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(Received for publication, January 16, 1997, and in revised form, April 21, 1997)
From the Department of Molecular Pathology, University of Texas
M. D. Anderson Cancer Center, Houston, Texas 77030
The expression of P-glycoproteins encoded by the
mdr gene family is associated with the emergence of
multidrug resistance phenotype in animal cells. However, the mechanisms
controlling the expression of these genes have not been well
elucidated. Here, we report that the expression of rat
mdr1b gene in cultured H-4-II-E hepatoma cells can be
induced by insulin. Transient transfection assays using reporter gene
constructs containing various 5
Volume 272, Number 24,
Issue of June 13, 1997
pp. 15174-15183
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
B-mediated Induction of mdr1b Expression by
Insulin in Rat Hepatoma Cells
mdr1b sequences showed
that the sequence located between base pairs 
243 and 163 is
important for insulin's induction of mdr1b promoter activity. Further analyses revealed that a NF-
B-binding site (located between base pairs 167 and 158) is required for
insulin-induced promoter activity. Gel mobility shift assay
demonstrated that insulin stimulates the binding of nuclear p50/p65
subunits to the mdr1b NF-B sequence. Cotransfection of
plasmids expressing either the p50/p65 NF-B subunits or Raf-1 kinase
or both resulted in increased expression of the gene containing
wild-type but not NF-B site-mutated mdr1b promoter.
Finally, expression of either the antisense p65 subunit of NF-B or
dominant negative Raf-1 kinase blocked insulin's induction of the
mdr1b promoter activity. Taken together, our results
suggest that the insulin-induced mdr1b expression is
mediated by transcription factor NF-B via the Raf-1 kinase signaling
pathway.
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