The nuclear localization of WAP and CSN genes is modified by lactogenic hormones in HC11 cells

2008 ◽  
Vol 105 (1) ◽  
pp. 262-270 ◽  
Author(s):  
Maria Ballester ◽  
Clémence Kress ◽  
Cathy Hue-Beauvais ◽  
Kiên Kiêu ◽  
Gaëtan Lehmann ◽  
...  
Keyword(s):  
Nuclear Localization ◽  
Lactogenic Hormones ◽  
Hc11 Cells

scholarly journals The Intracellular Domain of ErbB4 Induces Differentiation of Mammary Epithelial Cells

2006 ◽  
Vol 17 (9) ◽  
pp. 4118-4129 ◽  
Author(s):  
Rebecca S. Muraoka-Cook ◽  
Melissa Sandahl ◽  
Carty Husted ◽  
Debra Hunter ◽  
Leah Miraglia ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Nuclear Localization ◽  
Transmembrane Domain ◽  
Mammary Epithelial Cells ◽  
Three Dimensional ◽  
Mammary Epithelial ◽  
Differentiation Markers ◽  
Intracellular Domain ◽  
Lumen Formation ◽  
Hc11 Cells

Differentiation of mammary epithelium in vivo requires signaling through prolactin- and ErbB4/HER4-dependent mechanisms; how these pathways intersect is unknown. We show herein that HC11 mouse mammary cells undergo ErbB4-dependent lactational differentiation. Prolactin and the ErbB4 ligand HB-EGF each induced STAT5A activation, expression of lactogenic differentiation markers, and lumen formation in three-dimensional Matrigel cultures in HC11 cells. ErbB4 undergoes ligand-dependent transmembrane domain cleavage at Val-675, releasing a soluble 80-kDa intracellular domain (s80HER4) that localizes to nuclei; the physiological relevance of s80HER4 is unknown. A HER4V675A mutant abolishing transmembrane cleavage impaired STAT5A activity, lactogenic gene expression, and lumen formation. Kinase-dead HER4KD was neither cleaved nor able to induce differentiation of HC11 cells. Without treating HC11 cells with prolactin or HB-EGF, s80HER4 (expressed from a cDNA construct) localized to the nucleus, activated STAT5A, and induced three-dimensional lumen formation. Nuclear localization of exogenous s80HER4 required intact kinase activity of s80HER4, as did activation of STAT5A. In contrast, nuclear localization of s80HER4 and STAT5A activation did not require the 16-amino acid region of the ErbB4 intracellular domain specific to the Cyt-1 isoform of ErbB4, and absent in the Cyt-2 isoform. These results suggest that s80HER4 formation contributes to ErbB4-dependent differentiation of mammary epithelial cells.

Epidermal growth factor receptor, but not c-erbB-2, activation prevents lactogenic hormone induction of the beta-casein gene in mouse mammary epithelial cells

1990 ◽  
Vol 10 (8) ◽  
pp. 4027-4034
Author(s):  
N E Hynes ◽  
D Taverna ◽  
I M Harwerth ◽  
F Ciardiello ◽  
D S Salomon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Transforming Growth Factor ◽  
Mammary Epithelial ◽  
Transforming Growth Factor Alpha ◽  
Beta Casein ◽  
Epidermal Growth ◽  
Factor Alpha ◽  
Lactogenic Hormones ◽  
Hc11 Cells

The HC11 cell line was isolated from mammary gland cells of pregnant mice. The cells displayed a normal phenotype and retained some characteristics of mammary epithelial cell differentiation. After treatment with the lactogenic hormones prolactin and glucocorticoids, the HC11 cells expressed the milk protein beta-casein. Various oncogenes were transfected and expressed in HC11 cells. The oncogenes were tested for their transformation ability and for their effects upon the differentiation of the HC11 cells. All of the oncogenes tested, including activated human Ha-ras, human transforming growth factor-alpha, activated rat neuT, and human c-erbB-2 activated by a point mutation in the transmembrane domain, caused transformation of the HC11 cells, as shown by tumor formation in nude mice. HC11 cells expressing the neuT and activated c-erbB-2 genes synthesized beta-casein in response to lactogenic hormones, whereas those expressing the Ha-ras or transforming growth factor-alpha oncogenes were no longer able to respond to the lactogenic hormones. This inhibition of beta-casein production occurs at the transcriptional level and in the transforming growth factor-alpha-transformed cells is due to an autocrine mechanism involving the activation of the epidermal growth factor receptor. This suggests that, although the c-erbB-2 and epidermal growth factor receptors are structurally quite similar, their activation has different effects upon mammary epithelial cell differentiation.

scholarly journals Epidermal growth factor receptor, but not c-erbB-2, activation prevents lactogenic hormone induction of the beta-casein gene in mouse mammary epithelial cells.

