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-Casein Gene in Mammary Epithelial Cells Is Independent of p42 ERK2
Mitogen-activated Protein Kinase Activity
(Received for publication, July 1, 1996, and in revised form, August 20, 1996)
,
From the Friedrich Miescher Institute, P.O. Box 2543, CH-4002
Basel, Switzerland, the HC11 mammary epithelial cells have been used to
characterize molecular events involved in the regulation of milk
protein gene expression. Treatment of HC11 cells with the lactogenic
hormones prolactin, insulin, and glucocorticoids results in
transcription of the 
Institute for Experimental Cancer
Research, Tumor Biology Center, D-79106 Freiburg, Germany, and
" Laboratory of Biochemistry and Metabolism, NIDDK, National
Institutes of Health, Bethesda, Maryland 20892
-casein gene. Prolactin induces a signaling
event which involves tyrosine phosphorylation of the mammary gland
factor, Stat5, a member of the family of signal transducers and
activators of transcription (Stat). Here we show that HC11 cells
express two Stat5 proteins, Stat5a and Stat5b. Phosphopeptide and
phosphoamino acid analysis of Stat5a and Stat5b immunoprecipitated from
phosphate-labeled HC11 cells revealed that both proteins were
constitutively phosphorylated on serine. Lactogenic hormone treatment
resulted in the appearance of a tyrosine-phosphorylated peptide in both
Stat5 proteins. Consistent with this observation, a Western blot
analysis of Stat5a and Stat5b showed that lactogenic hormones induced a
rapid, transient increase in phosphotyrosine which paralleled the
binding of Stat5 to its cognate recognition sequence in the -casein
gene promoter. Lactogenic hormone treatment of the HC11 cells also led
to a rapid activation of the mitogen-activated protein (MAP) kinase
pathway. We examined the role of this pathway in -casein
transcription using a specific MAP kinase kinase inhibitor, PD98059.
Concentrations of PD98059 which completely abrogated lactogen-induced
MAP kinase activation did not affect the phosphorylation state of
Stat5, its DNA binding activity, or transcriptional activation of a
-casein reporter construct. This indicates that the MAP kinase
pathway does not contribute to lactogenic hormone induction of the
-casein gene.
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