Temporal changes in intracellular distribution of protein kinase C in Swiss 3T3 cells during mitogenic stimulation with insulin-like growth factor I and bombesin: translocation to the nucleus follows rapid changes in nuclear polyphosphoinositides

Biochem Biophys Res Commun. 1991 May 31;177(1):480-7. doi: 10.1016/0006-291x(91)92009-9.

Abstract

Using a polyclonal antibody raised against a synthetic peptide of the catalytic region of protein kinase C, we have carried out a combined immunocytochemical and immunochemical analysis to follow the subcellular localisation of this enzyme in response to mitogenic stimulation with insulin-like growth factor I and bombesin. These investigations show a time dependent translocation of protein kinase C from the cytoplasm to the nucleus since 5 min stimulation reaching a maximal effect after 45 min. These results show clearly that mitogen induced translocation of protein kinase C to the nucleus follows temporally the earlier changes in nuclear polyphosphoinositide metabolism previously demonstrated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bombesin / pharmacology*
  • Cell Compartmentation / drug effects
  • Cell Division / drug effects
  • Cell Line
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Immunoblotting
  • Immunohistochemistry
  • Insulin-Like Growth Factor I / pharmacology*
  • Kinetics
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Proteins / isolation & purification
  • Nuclear Proteins / metabolism
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols / metabolism*
  • Protein Kinase C / metabolism*
  • Time Factors

Substances

  • Nuclear Proteins
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols
  • Insulin-Like Growth Factor I
  • Protein Kinase C
  • Bombesin