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(Received for publication, July 31, 1996, and in revised form, October 8, 1996)
From the Department of Molecular Genetics, Kumamoto University
School of Medicine, Kuhonji, Kumamoto 862, Japan
The gene for liver-type arginase, an ornithine
cycle enzyme, is induced by glucocorticoids in a delayed secondary
manner. An enhancer element located around intron 7 of the rat arginase gene shows delayed glucocorticoid responsiveness, and it harbors two
sites binding with members of the CCAAT/enhancer binding protein (C/EBP) family. Here, we investigate the role of these C/EBP binding sites in glucocorticoid response of the arginase gene. When inserted in
front of the herpes simplex virus thymidine kinase promoter, these
C/EBP sites exhibited glucocorticoid responsiveness in reporter transfection assay using rat hepatoma H4IIE cells. In footprint analysis using nuclear extracts of H4IIE cells, profiles of the protected areas of the two C/EBP sites changed when cells were treated
with dexamethasone. In gel shift analysis, the complex formation for
the two C/EBP sites was augmented in response to dexamethasone.
Antibody supershift/inhibition analysis demonstrated that a major
portion of the binding proteins induced by dexamethasone is C/EBP
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3694-3698
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
ACTIVATION OF THE RAT ARGINASE GENE THROUGH INDUCTION OF
C/EBP
.
Induction of arginase mRNA by dexamethasone was preceded by
augmentation of the C/EBP site-binding activities, which followed increase in C/EBP mRNA. These results were consistent with the notion that the glucocorticoid response of the arginase gene is mediated by C/EBP.
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