Phospholipase-induced maturation of Xenopus laevis oocytes: mitogenic activity of generated metabolites

J Cell Biochem. 1993 Aug;52(4):440-8. doi: 10.1002/jcb.240520408.

Abstract

Signal transduction induced by generation of second messengers from membrane phospholipids is considered a major regulatory mechanism in control of cell proliferation. We report here that in the Xenopus laevis oocytes model, microinjection of the three most relevant types of phospholipases acting on membrane phospholipids (A2, C, and D) are capable of inducing oocyte maturation with similar efficiencies. This effect is mediated by the generation of known second messengers such as lyso-phospholipids, arachidonic acid, diacylglycerol, and phosphatidic acid. Specific inhibitors of protein kinase C made it possible to identify alternative independent signalling pathways for induction of oocyte maturation. Our results indicate that while phospholipase C seems to be dependent on protein kinase C (PKC), phospholipase A2, and phospholipase D are completely independent of protein kinase C function. Thus, the oocyte system is a powerful tool for the analysis of the potential mitogenic activity of lipid metabolites. It is also an excellent tool for unravelling the different routes involved in the regulation of cell growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaloids / pharmacology
  • Animals
  • Diglycerides / metabolism
  • Indoles / pharmacology
  • Maleimides / pharmacology
  • Microinjections
  • Mitosis / drug effects
  • Oocytes / cytology*
  • Oocytes / metabolism
  • Peptide Fragments / metabolism
  • Phosphatidylcholines / metabolism
  • Phosphatidylinositols / metabolism
  • Phospholipases / pharmacology
  • Phospholipases / physiology*
  • Protein Kinase C / physiology
  • Signal Transduction*
  • Staurosporine
  • Xenopus laevis

Substances

  • Alkaloids
  • Diglycerides
  • Indoles
  • Maleimides
  • Peptide Fragments
  • Phosphatidylcholines
  • Phosphatidylinositols
  • Protein Kinase C
  • Phospholipases
  • Staurosporine
  • bisindolylmaleimide I