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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
. 1973 Jan;70(1):76–79. doi: 10.1073/pnas.70.1.76

Induction of Cytolysis of Cultured Lymphoma Cells by Adenosine 3′:5′-Cyclic Monophosphate and the Isolation of Resistant Variants

Violet Daniel 1,*, Gerald Litwack 1,, Gordon M Tomkins 1
PMCID: PMC433187  PMID: 4346041

Abstract

Cultured mouse lymphosarcoma cells are killed on exposure to 0.1 mM N6,O2′-dibutyryl-adenosine 3′:5′-cyclic monophosphate. A population of cells resistant to the killing effect of dibutyryl cyclic AMP at concentrations as high as 1 mM was selected. The growth characteristics of the resistant cells were similar to those of the sensitive parental line. However, the resistant cells contain less cytoplasmic cyclic AMP-binding proteins and decreased cyclic AMP-stimulated protein kinase activity. It is proposed that transition from sensitivity to resistance to dibutyryl cyclic AMP in lymphoma cells is connected with a modification of the cyclic AMP-binding protein, which appears to be the regulatory subunit of the cyclic AMP-activated protein kinase.

Keywords: cytoplasmic receptor molecules, protein kinase

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baxter J. D., Harris A. W., Tomkins G. M., Cohn M. Glucocorticoid receptors in lymphoma cells in culture: relationship to glucocorticoid killing activity. Science. 1971 Jan 15;171(3967):189–191. doi: 10.1126/science.171.3967.189. [DOI] [PubMed] [Google Scholar]
  2. Gilman A. G. A protein binding assay for adenosine 3':5'-cyclic monophosphate. Proc Natl Acad Sci U S A. 1970 Sep;67(1):305–312. doi: 10.1073/pnas.67.1.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Granner D., Chase L. R., Aurbach G. D., Tomkins G. M. Tyrosine aminotransferase: enzyme induction independent of adenosine 3', 5'-monophosphate. Science. 1968 Nov 29;162(3857):1018–1020. doi: 10.1126/science.162.3857.1018. [DOI] [PubMed] [Google Scholar]
  4. Horibata K., Harris A. W. Mouse myelomas and lymphomas in culture. Exp Cell Res. 1970 Apr;60(1):61–77. doi: 10.1016/0014-4827(70)90489-1. [DOI] [PubMed] [Google Scholar]
  5. Johnson G. S., Friedman R. M., Pastan I. Restoration of several morphological characteristics of normal fibroblasts in sarcoma cells treated with adenosine-3':5'-cyclic monphosphate and its derivatives. Proc Natl Acad Sci U S A. 1971 Feb;68(2):425–429. doi: 10.1073/pnas.68.2.425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kabat D. Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity. Biochemistry. 1971 Jan 19;10(2):197–203. doi: 10.1021/bi00778a001. [DOI] [PubMed] [Google Scholar]
  7. Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. IV. Widespread occurrence of adenosine 3',5'-monophosphate-dependent protein kinase in various tissues and phyla of the animal kingdom. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1349–1355. doi: 10.1073/pnas.64.4.1349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Makman M. H., Dvorkin B., White A. Evidence for induction by cortisol in vitro of a protein inhibitor of transport and phosphorylation processes in rat thymocytes. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1269–1273. doi: 10.1073/pnas.68.6.1269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Rosenau W., Baxter J. D., Rousseau G. G., Tomkins G. M. Mechanism of resistance to steroids: glucocorticoid receptor defect in lymphoma cells. Nat New Biol. 1972 May 3;237(70):20–24. doi: 10.1038/newbio237020a0. [DOI] [PubMed] [Google Scholar]
  11. Rousseau G. G., Baxter J. D., Tomkins G. M. Glucocorticoid receptors: relations between steroid binding and biological effects. J Mol Biol. 1972 Jun 14;67(1):99–115. doi: 10.1016/0022-2836(72)90389-0. [DOI] [PubMed] [Google Scholar]
  12. Walsh D. A., Perkins J. P., Krebs E. G. An adenosine 3',5'-monophosphate-dependant protein kinase from rabbit skeletal muscle. J Biol Chem. 1968 Jul 10;243(13):3763–3765. [PubMed] [Google Scholar]

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