scholarly journals cDNA cloning of a mouse mammary epithelial cell surface protein reveals the existence of epidermal growth factor-like domains linked to factor VIII-like sequences.

1990 ◽  
Vol 87 (21) ◽  
pp. 8417-8421 ◽  
Author(s):  
J. D. Stubbs ◽  
C. Lekutis ◽  
K. L. Singer ◽  
A. Bui ◽  
D. Yuzuki ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cell ◽  
Epidermal Growth Factor ◽  
Mammary Epithelial Cell ◽  
Surface Protein ◽  
Mammary Epithelial ◽  
Cell Surface Protein ◽  
Mouse Mammary Epithelial Cell ◽  
Epithelial Cell Surface ◽  
Epidermal Growth

scholarly journals Tyrosine Phosphorylation of Grb2: Role in Prolactin/Epidermal Growth Factor Cross Talk in Mammary Epithelial Cell Growth and Differentiation

2009 ◽  
Vol 29 (10) ◽  
pp. 2505-2520 ◽  
Author(s):  
Eric Haines ◽  
Parham Minoo ◽  
Zhenqian Feng ◽  
Nazila Resalatpanah ◽  
Xin-Min Nie ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Growth Factor ◽  
Cell Growth ◽  
Epithelial Cell ◽  
Epidermal Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial ◽  
Cell Growth And Differentiation ◽  
Epidermal Growth

ABSTRACT Characterizing mechanisms regulating mammary cell growth and differentiation is vital, as they may contribute to breast carcinogenesis. Here, we examine a cross talk mechanism(s) downstream of prolactin (PRL), a primary differentiation hormone, and epidermal growth factor (EGF), an important proliferative factor, in mammary epithelial cell growth and differentiation. Our data indicate that EGF exerts inhibitory effects on PRL-induced cellular differentiation by interfering with Stat5a-mediated gene expression independent of the PRL-proximal signaling cascade. Additionally, our data show that PRL is a potent inhibitor of EGF-induced cell proliferation. We identify tyrosine phosphorylation of the growth factor receptor-bound protein 2 (Grb2) as a critical mechanism by which PRL antagonizes EGF-induced cell proliferation by attenuating the activation of the Ras/mitogen-activated protein kinase (MAPK) pathway. Together, our results define a novel negative cross-regulation between PRL and EGF involving the Jak2/Stat5a and Ras/MAPK pathways through tyrosine phosphorylation of Grb2.

Transient effect of epidermal growth factor on the motility of an immortalized mammary epithelial cell line

1993 ◽  
Vol 106 (3) ◽  
pp. 869-878 ◽  
Author(s):  
M.A. Matthay ◽  
J.P. Thiery ◽  
F. Lafont ◽  
F. Stampfer ◽  
B. Boyer
Keyword(s):  
Growth Factor ◽  
Epithelial Cell ◽  
Cell Motility ◽  
Cell Line ◽  
Mammary Epithelial Cell ◽  
Wound Closure ◽  
Mammary Epithelial ◽  
Epithelial Cell Line ◽  
Mammary Epithelial Cell Line ◽  
Epidermal Growth

The effects of growth factors on epithelial cell motility and dispersion have been examined on an immortalized human mammary epithelial cell line, the 184A1 nontumorigenic cell line. Among all the molecules tested, epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha) were demonstrated to stimulate an increase in mammary epithelial cell motility and wound closure that was associated with a morphological transformation of the cells and was accompanied by modifications in cell-cell and cell-substrate adhesion systems. The EGF-induced increase in cell motility and monolayer wound closure occurred over a 24 hour period and was not dependent on an increase in cell number. The effect of EGF was abolished by inhibiting alpha 2 integrins with specific antibodies, indicating that part of the mechanism for the increase in cell motility and accelerated wound closure depends on alpha 2 integrin functional expression. After 72 hours of exposure to EGF, the EGF-induced alterations in cell morphology, motility and cell adhesion systems underwent a spontaneous reversion that was correlated with a 10-fold reduction in the number of EGF receptors. The ability to regulate the scattering response induced by growth factors might be an important feature distinguishing normal epithelial cells from their tumoral counterparts.

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