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Updated: Sep 2, 2026

Induction and Analysis of Epithelial to Mesenchymal Transition
Published on: August 27, 2013
Human transforming growth factors induce tyrosine phosphorylation of EGF receptors
Abstract:
Cultured cell lines of human tumour origin as well as cells transformed by various RNA tumour viruses secrete low molecular weight polypeptide transforming growth factors (TGFs). In addition to competing with epidermal growth factor (EGF) for binding to its cellular receptor, TGFs can transform morphologically fibroblast and epithelial cells in culture. In view of accumulating evidence that tyrosine phosphorylation activity is associated with the transforming genes of various tumour viruses, we determined whether phosphotyrosine levels were elevated in these human tumour cells. We show here that TGFs produced by human tumour cells induce phosphorylation of specific tyrosine acceptor sites in the 160,000-molecular weight (160 K) EGF receptor.
Insights
Human tumor cells secrete transforming growth factors (TGFs) that can alter cell behavior. These TGFs were found to increase phosphotyrosine levels in the epidermal growth factor (EGF) receptor.
Area of Science:
- Oncology
- Cell Biology
- Molecular Biology
Background:
- Cultured human tumor cell lines and RNA tumor virus-transformed cells secrete transforming growth factors (TGFs).
- TGFs compete with epidermal growth factor (EGF) for receptor binding and can induce cell transformation in vitro.
- Tyrosine phosphorylation activity is linked to transforming genes of tumor viruses.
Purpose of the Study:
- To investigate whether phosphotyrosine levels are elevated in human tumor cells.
- To determine the effect of TGFs produced by human tumor cells on the EGF receptor.
Main Methods:
- Culturing human tumor cell lines.
- Analyzing phosphotyrosine levels in tumor cells.
- Assessing the impact of TGFs on the EGF receptor's tyrosine phosphorylation sites.
Main Results:
- Human tumor cells secrete TGFs.
- TGFs produced by these cells induce phosphorylation at specific tyrosine sites on the 160,000-molecular weight (160 K) EGF receptor.
Conclusions:
- TGFs from human tumor cells activate tyrosine phosphorylation of the EGF receptor.
- This finding links TGF secretion by tumor cells to alterations in EGF receptor signaling pathways.
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