Chinese Science Bulletin

, Volume 44, Issue 4, pp 335–339 | Cite as

Cytoskeleton-associated protein tyrosine phosphorylation involved in induction of differentiation in mouse melanoma cells

  • Chunhong Yan
  • Rui Han


The malignancy of a cancer is due partly to its poor differentiation. Genistein, a protein tyrosine kinase inhibitor, is found to induce the highly malignant B16-BL6 mouse melanoma cells to differentiate to mature phenotypes. When Triton X-100 insoluble fraction of the differentiated cells is prepared and analyzed, tyrosine phosphorylation levels of three cytoskeleton-associated proteins (65, 60 and 53 ku respectively) are found to decrease dramatically. But no any change is found when phosphotyrosine contents of the cytosol fraction or the total cellular protein preparations are evaluated. It is concluded that cytoskeleton-associated protein tyrosine phosphorylation may be involved in the control of differentiation of cancer cells. The decrease of phosphotyrosine contents of cytoskeleton-associated proteins may be one of the important mechanisms underlying the differentiation induction of cancer cells by anticancer agents.


cytoskeleton-associated protein protein tyrosine phosphorylation cancer cell differentiation protein tyrosine kinase inhibitor 


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  1. 1.
    Pawson, T., Bernstein, A., Receptor tyrosine kinases: genetic evidence for their role inDrosophila and mouse development,Trend Genet., 1990, 6: 350.CrossRefGoogle Scholar
  2. 2.
    Hirao, A., Hamaguchi, I., Suda, al., Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombinstimulated platelets,EMBO J., 1997, 16: 2342.PubMedCrossRefGoogle Scholar
  3. 3.
    Leventhal, P. S., Peldman, E. L., Tyrosine phosphorylation and enhanced expression of paxillin during neuronal differentiationin vitro, J. Biol. Chem., 1996, 271: 5957.PubMedCrossRefGoogle Scholar
  4. 4.
    Filvaroff, E., Stern, D. F., Dotto, G. P., Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation,Mol. Cell Biol., 1990, 10: 1164.PubMedGoogle Scholar
  5. 5.
    Cartwright, C. A., Mamajiwalla, S., Skolnick, S. al., Intestinal crypt cells contain higher levels of cytoskeletal-associated pp60c-src protein tyrcsine kinase activity than do differentiated enterocytes,Oncogenes, 1993, 8: 1033.Google Scholar
  6. 6.
    Peterson, G., Evaluation of the biochemical targets of genistein in tumor cells,J. Nutr., 1995, 125: 784s.PubMedGoogle Scholar
  7. 7.
    Winder, A. J., Harris, H., New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase,Eur. J. Biochem., 1991, 198: 317.PubMedCrossRefGoogle Scholar
  8. 8.
    Smith, P. K., Krohn, R. I., Hermanson, G. al., Measurement of protein using bicinchoninic acid,Anal. Biochem., 1985, 150: 76.PubMedCrossRefGoogle Scholar
  9. 9.
    Constantinou, A., Kiguchi, K., Huberman, E., Induction of differentiation and DNA strand breakage in human HL-60 and K-562 leukemia cells by genistein,Cancer Res., 1990, 50: 2618.PubMedGoogle Scholar
  10. 10.
    Yan, S. R., Fumagalli, L., Berton, G., Activation of SRC family kinases in human neutrophils. Evidence that p58c-FGR and p53/56LYN redistributed to a Triton X-100 insoluble cytoskeleton fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity,FEBS Lett., 1996, 380: 198.PubMedCrossRefGoogle Scholar

Copyright information

© Science in China Press 1999

Authors and Affiliations

  • Chunhong Yan
    • 1
  • Rui Han
    • 1
  1. 1.Institute of Materia MedicaChinese Academy of Medical Sciences and Peking Union Medical CollegeBeijingChina

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