Transformation‐specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells

Mamoru Oh‐uchida, Kazumi Yano, Shoko Kawamoto, Kenji Shimizu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Phosphorylation in normal and transformed NIH3T3 cells of the 80K protein, a specific substrate for protein kinase C, was compared by means of two‐dimensional gel analysis. We obtained evidence that NIH3T3 cells transformed by the c‐raf or H‐ras oncogene maintained a decreased level of phosphorylation of the 80K protein, with or without phorbol ester (TPA)‐stimulation, at all concentrations of serum tested while normal NIH3T3 cells maintained an elevated level of phosphorylation of the 80K protein. Furthermore, NIH3T3 cells transformed by N‐ras, K‐ras, src, mos or polyoma middle T antigen exhibited a decreased level of phosphorylation of the 80K protein. These events were confirmed by an analysis of a hormone‐inducible H‐ras transformant. Thus, phosphorylation of the 80K protein is inversely correlated with cellular transformation.

Original languageEnglish
Pages (from-to)799-806
Number of pages8
JournalJapanese Journal of Cancer Research
Volume81
Issue number8
DOIs
Publication statusPublished - Aug 1990
Externally publishedYes

Keywords

  • 80K Protein phosphorylation
  • H‐ras transformant
  • Phorbol ester
  • Protein kinase C
  • raf
  • transformant

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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