Potentiation of K252a, a protein kinase inhibitor-induced polyploidization by cAMP in cultured fibrosarcoma cell line

Biochem Biophys Res Commun. 1994 Nov 30;205(1):746-50. doi: 10.1006/bbrc.1994.2728.

Abstract

We found that K252a, a potent inhibitor of protein kinases (PK), induced DNA re-replication of Meth-A cells, i.e., DNA synthesis at a higher DNA ploidy without undergoing cytokinesis (polyploidization). The K252a-induced polyploidization was inhibited by phorbol 12-myristate 13-acetate (PMA), a protein kinase C (PKC) activator, suggesting that the polyploidization is caused through inhibition of PKC. By contrast, the polyploidization was potentiated by adenosine 3':5'-cyclic monophosphate (cAMP), a cAMP-dependent protein kinase (PKA) activator. These findings suggest that the cAMP-dependent signaling pathway and diacylglycerol (DAG)-dependent signaling pathway play an important role in regulating the induction of polyploidization in Meth-A cells, through a possible "cross-talk" between the two pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / pharmacology
  • Animals
  • Bucladesine / pharmacology*
  • Carbazoles / pharmacology*
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors*
  • Cycloheximide / pharmacology
  • DNA / biosynthesis
  • Down-Regulation
  • Drug Synergism
  • Indole Alkaloids
  • Mice
  • Mice, Inbred BALB C
  • Polyploidy*
  • Signal Transduction
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tumor Cells, Cultured

Substances

  • Carbazoles
  • Indole Alkaloids
  • Bucladesine
  • Adenosine Triphosphate
  • DNA
  • staurosporine aglycone
  • Cycloheximide
  • Cyclic AMP-Dependent Protein Kinases
  • Tetradecanoylphorbol Acetate