Summary
Adenosine 3′,5′-cyclic monophosphate (cyclic AMP) phosphodiesterase activity in mouse neuroblastoma cells in culture markedly increased during exponential growth and reached a maximal level at confluency; whereas guanosine 3′, 5′-cyclic monophosphate (cyclic GMP) phosphodiesterase activity only slightly but significantly increased under a similar experimental condition. The increase in cyclic AMP phosphodiesterase activity was blocked by both cycloheximide and dactinomycin, whereas the increase in cyclic GMP phosphodiesterase was blocked by only cycloheximide. When the confluent cells were replated at low density, the cyclic nucleotide phosphodiesterase activity decreased; however, when they were plated at high cell density which equaled confluency, the enzyme activity did not decrease. Unlike cyclic AMP phosphodiesterase activity, cyclic GMP phosphodiesterase activity did not change significantly in prostaglandin E1-treated cells, but decreased in cells treated with the inhibitor of phosphodiesterase. Like cyclic AMP phosphodiesterase activity, cyclic GMP phosphodiesterase activity also did not change in cells treated with serum-free medium, X-irradiation, sodium butyrate and 6-thioguanine.
Similar content being viewed by others
References
Prasad, K. N., and S. Kumar. 1973. Cyclic 3′,5′-AMP phosphodiesterase activity during cyclic AMP-induced differentiation of neuroblastoma cells in culture. Proc. Soc. Exp. Biol. Med. 142: 406–409.
D’Armiento, M., G. S. Johnson, and I. Pastan. 1972. Regulation of adenosine 3′,5′-cyclic monophosphate phosphodiesterase activity in fibroblasts by intracellular concentrations of cyclic adenosine monophosphate. Proc. Natl. Acad. Sci. U.S.A. 69: 425–429.
Maganiello, V., and M. Vaughan. 1972. Prostaglandin E1 effects on adenosine 3′,5′-cyclic monophosphate concentration and phosphodiesterase activity in fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 69: 269–273.
Lynch, T. J., E. A. Tallant, and W. Y. Cheung. 1975. Marked reduction of cyclic GMP phosphodiesterase activity in virally transformed mouse fibroblasts. 65: 1115–1122.
Schwartz, J. P., and J. U. Passonneau. 1974. Cyclic AMP mediated induction of the cyclic AMP phosphodiesterase of C-6 glioma cells. Proc. Natl. Acad. Sci. U.S.A. 71: 3844–3848.
Schwartz, J. P., N. R. Morris, and B. L. Breckenridge. 1973. Adenosine 3′,5′-monophosphate in glial tumor cells. Alteration by 5-bromodeoxyuridine. J. Biol. Chem. 248: 2699–2704.
Prasad, K. N. 1973. Role of cyclic AMP in differentiation of neuroblastoma cells in culture. In: J. Schultz, and H. G. Gratzner, (Eds.),The Role of Cyclic Nucleotides in Carcinogenesis Vol. 6. Academic Press, New York, pp. 207–247.
Rosenberg, R. N., L. Vandeventer, L. De Francesco, and M. K. 1971. Regulation of the synthesis of choline-0-acetyltransferase and thymydylate synthetase in mouse neuroblastoma in culture. Proc. Natl. Acad. Sci. U.S.A. 68: 1436–1440.
Bachrach, U. 1976. Induction of ornithine decarboxylase in glioma and neuroblastoma cells. FEBS Lett. 68: 63–67.
Prasad, K. N. and A. W. Hsie. 1971. Morphologic differentiation of mouse neuroblastoma cells induced in vitro by dibutyryl adenosine 3′:5′-cyclic monophosphate. Nature [New Biol.] 233: 141–142.
Prasad, K. N., B. Mandal, J. C. Waymire, G. J. Lees, A. Vernadakis, and N. Weiner. 1973. Basal level of neurotransmitter synthesizing enzymes and effect of cyclic AMP agents on the morphological differentiation of isolated neuroblastoma clones. Nature [New Biol.] 241: 117–119.
Sheppard, H., G. Wiggan, and W. H. Tsien. 1972. Structure-activity relationships for inhibitors of phosphodiesterase from erythrocytes and other tissue. In: P. Greengard, G. A. Robinson, and R. Paoletti (Eds.),Advances in Cyclic Nucleotide Research. Vol. 1. Raven Press, New York, pp. 102–112.
Prasad, K. N. 1975. Differentiation of neuroblastoma cells in culture. Biol. Rev. 50: 129–165.
Eagle, H. 1974. Effect of environmental pH on the growth and function of culture mammalian cells. In: B. Clarkson, and R. Baserga (Eds.)Control of Proliferation in Animal Cells. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp. 1–11.
O’Dea, R. F., M. K. Haddox, and N. D. Goldberg. 1971. Interaction with phosphodiesterase of free and kinase complexed cyclic adenosine 3′,5′-monophosphate. J. Biol. Chem. 246: 6183–6190.
Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193: 265–275.
Kumar, S., G. Becker, and K. N. Prasad. 1975. Cyclic adenosine 3′,5′-monophosphate phosphodiesterase activity in malignant and cyclic adenosine 3′,5′-monophosphate-induced “differentiated” neuroblastoma cells. Cancer Res. 35: 82–87.
Cheung, W. Y. 1970. Cyclic nucleotide phosphodiesterase. In: P. Greengard, and E. Costa (Eds.),Role of Cyclic AMP in Cell Function. Raven Press, New York, pp. 51–65.
Prasad, K. N., G. Becker, and K. Tripathy. 1975. Differences and similarities between guanosine 3′,5′-cyclic monophosphate phosphodiesterase and adenosine 3′,5′-cyclic monophosphate phosphodiesterase activities in neuroblastoma cells in culture. Proc. Soc. Exp. Biol. Med. 149: 757–762.
Bourne, H. R., G. M. Tomkins, and S. Dion. 1973. Regulation of phosphodiesterase synthesis: requirement for cyclic adenosine monophosphate-dependent protein kinase. Science 181: 952–954.
Prasad, K. N., D. Fogleman, M. Gaschler, P. K. Sinha, and J. L. Brown. 1976. Cyclic nucleotide-dependent protein kinase activity in malignant and cyclic AMP-induced “differentiated” neuroblastoma cells in culture. Biochem. Biophys. Res. Commun. 68: 1248–1255.
Author information
Authors and Affiliations
Additional information
This work was supported by USPHS NS-09230, and DRG-1273 from Damon Runyon-Walter Winchell Cancer Fund.
Rights and permissions
About this article
Cite this article
Sinha, P.K., Prasad, K.N. A further study on the regulation of cyclic nucleotide phosphodiesterase activity in neuroblastoma cells: Effect of growth. In Vitro 13, 497–501 (1977). https://doi.org/10.1007/BF02615142
Issue Date:
DOI: https://doi.org/10.1007/BF02615142