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(Received for publication, February 20, 1996, and in revised form, April 25, 1996)
From the Department of Microbiology and Molecular Genetics,
Division of Clinical Oncology, and Division of Cellular and Molecular
Biology, Harvard Medical School and the Dana-Farber Cancer Institute,
Boston, Massachusetts 02115
A broad panel of agents including serum,
interleukin-1, double-stranded RNA, and platelet-derived growth factor
(PDGF) stimulate transcription of the ``slow'' immediate-early gene
MCP-1. These disparate inducers act through a tight cluster
of regulatory elements in the distal 5
Volume 271, Number 29,
Issue of July 19, 1996
pp. 17417-17424
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
B and a 90-kDa
Phosphoprotein Coactivator
-flanking sequences of the
MCP-1 gene. We describe a 22-base element in this cluster
which, in single copy, confers PDGF-inducibility to a tagged
MCP-1 reporter gene. In mobility shift assays, the element
binds a PDGF-activated form of NF-
B, and a 90-kDa protein (p90)
which binds constitutively. Antibody supershift and UV cross-linking
experiments indicate that the PDGF-activated NF-B species is a Rel A
homodimer. The DNA binding form of p90 is a nuclear-restricted
serine/threonine phosphoprotein. Mutagenesis of the 22-base element
shows that the NF-B and p90 binding sites overlap, but binding of
the two species is mutually independent. Both sites, however, are
required for optimum PDGF induction of MCP-1. Therefore,
p90 appears to be a coactivator with NF-B in PDGF-mediated induction
of MCP-1.
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