EGF Receptor in Tumor Growth and Progression

Keyword(s):  
Oncotarget ◽  
2014 ◽  
Vol 6 (7) ◽  
pp. 5164-5181 ◽  
Author(s):  
Parthasarathy Seshacharyulu ◽  
Moorthy P. Ponnusamy ◽  
Satyanarayana Rachagani ◽  
Imayavaramban Lakshmanan ◽  
Dhanya Haridas ◽  
...  

1992 ◽  
Vol 101 (6) ◽  
pp. 519-524 ◽  
Author(s):  
Sohtaro Komiyama ◽  
Shohji Kudoh ◽  
Katsuko Matsui ◽  
Hiromoto Mizoguchi ◽  
Hiroshi Miyazaki ◽  
...  

We have established three cell lines (IMC-2, IMC-3, and IMC-4) from a human maxillary tumor, which exhibited different sensitivities to epidermal growth factor (ECF). It was inhibitory to colony-forming abilities of IMC-3 and IMC-4 cells in culture, while it affected that of IMC-2 cells slightly if at all. The differential sensitivities to EGF among the three cell lines were reproducibly observed when several cell sublines were further established from tumors appearing in nude mice. Saturation-binding kinetics with 125I-EGF showed similar levels of EGF-binding activities among the three cell lines. However, IMC-2, IMC-3, and IMC-4 showed almost similar sensitivities to cisplatin. Autophosphorylation of EGF receptor in the presence of EGF proceeded at similar levels among the three cell lines. Tumor growth was followed in nude mice when IMC-2, IMC-3, and IMC-4 at 1 × 107 cells were inoculated. The IMC-2 tumors enlarged at much faster rates than the other two cell lines. The IMC-4 tumors showed very slow growth rates, and IMC-3 tumors enlarged at an intermediate rate. These data suggest that the maxillary tumor used comprised cell populations that differed in their growth behaviors in response to EGF.


2009 ◽  
Vol 390 (12) ◽  
Author(s):  
Peter Camaj ◽  
Hendrik Seeliger ◽  
Ivan Ischenko ◽  
Stefan Krebs ◽  
Helmut Blum ◽  
...  

Abstract The EGF-related protein EFEMP1 (EGF-containing fibulin-like extracellular matrix protein 1) has been shown to promote tumor growth in human adenocarcinoma. To understand the mechanism of this action, the signal transduction activated upon treatment with this protein has been investigated. We show that EFEMP1 binds EGF receptor (EGFR) in a competitive manner relative to epidermal growth factor (EGF), implicating that EFEMP1 and EGF share the same or adjacent binding sites on the EGFR. Treatment of pancreatic carcinoma cells with purified EFEMP1 activates autophosphorylation of EGFR at the positions Tyr-992 and Tyr-1068, but not at the position Tyr-1048. This signal is further transduced to phosphorylation of Akt at position Thr-308 and p44/p42 MAPK (mitogen-activated protein kinase) at positions Thr-202 and Tyr-204. These downstream phosphorylation events can be inhibited by treatment with the EGFR kinase inhibitor PD 153035. The observed signal transduction upon treatment with EFEMP1 can contribute to the enhancement of tumor growth shown in pancreatic carcinoma cells overexpressing EFEMP1.


2009 ◽  
Vol 137 (3) ◽  
pp. 914-923 ◽  
Author(s):  
Xinhua Chen ◽  
Johannes Fruehauf ◽  
Jeffrey D. Goldsmith ◽  
Hua Xu ◽  
Kianoosh K. Katchar ◽  
...  

2010 ◽  
Vol 28 (4) ◽  
pp. 731-741 ◽  
Author(s):  
David Schaffert ◽  
Melinda Kiss ◽  
Wolfgang Rödl ◽  
Alexei Shir ◽  
Alexander Levitzki ◽  
...  

2006 ◽  
Vol 238 (4) ◽  
pp. 771-779 ◽  
Author(s):  
Chaitanya A. Athale ◽  
Thomas S. Deisboeck

Nanomedicine ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. 475-491 ◽  
Author(s):  
B Leticia Rodriguez ◽  
Xinran Li ◽  
Kaoru Kiguchi ◽  
John DiGiovanni ◽  
Evan C Unger ◽  
...  

2005 ◽  
Vol 173 (4S) ◽  
pp. 178-179
Author(s):  
Tetsuo Ogushi ◽  
Takahashi Satoru ◽  
Takumi Takeuchi ◽  
Tetsuya Fujimura ◽  
Tomohiko Urano ◽  
...  

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