1990 ◽  
Vol 10 (8) ◽  
pp. 4027-4034 ◽  
Author(s):  
N E Hynes ◽  
D Taverna ◽  
I M Harwerth ◽  
F Ciardiello ◽  
D S Salomon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Transforming Growth Factor ◽  
Mammary Epithelial ◽  
Transforming Growth Factor Alpha ◽  
Beta Casein ◽  
Epidermal Growth ◽  
Factor Alpha ◽  
Lactogenic Hormones ◽  
Hc11 Cells

The HC11 cell line was isolated from mammary gland cells of pregnant mice. The cells displayed a normal phenotype and retained some characteristics of mammary epithelial cell differentiation. After treatment with the lactogenic hormones prolactin and glucocorticoids, the HC11 cells expressed the milk protein beta-casein. Various oncogenes were transfected and expressed in HC11 cells. The oncogenes were tested for their transformation ability and for their effects upon the differentiation of the HC11 cells. All of the oncogenes tested, including activated human Ha-ras, human transforming growth factor-alpha, activated rat neuT, and human c-erbB-2 activated by a point mutation in the transmembrane domain, caused transformation of the HC11 cells, as shown by tumor formation in nude mice. HC11 cells expressing the neuT and activated c-erbB-2 genes synthesized beta-casein in response to lactogenic hormones, whereas those expressing the Ha-ras or transforming growth factor-alpha oncogenes were no longer able to respond to the lactogenic hormones. This inhibition of beta-casein production occurs at the transcriptional level and in the transforming growth factor-alpha-transformed cells is due to an autocrine mechanism involving the activation of the epidermal growth factor receptor. This suggests that, although the c-erbB-2 and epidermal growth factor receptors are structurally quite similar, their activation has different effects upon mammary epithelial cell differentiation.

Laminin and tenascin assembly and expression regulate HC11 mouse mammary cell differentiation

1994 ◽  
Vol 107 (4) ◽  
pp. 1031-1040 ◽  
Author(s):  
R. Chammas ◽  
D. Taverna ◽  
N. Cella ◽  
C. Santos ◽  
N.E. Hynes
Keyword(s):  
Extracellular Matrix ◽  
Growth Conditions ◽  
Mammary Epithelial ◽  
Epithelial Cell Line ◽  
Competent Cells ◽  
Extracellular Matrix Components ◽  
Beta Casein ◽  
Lactogenic Hormones ◽  
Differentiation Marker ◽  
Hc11 Cells

HC11 is a normal mouse mammary epithelial cell line that requires certain growth factors, such as EGF or bFGF, to respond optimally to lactogenic hormones and produce the differentiation marker beta-casein. Growth in insulin (Ins) or PDGF does not produce cells competent to respond to lactogenic hormones. Here we show that competency for differentiation is due at least in part to the modulation of extracellular matrix components. In particular we have studied laminin and tenascin. EGF alters endogenous laminin assembly. In addition, promotion of competency can be partially mimicked by plating HC11 cells on the E8 laminin fragment, which is able to induce lactogenic responsiveness in cells grown in the absence of EGF or bFGF. The production and assembly of tenascin is also dependent upon the growth conditions of the HC11 cells. EGF- or bFGF-grown competent cells produce tenascin but do not assemble it at the extracellular matrix as efficiently as Ins- or PDGF-grown, non-competent cells. This alteration apparently leads to a change in the cellular microenvironment that supports beta-casein production. In addition, when competent cells are plated on dishes coated with tenascin, lactogenic hormone induction of beta-casein is inhibited. The data suggest that tenascin assembly and beta-casein production are opposing features of a coordinated differentiation program of HC11 cells.

386: Nuclear Localization of ERBB3: A Potential Diagnostic/Prognostic Marker of Prostate Cancer

2005 ◽  
Vol 173 (4S) ◽  
pp. 105-106
Author(s):  
Ismaël H. Koumakpayi ◽  
Jean-Simon Diallo ◽  
Cecile Le Page ◽  
Laurent Lessard ◽  
Martin E. Gleave ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Prognostic Marker ◽  
Nuclear Localization
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