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 language | English |
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Pages (from-to) | 799-806 |
Number of pages | 8 |
Journal | Japanese Journal of Cancer Research |
Volume | 81 |
Issue number | 8 |
DOIs | |
Publication status | Published - Aug 1990 |
Externally published | Yes |
Keywords
- 80K Protein phosphorylation
- H‐ras transformant
- Phorbol ester
- Protein kinase C
- raf
- transformant
ASJC Scopus subject areas
- Oncology
- Cancer Research