Epidermal growth factor (EGF) receptor localization in cultured human granulosa lutein cells and the stimulation of progesterone production by EGF and transforming growth factor-α (TGF-α)

1995 ◽  
Vol 12 (10) ◽  
pp. 720-727 ◽  
Author(s):  
Francis R. Tekpetey ◽  
Susan A. J. Daniel ◽  
Albert Yuzpe
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Egf Receptor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Α ◽  
Progesterone Production ◽  
Receptor Localization ◽  
Epidermal Growth ◽  
Factor Α ◽  
Stimulation Of

Epidermal growth factor regulation of glutathione S-transferase gene expression in the rat is mediated by class Pi glutathione S-transferase enhancer I

2000 ◽  
Vol 349 (1) ◽  
pp. 225-230 ◽  
Author(s):  
Michi MATSUMOTO ◽  
Masayoshi IMAGAWA ◽  
Yasunobu AOKI
Keyword(s):  
Gene Expression ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Transforming Growth Factor ◽  
Signal Transduction Pathway ◽  
Glutathione S Transferase ◽  
Transforming Growth Factor Α ◽  
Epidermal Growth ◽  
Factor Α ◽  
Stimulation Of

Using chloramphenicol acetyltransferase assays we showed that epidermal growth factor (EGF), transforming growth factor α (TGFα), and 3,3ʹ,4,4ʹ,5-pentachlorobiphenyl (PenCB) induce class Pi glutathione S-transferase (GSTP1) in primary cultured rat liver parenchymal cells. GSTP1 enhancer I (GPEI), which is required for the stimulation of GSTP1 expression by PenCB, also mediates EGF and TGFα stimulation of GSTP1 gene expression. However, hepatocyte growth factor and insulin did not stimulate GPEI-mediated gene expression. On the other hand, the antioxidant reagents butylhydroxyanisole and t-butylhydroquinone, stimulated GPEI-mediated gene expression, but the level of GSTP1 mRNA was not elevated. Our observations suggest that EGF and TGFα induce GSTP1 by the same signal transduction pathway as PenCB. Since the sequence of GPEI is similar to that of the antioxidant responsive element (ARE), some factors which bind to ARE might play a role in GPEI-mediated gene expression.

scholarly journals The linear C-terminal regions of epidermal growth factor (EGF) and transforming growth factor-α bind to different epitopes on the human EGF receptor

1998 ◽  
Vol 336 (1) ◽  
pp. 147-151 ◽  
Author(s):  
Anne E. G. LENFERINK ◽  
Albert D. G. De ROOS ◽  
Marianne J. H. Van VUGT ◽  
Monique L. M. Van De POLL ◽  
Everardus J. J. Van ZOELEN
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Release ◽  
Egf Receptor ◽  
Transforming Growth Factor ◽  
Binding Characteristics ◽  
Transforming Growth Factor Α ◽  
Identical Manner ◽  
Epidermal Growth ◽  
Factor Α

Epidermal growth factor (EGF) and transforming growth factor-α (TGFα) bind with similar affinities in a competitive fashion to the human EGF receptor, and basically induce similar mitogenic responses. In spite of the fact that EGF and TGFα are structurally alike, it is still not clear if the two growth factors bind the receptor in an identical manner. The observation that the 13A9 antibody blocks binding of TGFα, but not that of EGF, to the human EGF receptor [Winkler, O'Connor, Winget and Fendly (1989) Biochemistry 28, 6373–6378] suggests that their binding characteristics are not identical. In the present study we have made use of a set of EGF/TGFα chimaeric molecules to show that the 13A9 antibody blocks receptor binding of ligands with TGFα sequences, but not of ligands with EGF sequences, in their C-terminal linear regions. Using HaCaT human keratinocyte cells in culture, it was determined that ligands that are able to bind the EGF receptor in the presence of 13A9 are also able to induce calcium release from intracellular stores in these cells, indicating that these ligands have the ability to activate the EGF receptor in the presence of the antibody. From these data it is concluded that the flexible C-terminal linear domains of EGF and TGFα bind to separate sequences on the EGF receptor, such that the binding domain of TGFα, but not that of EGF, overlaps with the binding epitope of the 13A9 antibody.

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