Polypeptide Synthesis in Human Sarcoma and Normal Tissue

  • J. Forchhammer
  • H. Macdonald-Bravo


Over the past few years the study of quantitative changes in the proteins of transformed cell lines have mainly taken two directions. One line of experimentation has been concerned with the total cellular response to transformation (1–5), while the other has been directed to search for changes in few cellular proteins whose expression is presumed to represent primary lesions in cells transformed with DNA or RNA tumour viruses (6–9). Both experimental approaches have made use mainly of cultured cell lines. At present, the relative proportions of at least 50 polypeptides have been shown to change in transformed cell lines of human origin (1). Furthermore 13 host genes have been shown to be involved in transmission of different malignancies with different retroviruses (9). (See also other related articles in this volume).


Control Tissue Malignant Fibrous Histiocytoma Fibrous Connective Tissue Transform Cell Line Rous Sarcoma Virus 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1).
    BRAVO, R. and CELIS, J.E. (1982). Human proteins sensitive to neoplastic transformation in cultured epithelial and fibroblast cells. Clin. Chem. 28, 949.PubMedGoogle Scholar
  2. 2).
    STRand, M. and AUGUST, J.T. (1978). Polypeptide maps of cells infected with murine type C leukemia or sarcoma oncovirus. Cell, 13, 399.PubMedCrossRefGoogle Scholar
  3. 3).
    FORCHHAMMER, J. and KLARLUND, J. (1979). Changes in proteins from transformed cultures and tumours induced by sarcoma virus. In: Advances in Medical Oncology, Research and Education (ed. P.G. Margison) Vol. 1, p. 51, Pergamon Press, Oxford.Google Scholar
  4. 4).
    BRAVO, R. and CELIS, J.E. (1980). Gene expression in normal and vi rally transformed mouse 3T3B and hamster BHK21 cells. Exp. Cell Res. 127, 249.PubMedCrossRefGoogle Scholar
  5. 5).
    BRZESKI, H. and EGE, T. (1980). Changes in polypeptide pattern in ASV-transformed rat cells are correlated with the degree of morphological transformation. Cell, 22, 513.PubMedCrossRefGoogle Scholar
  6. 6).
    BRUGGE, J.S., ERIKSON, E. and ERIKSON, R.L. (1981). The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins. Cell, 25, 363.PubMedCrossRefGoogle Scholar
  7. 7).
    RADKE, K. and MARTIN, G.S. (1980). Transformation by Rous sarcoma virus: Effects of src-gene expression on the synthesis and phosphorylation of cellular polypeptides. Cold Spring Harbor Symp. Quant. Biol. 44, 975.PubMedCrossRefGoogle Scholar
  8. 8).
    SHARP, P.A. (1980). Summary: Molecular biology of viral oncogenes. Cold Spring Harbor Symp. Quant. Biol. 44, 1305.PubMedCrossRefGoogle Scholar
  9. 9).
    COFFIN, J.M., VARMUS, H.E., BISHOP, J.M., ESSEX, M., HARDY, W.D., MARTIN, G.S., ROSENBERG, N.E., SCOLNICK, E.M., WEINBERG, R.A. and VOGT, P.K. (1981). Proposal for naming host cell derived inserts in retrovirus genomes. J. Virol. 40, 953.PubMedGoogle Scholar
  10. 10).
    O’FARRELL, P.H. (1975). High resolution two dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007.PubMedGoogle Scholar
  11. 11).
    O’FARRELL, P.Z., GOODMAN, H.M. and O’FARRELL, P.H. (1977). High resolution two dimensional electrophoresis of basic as well as acidic proteins. Cell, 12, 1133.PubMedCrossRefGoogle Scholar
  12. 12).
    ANSORGE, W. (1981). Preparation of ultrathin gels (0.1–0.2 mm). Applications to protein separation with a new silver staining. In: International Conference in Electrophoresis, Charlston, S.C., in press.Google Scholar
  13. 13).
    MOSE LARSEN, P. (1981). An assessment of the potential offered by two dimensional gel electrophoresis and silver staining for developmental biology. (Thesis: Dept of Chemistry, Aarhus University, Denmark).Google Scholar
  14. 14).
    HAJDU, S. (1979). Pathology of soft tissue tumours. Lea and Fibiger, Philadelphia, ISBN 0–8121-0693–8.Google Scholar
  15. 15).
    BRAVO, R., SMALL, J.V., FEY, S.J., MOSE LARSEN, P. and CELIS, J.E. (1982). Architecture and polypeptide composition of HeLa cytoskeletons. Modification of cytoarchitectural polypeptides during mitosis. J. Mol. Biol. 154, 121.PubMedCrossRefGoogle Scholar
  16. 16).
    BRAVO, R., FEY, S.J., SMALL, J.V., MOSE LARSEN, P. and CELIS, J.E. (1981). Coexistence of three major isoactins in a single sarcoma 180 cell. Cell, 25, 195.PubMedCrossRefGoogle Scholar
  17. 17).
    BRAVO, R. and CELIS, J.E. (1982). Up-dated catalogue of HeLa cell proteins: Percentages and characteristics of the major cell polypeptides labelled with a mixture of 16 [14C]-amino acids. Clin. Chem. 28, 766.PubMedGoogle Scholar
  18. 18).
    FORCHHAMMER, J. (1982). Quantitative changes of some cellular polypeptides in C3H mouse following transformation by Moloney sarcoma virus. In: “Biological markers of neoplastic transformation”. (ed. P. Chandra), Plenum, in press.Google Scholar
  19. 19).
    BUZIN, C.H. and PETERSEN, N.S. (1982). A comparison of the multiple Drosophila heat shock proteins in cell lines and larval salivary glands by two dimensional gel electrophoresis. J. Mol. Biol. 158, 181.PubMedCrossRefGoogle Scholar
  20. 20).
    HICKEY, E.D. and WEBER, L.A. (1982). Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery. Biochemistry, 21, 1513.PubMedCrossRefGoogle Scholar
  21. 21).
    TOPP, U.C., LANE, D. and POLLACK, R. (1980). Transformation by SV40 and polyoma virus. In: Molecular biology of tumour viruses, (ed. J. Tooze) part 2, pp. 205. Cold Spring Harbor, New York.Google Scholar
  22. 22).
    BRAVO, R., FEY, S.J., BELLATIN, J., MOSE LARSEN, P. and CELIS, J.E. (1982). Identification of a nuclear polypeptide (cyclin) whose relative proportion is sensitive to changes in the rate of cell proliferation and to transformation. In: Proceedings of the International Society of Developmental Biology, (ed. M. Burger), Alan R. Liss, New York, In press.Google Scholar
  23. 23).
    CURRIE, R.W. and WHITE, F.P. (1981). Trauma-induced protein in rat tissues. A physiological role for a “heat shock” protein?. Science, 214, 72.PubMedCrossRefGoogle Scholar
  24. 24).
    HAMMOND, G.L., LAI, Y.-K. and MARKERT, C.L. (1982). Diverse forms of stress lead to new patterns of gene expression through a common and essential metabolic pathway. Proc. Natl. Acad. Sci. USA, 79, 3485.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • J. Forchhammer
    • 1
    • 2
  • H. Macdonald-Bravo
    • 1
  1. 1.Department of ChemistryUniversity of AarhusAarhus CDenmark
  2. 2.The Fibiger LaboratoryCopenhagen ØDenmark

Personalised recommendations