Growth Factors and Malignant Transformation

  • Stuart A. Aaronson
  • Toru Miki
  • Kimberly Meyers
  • Andrew Chan
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 348)


In the early 1980’s, approaches aimed at identifying the functions of retroviral oncogenes converged with efforts to investigate normal mitogenic signaling by growth factors. A number of retroviral oncogene products were found to be similar to the protein kinase encoded by v-src product1. Unlike many protein kinases that phosphorylate serine or threonine residues, the v-src product is a protein kinase that specifically phosphorylates tyrosine residues2. Purification and sequencing of growth factors and their receptors revealed that the platelet derived growth factor (PDGF) B-chain is similar to the predicted v-sis oncogene product3 and that the v-erbB oncogene product, which has sequence similarity to the v-src product, is a truncated form of the EGF receptor4. Binding of EGF to its receptor results in autophosphorylation of the receptor on tyrosine5. Oncogenes activated by a variety of mechanisms6 frequently have been shown to encode growth factors, receptor tyrosine kinases or downstream effectors.


Tyrosine Kinase Tyrosine Phosphorylation Platelet Derive Growth Factor GTPase Activate Protein Guanine Nucleotide Binding Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Stuart A. Aaronson
    • 1
  • Toru Miki
    • 1
  • Kimberly Meyers
    • 1
  • Andrew Chan
    • 1
  1. 1.Laboratory of Cellular and Molecular BiologyNational Cancer InstituteBethesdaUSA

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