Advertisement

High Levels of Oncomodulin and Calmodulin Expression in the Log Phase of Cell Growth in a Chemically Transformed Rat Fibroblast Cell Line

  • Janaki K. Blum
  • Ernst W. Sommer
  • Marianne C. Berger
  • Martin W. Berchtold
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)

Abstract

A variety of cellular processes are under the regulatory control of calcium. Alterations in fluxes and steady state levels of intracellular calcium appear to be responsible for evoking these events. Calcium homeostasis has been reported to be altered during tumorigenesis as well as upon transformation of cells in vitro by chemicals or viruses1. Neither the underlying molecular mechanisms related to calcium regulation in normal and tumor cells, nor the fact that transformed cells do not respond properly to normal regulatory controls are as yet well understood. Increased intracellular calcium levels could be partially responsible for a permanent activation of DNA synthesis and/or an increased mobility (invasive behaviour) of tumor cells.

Keywords

Calmodulin Gene Morris Hepatoma Proliferate Granulation Tissue Phase Specific Expression T14c Cell 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    J.F. Whitfield, A.L. Boynton, J.P. MacManus, M. Sikorska and B.K. Tsang, The regulation of cell proliferation by Ca2+ and cAMP. Mol.Cell Biochem. 27:155 (1979)PubMedCrossRefGoogle Scholar
  2. 2.
    J.P. MacManus, L.M. Brewer and J.F. Whitfield, The widely distributed tumor protein, oncomodulin is a normal constituent of human and rodent placentas. Cancer Lett. 21:309 (1985)CrossRefGoogle Scholar
  3. 3.
    E.W. Sommer and C.W. Heizmann, Expression of the tumor-specific and calcium-binding protein oncomodulin during chemical transformation of rat fibroblasts. Cancer Res. 49:899 (1989)PubMedGoogle Scholar
  4. 4.
    C.S. Furter, C.W. Heizmann and M.W. Berchtold, Isolation of a genomic oncomodulin clone and full length placental cDNA from rat. Experientia 45:A21 (1989)CrossRefGoogle Scholar
  5. 5.
    M.F. Gillen, D.Banville, R.G. Rutledge, S. Narang, V.L. Seligy, J.F. Whitfield, and J.P. MacManus, A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin. J.Biol.Chem. 262:5308 (1987)PubMedGoogle Scholar
  6. 6.
    J.A. Putkey, K.F. Ts’ui, T. Tanaka, L. Lagacé, J.P. Stein, E.C. Lai, and A.R. Means, Chicken calmodulin genes. A species comparison of cDNA sequences and isolation of a genomic clone. J.Biol.Chem. 258:11864 (1983)PubMedGoogle Scholar
  7. 7.
    H. Nojima and H. Sokabe, Structure of calmodulin genes in the rat genome. In: “Ca2+ signalling”, H. Hidaka, ed., Plenum Press, in press (1989)Google Scholar
  8. 8.
    C.D. Rasmussen, and A.R. Means, Calmodulin is involved in regulation of cell proliferation. EMBO J. 6:3961 (1987)PubMedGoogle Scholar
  9. 9.
    A.L. Boynton, J.P. MacManus and J.F. Whitfield, Stimulation of liver cell DNA synthesis by oncomodulin, a MW 11,500 calcium-binding protein from hepatoma. Exp.Cell.Res. 138: 454 (1982)PubMedCrossRefGoogle Scholar
  10. 10.
    B. Mutus, N. Karrupiah, and J.P. MacManus, The differential stimulation of brain and heart cyclic-AMP phosphodiesterase by oncomodulin. Biochem. Biophys. Res. Commun. 131:500 (1985)PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Janaki K. Blum
    • 1
    • 2
  • Ernst W. Sommer
    • 1
    • 2
  • Marianne C. Berger
    • 1
    • 2
  • Martin W. Berchtold
    • 1
    • 2
  1. 1.Institute of Pharmacology and BiochemistryUniversity of Zürich-IrchelZürichSwitzerland
  2. 2.Institute of ToxicologyETH-ZürichSchwerzenbachSwitzerland

Personalised recommendations