFN-responsive genes IFN-responsive factor 1 and
2'-5' oligoadenylate synthetase, as well as with an augmentation in the
levels of IFN alpha secretion. Our data show that ATRA is capable of
modulating the amounts and the state of activation of some of the
components of the IFN intracellular signaling pathways. They also suggest
that the retinoid can bypass IFN/IFN-receptor interactions and induce the
expression of IFN-regulated genes.
Volume 89,
Issue 3,
pp. 1001-1012,
02/01/1997
Copyright © 1997 by The American Society of Hematology
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