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Transformation-specific decrease of phosphorylation of 80K protein, a substrate of protein kinase C, in NIH3T3 cells.
M Oh-uchida1, K Yano, S Kawamoto
1Department of Biology, Faculty of Science, Kyushu University, Fukuoka.
Japanese Journal of Cancer Research : Gann
|August 1, 1990
Summary
Cellular transformation by oncogenes leads to decreased 80K protein phosphorylation. Normal cells show elevated 80K protein phosphorylation, indicating an inverse correlation with transformation.
Area of Science:
- Cell Biology
- Molecular Oncology
Background:
- Protein kinase C (PKC) plays a role in cellular signaling pathways.
- The 80K protein is a specific substrate for PKC.
- Cellular transformation can alter protein phosphorylation patterns.
Purpose of the Study:
- To compare the phosphorylation levels of the 80K protein in normal versus transformed NIH3T3 cells.
- To investigate the relationship between oncogene-induced cellular transformation and 80K protein phosphorylation.
Main Methods:
- Two-dimensional gel electrophoresis was used to analyze protein phosphorylation.
- NIH3T3 cells were transformed with various oncogenes (c-raf, H-ras, N-ras, K-ras, src, mos, polyoma middle T antigen).
- Phosphorylation levels were assessed with and without phorbol ester (TPA) stimulation and varying serum concentrations.
Main Results:
- NIH3T3 cells transformed by c-raf or H-ras oncogenes exhibited decreased 80K protein phosphorylation.
- Normal NIH3T3 cells maintained elevated 80K protein phosphorylation levels.
- Transformation by other oncogenes (N-ras, K-ras, src, mos, polyoma middle T antigen) also resulted in decreased 80K protein phosphorylation.
Conclusions:
- Phosphorylation of the 80K protein is inversely correlated with cellular transformation.
- Oncogene-induced transformation disrupts normal 80K protein phosphorylation patterns.