scholarly journals Regulation of human type II phosphatidylinositol kinase activity by epidermal growth factor-dependent phosphorylation and receptor association.

1994 ◽  
Vol 269 (49) ◽  
pp. 31243-31251
Author(s):  
A Kauffmann-Zeh ◽  
R Klinger ◽  
G Endemann ◽  
M D Waterfield ◽  
R Wetzker ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Kinase Activity ◽  
Type Ii ◽  
Human Type ◽  
Phosphatidylinositol Kinase ◽  
Epidermal Growth

scholarly journals Activation of Thyroid Hormone Is Transcriptionally Regulated by Epidermal Growth Factor in Human Placenta-Derived JEG3 Cells

Endocrinology ◽  
2007 ◽  
Vol 149 (2) ◽  
pp. 695-702 ◽  
Author(s):  
Gianluca Canettieri ◽  
Antonella Franchi ◽  
Michele Della Guardia ◽  
Ianessa Morantte ◽  
Maria Giulia Santaguida ◽  
...  
Keyword(s):  
Growth Factor ◽  
Thyroid Hormone ◽  
Epidermal Growth Factor ◽  
Enzymatic Activity ◽  
Early Stage ◽  
First Trimester ◽  
Mrna Levels ◽  
Type Ii ◽  
Human Type ◽  
Epidermal Growth

Human type II deiodinase is a master regulator of thyroid hormone activation in several tissues. In placenta, type II deiodinase mRNA levels and enzymatic activity are elevated only during the first trimester of pregnancy and then progressively decline. During this early stage, mitogens such as epidermal growth factor (EGF) have been shown to promote the proliferation of the trophoblast by acting through multiple mechanisms. Here we show that EGF modulates transcription of human type II deiodinase gene (Dio2) through distinct signaling pathways, leading to the assembly of a heterogeneous transcription factor complex. Gene expression and deiodination assays have shown that EGF promptly induces a short-lived Dio2 mRNA and enzymatic activity. The induction is mediated by ERK and p38 kinases, as demonstrated by selective inhibition or overexpression of different mitogen-activated kinases. Reporter assays of mutant constructs indicate that EGF-induced transcriptional activity on Dio2 promoter is mediated by the cAMP response element (CRE) and does not involve the activating protein 1 site. With functional and biochemical approaches, we have demonstrated that the EGF stimulation culminates with the assembly and recruitment over the Dio2 CRE of a composite complex, which consists of c-Jun, c-Fos, and CRE-binding protein. These results further support the hypothesis that placental iodothyronine metabolism is critical during early pregnancy.

scholarly journals Epidermal growth factor (EGF) stimulates association and kinase activity of Raf-1 with the EGF receptor.

1991 ◽  
Vol 11 (2) ◽  
pp. 913-919 ◽  
Author(s):  
H App ◽  
R Hazan ◽  
A Zilberstein ◽  
A Ullrich ◽  
J Schlessinger ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Kinase Activity ◽  
Egf Receptor ◽  
Sodium Dodecyl ◽  
Specific Protein ◽  
Kinase Assay ◽  
Downstream Effector ◽  
Epidermal Growth

Raf-1 serine- and threonine-specific protein kinase is transiently activated in cells expressing the epidermal growth factor (EGF) receptor upon treatment with EGF. The stimulated EGF receptor coimmunoprecipitates with Raf-1 kinase and mediates protein kinase C-independent phosphorylation of Raf-1 on serine residues. Hyperphosphorylated Raf-1 has lower mobility on sodium dodecyl sulfate gels and has sixfold-increased activity in immunocomplex kinase assay with histone H1 or Raf-1 sequence-derived peptide as a substrate. Raf-1 activation requires kinase-active EGF receptor; a point mutant lacking tyrosine kinase activity in inactive in Raf-1 coupling and association. It is noteworthy that tyrosine phosphorylation of c-Raf-1 induced by EGF was not detected in these cells. These observations suggest that Raf-1 kinase may act as an important downstream effector of EGF signal transduction.

Measurement of downstream kinase activity modulation as indicator of epidermal growth factor receptor inhibitor efficacy

2014 ◽  
Vol 448 ◽  
pp. 65-67 ◽  
Author(s):  
W. Matthew Dickerson ◽  
Ashley Saab ◽  
Kristen Leong ◽  
Michael Miller ◽  
Martin Latterich ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Kinase Activity ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Receptor Inhibitor

Aging: altered responsiveness of gastric mucosa to epidermal growth factor

1989 ◽  
Vol 257 (4) ◽  
pp. G554-G560 ◽  
Author(s):  
A. P. Majumdar ◽  
F. L. Arlow
Keyword(s):  
Growth Factor ◽  
Gastric Mucosa ◽  
Epidermal Growth Factor ◽  
Dna Synthesis ◽  
Thymidine Kinase ◽  
Membrane Fraction ◽  
Kinase Activity ◽  
Thymidine Kinase Activity ◽  
Epidermal Growth ◽  
K Activity

The present investigation examines the responsiveness of the gastric mucosa to the growth-promoting action of epidermal growth factor (EGF) during advancing age. Two sets of experiments were performed. In the first set of experiments, groups of 4-, 8-, 16-, and 24-mo-old Fischer 344 rats were injected subcutaneously at 12-h intervals for 2 days with either EGF (10 micrograms/kg) in gelatin or the vehicle only (controls). The animals were killed 16-18 h after the last injection. The oxyntic gland mucosa was assayed for thymidine kinase and the rate of DNA synthesis in vitro (indicators of proliferative activity) as well as for tyrosine kinase (Tyr-k) activity. In control rats, the rate of DNA synthesis and thymidine kinase activity rose steadily between 4 and 24 mo of age. However, whereas Tyr-k activity in the gastric mucosal cytosol changed only marginally with age, activity of the enzyme in the membrane fraction rose steadily between 4 and 16 mo and then increased abruptly. EGF stimulated gastric mucosal DNA synthesis and thymidine kinase activity in 4- to 16-mo-old rats compared with the corresponding controls, but in the 24-mo-old animals, it caused a significant 40-50% inhibition. EGF had no demonstrable effect on Tyr-k activity in either cytosolic or membrane fraction. We postulated that Tyr-k activity might have returned to basal level 16-18 h after the last EGF injection.(ABSTRACT TRUNCATED AT 250 WORDS)

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