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Updated: Aug 11, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
Published on: January 7, 2013
A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by
Y Ishizaka1, M Takahashi, T Ushijima
1Carcinogenesis Division, National Cancer Center Research Institute, Tokyo, Japan.
Abstract:
A 57 kDa protein was detected in an NIH3T3 transformant induced by retTPC, an activated form of the ret proto-oncogene which encodes a receptor-tyrosine kinase. A high phosphorylation state and increased activity of a TPA responsive element was observed in the transformant. Increased expression of c-jun mRNA was also detected. A 40 kDa protein in the retTPC transformant, which was specifically immunoprecipitable with v-jun antiserum, was highly phosphorylated mainly at a serine residue(s). These data suggest that an aberrant signal triggered by a retTPC product affects the cellular serine/threonine phosphorylation state resulting in high phosphorylation of c-jun protein.
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