Activation of fibroblast growth factor 8 gene expression in human embryonal carcinoma cells

1997 ◽  
Vol 62 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Jackson Wu ◽  
Robert A. Payson ◽  
Jas C. Lang ◽  
Ing-Ming Chiu
Keyword(s):  
Gene Expression ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Fibroblast Growth ◽  
Embryonal Carcinoma Cells ◽  
Fibroblast Growth Factor 8

Interaction between a novel F9-specific factor and octamer-binding proteins is required for cell-type-restricted activity of the fibroblast growth factor 4 enhancer

1994 ◽  
Vol 14 (12) ◽  
pp. 7758-7769
Author(s):  
L Dailey ◽  
H Yuan ◽  
C Basilico
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Binding Proteins ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Specific Factor ◽  
Fibroblast Growth ◽  
Embryonal Carcinoma Cells ◽  
Enhancer Function ◽  
Restricted Activity

Understanding how diverse transcription patterns are achieved through common factor binding elements is a fundamental question that underlies much of developmental and cellular biology. One example is provided by the fibroblast growth factor 4 (FGF-4) gene, whose expression is restricted to specific embryonic tissues during development and to undifferentiated embryonal carcinoma cells in tissue culture. Analysis of the cis- and trans-acting elements required for the activity of the previously identified FGF-4 enhancer in F9 embryonal carcinoma cells showed that enhancer function depends on sequences that bind Sp1 and ubiquitous as well as F9-specific octamer-binding proteins. However, sequences immediately upstream of the octamer motif, which conform to a binding site for the high-mobility group (HMG) domain factor family, were also critical to enhancer function. We have identified a novel F9-specific factor, Fx, which specifically recognizes this motif. Fx formed complexes with either Oct-1 or Oct-3 in a template-dependent manner. The ability of different enhancer variants to form the Oct-Fx complexes correlated with enhancer activity, indicating that these complexes play an essential role in transcriptional activation of the FGF-4 gene. Thus, while FGF-4 enhancer function is octamer site dependent, its developmentally restricted activity is determined by the interaction of octamer-binding proteins with the tissue-specific factor Fx.

scholarly journals The expression and localization of urokinase-type plasminogen activator and its type 1 inhibitor are regulated by retinoic acid and fibroblast growth factor in human teratocarcinoma cells.

1991 ◽  
Vol 2 (4) ◽  
pp. 285-297 ◽  
Author(s):  
J Tienari ◽  
T Alanko ◽  
E Lehtonen ◽  
O Saksela
Keyword(s):  
Retinoic Acid ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Fibroblast Growth ◽  
Embryonal Carcinoma Cells ◽  
Undifferentiated Cells ◽  
Pai 1

Human Tera 2 embryonal carcinoma cells switch gradually from rapidly growing undifferentiated cells to almost nonproliferating cells during retinoic acid (RA)-induced neuronal differentiation. This process is associated with the increased expression of type 1 plasminogen activator inhibitor (PAI 1) mRNA, and the secreted inhibitor is immobilized to the pericellular area. Furthermore, the differentiation is accompanied by a decrease in the amount of both the secreted tissue-type PA (tPA) and the mainly cell-associated urokinase-type PA (uPA) activity. In RA-differentiated cells, uPA becomes localized at the vinculin-rich cell-substratum adhesion sites. Fibroblast growth factor activity has been associated with various events during embryonal growth and with the regulation of proteolytic enzymes. A short-term treatment of the undifferentiated Tera 2 cells with basic fibroblast growth factor (bFGF) increases uPA mRNA levels and the cell-associated uPA activity, whereas the secretory tPA activity decreases. bFGF induces PAI 1 mRNA expression in the undifferentiated cells, but unlike PAI 1 protein after RA-treatment, the inhibitor does not accumulate around the cells but is released in the medium. A similar exposure to bFGF has less effect on the RA-differentiated Tera 2 cells. Under these conditions bFGF treatment leads to an increase in the amounts of PAI 1 and uPA mRNAs, but no changes in the localization of these components can be seen. Differentiation of human embryonal carcinoma cells is thus connected with an altered response to bFGF.

scholarly journals Interaction between a novel F9-specific factor and octamer-binding proteins is required for cell-type-restricted activity of the fibroblast growth factor 4 enhancer.

1994 ◽  
Vol 14 (12) ◽  
pp. 7758-7769 ◽  
Author(s):  
L Dailey ◽  
H Yuan ◽  
C Basilico
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Binding Proteins ◽  
Embryonal Carcinoma ◽  
Carcinoma Cells ◽  
Specific Factor ◽  
Fibroblast Growth ◽  
Embryonal Carcinoma Cells ◽  
Enhancer Function ◽  
Restricted Activity

Understanding how diverse transcription patterns are achieved through common factor binding elements is a fundamental question that underlies much of developmental and cellular biology. One example is provided by the fibroblast growth factor 4 (FGF-4) gene, whose expression is restricted to specific embryonic tissues during development and to undifferentiated embryonal carcinoma cells in tissue culture. Analysis of the cis- and trans-acting elements required for the activity of the previously identified FGF-4 enhancer in F9 embryonal carcinoma cells showed that enhancer function depends on sequences that bind Sp1 and ubiquitous as well as F9-specific octamer-binding proteins. However, sequences immediately upstream of the octamer motif, which conform to a binding site for the high-mobility group (HMG) domain factor family, were also critical to enhancer function. We have identified a novel F9-specific factor, Fx, which specifically recognizes this motif. Fx formed complexes with either Oct-1 or Oct-3 in a template-dependent manner. The ability of different enhancer variants to form the Oct-Fx complexes correlated with enhancer activity, indicating that these complexes play an essential role in transcriptional activation of the FGF-4 gene. Thus, while FGF-4 enhancer function is octamer site dependent, its developmentally restricted activity is determined by the interaction of octamer-binding proteins with the tissue-specific factor Fx.

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