ADP-ribosylation of the rho/rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells

Biochem Biophys Res Commun. 1990 Feb 28;167(1):265-72. doi: 10.1016/0006-291x(90)91760-p.


Botulinum ADP-ribosyltransferase C3 (C3 exoenzyme) was purified to homogeneity and added to cultured rat pheochromocytoma PC-12 cells. Incubation with this exoenzyme caused inhibition of cell growth and induced neurites as well as acetylcholine esterase in these cells. These changes were dependent on the amount of the enzyme added to the culture, which correlated with the in situ ADP-ribosylation of the rho/rac proteins in the cells. Preincubation with a specific anti-C3 exoenzyme monoclonal antibody inhibited both the ADP-ribosyltransferase activity and the neurite-inducing activity of the enzyme preparation. These results suggest that C3 exoenzyme affected the cellular function of the rho/rac proteins by ADP-ribosylation to induce these changes in the cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / biosynthesis*
  • Animals
  • Axons / enzymology
  • Cell Division
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Induction
  • GTP-Binding Proteins / metabolism*
  • Membrane Proteins / metabolism
  • Neurons / cytology*
  • Poly(ADP-ribose) Polymerases / pharmacology*
  • Rats
  • Tumor Cells, Cultured / enzymology


  • Membrane Proteins
  • Poly(ADP-ribose) Polymerases
  • Acetylcholinesterase
  • GTP-Binding Proteins