Transformation-specific Decrease of Phosphorylation of 80K Protein, a Substrate of Protein Kinase C, in NIH3T3 Cells
| Autor: | Shoko Kawamoto, Kazumi Yano, Kenji Shimizu, Mamoru Oh-uchida |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Phorbol ester
Cancer Research macromolecular substances raf Biology Article Substrate Specificity Enzyme activator Stomach Neoplasms Protein kinase C Proto-Oncogene Proteins Tumor Cells Cultured Humans Protein phosphorylation Phosphorylation H‐ras transformant Protein kinase A neoplasms 80K Protein phosphorylation Cell Line Transformed Molecular biology transformant Enzyme Activation Molecular Weight Proto-Oncogene Proteins c-raf enzymes and coenzymes (carbohydrates) Oncology Tetradecanoylphorbol Acetate biology.protein Protein A Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Japanese Journal of Cancer Research : Gann |
| ISSN: | 0910-5050 |
| DOI: | 10.1111/j.1349-7006.1990.tb02648.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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