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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Aug;73(8):2711–2715. doi: 10.1073/pnas.73.8.2711

Calcium-dependent regulatory protein of cyclic nucleotide metabolism in normal and transformed chicken embryo fibroblasts.

D M Watterson, L J Van Eldik, R E Smith, T C Vanaman
PMCID: PMC430718  PMID: 183206

Abstract

The concentration of a calcium-binding protein modulator of 3':5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17; 3':5'-cyclic-nucleotide 5'-nucleotidohydrolase) activity is increased in chicken embryo fibroblasts upon transformation by Rous sarcoma virus. This modulator protein from fibroblasts, which has roughly the same molecular size, charge, and functional properties as that isolated from chicken brain, comprises approximately 1.32% of the soluble protein in homogenates of fibroblasts infected and transformed by Rous sarcoma virus. In comparison, the modulator comprises approximately 0.30% of the soluble protein in homogenates of normal fibroblasts from confluent cultures and 0.36% of the soluble protein in homogenates of fibroblasts infected with a transformation-defective mutant of Rous sarcoma virus. Modulator levels in normal fibroblasts at subconfluent cell densities are 0.42-0.76% of the homogenate soluble protein, i.e., between that found in confluent normal fibroblasts and in fibroblasts transformed by Rous sarcoma virus. These observations suggest that the levels of the modulator protein are elevated under conditions in which chicken embryo fibroblasts are undergoing rapid growth and have decreased adenosine 3':5'-cyclic monophosphate levels.

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Selected References

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