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J Biol Chem, Vol. 275, Issue 7, 5037-5042, February 18, 2000
From the Department of Pharmacological and Physiological Science,
St. Louis University School of Medicine,
St. Louis, Missouri 63104
Previously we showed that the activator protein-1
site and the runt domain binding site in the collagenase-3
promoter act cooperatively in response to parathyroid hormone (PTH) in
the rat osteoblastic osteosarcoma cell line, UMR 106-01. Our results of
the expression pattern of core binding factor
Parathyroid Hormone Regulation of the Rat Collagenase-3
Promoter by Protein Kinase A-dependent Transactivation
of Core Binding Factor
1*
1 (Cbfa1), which binds
to the runt domain site, indicated that there is no change in the levels of Cbfa1 protein or RNA under either control conditions or after PTH treatment. The importance of posttranslational
modification of Cbfa1 in the signaling pathway for PTH-induced
collagenase-3 promoter activity was analyzed. PTH stimulation of
collagenase-3 promoter activity was completely abrogated by protein
kinase A (PKA) inhibition. To determine the role of PKA activity with
respect to Cbfa1 activation (in addition to its known activity of
phosphorylating cAMP-response element-binding protein to enhance
c-fos promoter activity), we utilized the heterologous Gal4
transcription system. PTH stimulated the transactivation of activation
domain-3 in Cbfa1 through the PKA site. In vitro
phosphorylation studies indicated that the PKA site in the wild type
activation domain-3 is a substrate for phosphorylation by PKA. Thus, we
demonstrate that PTH induces a PKA-dependent
transactivation of Cbfa1, and this transactivation is required for
collagenase-3 promoter activity in UMR cells.
*
This work was supported by National Institutes of Health
Grants DK47420 and DK48109 (to N. C. P) and a National Osteoporosis Foundation grant (to N. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Pharmacological and Physiological Science, St. Louis University School of Medicine, 1402 South Grand Blvd., St. Louis, MO 63104. Tel.: 314-577-8551; Fax: 314-577-8233; E mail: Partrinc{at}slu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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