Expression of transforming growth factor-β3 by embryonal carcinoma cells, parietal endoderm-like cells and early mouse embryos

1990 ◽  
Vol 26 (12) ◽  
pp. 1181-1185 ◽  
Author(s):  
Wendy J. Campbell ◽  
David Kelly ◽  
Angie Rizzino
Keyword(s):  
Growth Factor ◽  
Embryonal Carcinoma ◽  
Transforming Growth Factor ◽  
Mouse Embryos ◽  
Carcinoma Cells ◽  
Embryonal Carcinoma Cells ◽  
Parietal Endoderm ◽  
Early Mouse

Transforming growth factor-β and its receptor are differentially regulated in human embryonal carcinoma cells

1989 ◽  
Vol 41 (3) ◽  
pp. 245-253 ◽  
Author(s):  
Sjerp M. Weima ◽  
Marga A. van Rooijen ◽  
Alie Feijen ◽  
Christine L. Mummery ◽  
Everardus J.J. van Zoelen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Embryonal Carcinoma ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Carcinoma Cells ◽  
Embryonal Carcinoma Cells

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.

Interaction of several related GC-box- and GT-box-binding proteins with the intronic enhancer is required for differential expression of the gb110 gene in embryonal carcinoma cells

1994 ◽  
Vol 14 (9) ◽  
pp. 5786-5793
Author(s):  
L Hamann ◽  
K U Bayer ◽  
K Jensen ◽  
K Harbers
Keyword(s):  
Transcription Factor ◽  
Binding Proteins ◽  
Embryonal Carcinoma ◽  
Regulatory Elements ◽  
Carcinoma Cells ◽  
Minor Importance ◽  
Embryonal Carcinoma Cells ◽  
Enhancer Element ◽  
F9 Cells ◽  
Parietal Endoderm

The molecular mechanisms by which expression of a gene is down-regulated after differentiation of F9 embryonal carcinoma cells into parietal endoderm-like cells was studied by characterizing the cis- and trans-regulatory elements of the gb110 gene. This gene encodes a putative RNA helicase, and its expression is down-regulated when F9 cells are differentiated with retinoic acid and cyclic AMP. The 5'-flanking region of the gene has all of the features of a GC-rich island promoter and seems to play only a minor role, if any, in the regulated expression. A 133-bp enhancer in the first intron was identified by transient chloramphenicol acetyltransferase assays that activated expression in undifferentiated F9 cells about 50- to 100-fold. As this enhancer was not active in differentiated F9 cells, it seems to be the prime mediator of the differentiation-specific down-regulation of the gb110 gene. Four different protein-binding sites, three of which contain GC- and GT-box motifs, were identified in the enhancer element. The fourth site, interacting with previously described transcription factor FTZ-F1/ELP, seems to be of minor importance for the activity of the enhancer. Mutational analysis showed that the cooperative interaction of several most likely related proteins with the three GC- and GT-box motifs was required for full enhancer activity. On the basis of their binding properties, at least two of these proteins seem to be identical or closely related to ubiquitous transcription factor Sp1. One of the GT-box-binding proteins was present in undifferentiated F9 cells but not, however, in its differentiated derivatives. The cell specificity of this transcription factor explains why the gb110 gene is not expressed or expressed only at low levels in parietal endoderm-like cells.

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