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(Received for publication, January 9, 1997, and in revised form, May 21, 1997)
From the Georgetown University Medical Center, Department of
Pharmacology and the Lombardi Cancer Center,
Washington, D.C. 20007
Transcription factor Sp1 is a phosphoprotein
whose level and DNA binding activity are markedly increased in
doxorubicin-resistant HL-60 (HL-60/AR) leukemia cells. The
trans-activating and DNA binding properties of Sp1 in
HL-60/AR cells are stimulated by cAMP-dependent protein
kinase (PKA) and PKA agonists and inhibited by PKA antagonists as well
as by the PKA regulatory subunit. Reporter gene activity under the
control of the Sp1-dependent SV40 promoter is stimulated in
insect cells transiently expressing Sp1 and PKA, and the DNA binding
activity of recombinant Sp1 is activated by exogenous PKA in
vitro. These results indicate that Sp1 is a cAMP-responsive transcription factor and that Sp1-dependent genes may be
modulated through a cAMP-dependent signaling pathway.
Volume 272, Number 34,
Issue of August 22, 1997
pp. 21137-21141
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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