Advertisement

Phospholipases a of Krebs II Ascites Cells: Specificity, Release and Subcellular Localization

  • J. Lloveras
  • M. Record
  • G. Ribbes
  • L. Douste-Blazy
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)

Abstract

The phenomenon of contact inhibition has proved to be closely related to growth control. It was demonstrated that insensibility of cells in culture to contact inhibition is proportional to their malignancy in animals (6). In attempting to define the biochemical basis of contact inhibition, attention has naturally centered on the cell surface and its components, and particularly on phospholipids. It was stated that virus-transformed cells, thus having malignant potentialities renewed their phospholipids at a greater rate than normal controls. Among the enzymes of the plasma membrane, the phospholipases A have been mainly studied in normal hepatocyte (5) (11) and in cells infected with measles virus (8). We have a poor knowledge of them in the neoplastic cell and their role in the cell membrane is not clear. Therefore we investigated the specificity Al or A2 the intracellular distribution and the release in the extracellular environment of phospholipases A in Krebs II ascites tumor cells, maintained in female Swiss strain mice (9–12 weeks aged) by weekly intraperitoneal transfer of ascitic fluid.

Keywords

Ascitic Fluid Measle Virus Contact Inhibition Normal Hepatocyte Fatty Acid Moieities 
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.
    Bligh, E.D. and Dyer, N.J. (1959). Can. J. Biochem. Physiol., 37, 911.PubMedCrossRefGoogle Scholar
  2. 2.
    Brockerhoff, H. and Jensen, R.J. (1974). In Lipolytic Enzymes (Brockerhoff, H. and Jensen, R.J. eds), p. 197, Academic Press, New York.Google Scholar
  3. 3.
    Lindhart, K. and Walter, K. (1963). In Methods in Enzymatic Analysis (Bergmeyer, H.U. ed.), p. 783, Academic Press, New York.Google Scholar
  4. 4.
    Lloveras, J. and Douste-Blazy, L. (1973). Eur. J. Biochem. 33, 567.PubMedCrossRefGoogle Scholar
  5. 5.
    Newkirk, J.D. and Waite, M. (1973). Biochim. Biophys. Acta, 298, 562.Google Scholar
  6. 6.
    Pasternak, C.A. (1973). In Tumor lipids: Biochemistry and Metabolism (Wood, R. ed.), p. 66, American Oil Chemists’ Society, Champaign Illinois.Google Scholar
  7. 7.
    Poole, A.R. (1973). In Lysosomes in Biology and Pathology (Dingle, J.T. ed.), p. 303, North Holland Publishing Company, Amsterdam.Google Scholar
  8. 8.
    Suzuki, Y. and Matsumoto, M. (1974). Biochem. Biophys. Res. Commun. 57, 505.PubMedCrossRefGoogle Scholar
  9. 9.
    Sylven, B. (1968), Eur. J. Cancer, 4, 443.Google Scholar
  10. 10.
    Tisdale, T.H. (1967). In Methods in Enzymology (Colowick, S.P. and Kaplan, N.O. eds) vol. X, p. 213, Academic Press, New York.Google Scholar
  11. 11.
    Victoria, E.J., Van Golde, L.M.C., Hostetler, K.Y., Sherpol, G.L. and Van Deenen, L.L.M. (1971). Biochim. Biophys. Acta, 239, 443.CrossRefGoogle Scholar
  12. 12.
    Wallach, D.F.H. and Kamat, V.B. (1974). In Methods in Enzymology (Colowick, J.P. and Kaplan, N.O. eds), vol. VIII, p. 164, Academic Press New York.Google Scholar
  13. 13.
    Wallach, D.F.H. and Winzler, R.J. (1974). In Evolving Strategies and Tactics in Membrane Research (Wallach, D.F.H. and Winzler, R.J. eds), p. 4, Springer-Verlag, Berlin.CrossRefGoogle Scholar
  14. 14.
    Wroblewsky, F. and La Due, J.J. (1955). Proc. Soc. Exp. Biol., 90, 210.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • J. Lloveras
    • 1
  • M. Record
    • 1
  • G. Ribbes
    • 1
  • L. Douste-Blazy
    • 1
  1. 1.I.N.S.E.R.M., Unité 101, Biochimie des LipidesHôpital PurpanToulouseFrance

Personalised recommendations