Corpus ID: 15962941

Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1.

@article{Recio2000BothNA,
  title={Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1.},
  author={J. Recio and J. Paez and B. Maskeri and M. Loveland and J. Velasco and V. Notario},
  journal={Cancer research},
  year={2000},
  volume={60 6},
  pages={
          1720-8
        }
}
Previous reports from our laboratory described the activation of the PCPH gene into the PCPH oncogene (mt-PCPH, reported previously as Cph) by a single point mutational deletion. As a consequence, the mt-PCPH oncoprotein is a truncated form of the normal PCPH protein. Although both proteins have ribonucleotide diphosphate-binding activity, only mt-PCPH acted synergistically with a human H-Ras oncoprotein to transform murine NIH3T3 fibroblasts. We report here the expression of the PCPH and mt… Expand
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Syrian hamster full-length cDNAs for the cph oncogene and proto-oncogene are isolated and show increased survival to various forms of stress, strongly suggesting that cph participates in cellular mechanisms of response to stress. Expand
Expression of the Protein Product of the PCPH Proto-oncogene in Human Tumor Cell Lines
TLDR
A study of PCPH expression in a larger sample of human neoplastic cell lines, including some derived from breast, nervous system, colon, lung and pancreas tumors, confirmed the frequent lack of PC PH expression in malignant cells and identified several immunoreactive forms ofPCPH being differentially expressed in cells of diverse tissue origins. Expand
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