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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
. 1989 Nov;86(21):8417–8421. doi: 10.1073/pnas.86.21.8417

Tumor necrosis factor induces phosphorylation of a 28-kDa mRNA cap-binding protein in human cervical carcinoma cells.

M W Marino 1, L M Pfeffer 1, P T Guidon Jr 1, D B Donner 1
PMCID: PMC298293  PMID: 2813400

Abstract

Tumor necrosis factor alpha (TNF-alpha) stimulated the phosphorylation of a 28-kDa protein (p28) in the ME-180 line of human cervical carcinoma cells. The effect of TNF-alpha on the phosphorylation state of p28 was rapid (4-fold increase within 15 min) and persistent, remaining above the basal level for at least 2 hr. The specific binding of 125I-labeled TNF-alpha to cell-surface binding sites, the stimulation of p28 phosphorylation by TNF-alpha, and the inhibition of cell proliferation by TNF-alpha occurred with nearly identical dose-response relationships. Two-dimensional SDS/PAGE resolved p28 into two isoforms having pI values of 6.2 and 6.1. A phosphorylated cap-binding protein was substantially enriched from lysates of control or TNF-alpha-treated ME-180 cells by affinity chromatography with 7-methylguanosine 5'-triphosphate-Sepharose. The phosphoprotein recovered from this procedure was the substrate for TNF-alpha-promoted phosphorylation, p28. Thus, TNF-alpha stimulates the phosphorylation of this mRNA cap-binding protein, which may be involved in the transduction of TNF-alpha-receptor binding into cellular responses.

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Selected References

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  1. Aggarwal B. B., Eessalu T. E. Induction of receptors for tumor necrosis factor-alpha by interferons is not a major mechanism for their synergistic cytotoxic response. J Biol Chem. 1987 Jul 25;262(21):10000–10007. [PubMed] [Google Scholar]
  2. Aggarwal B. B., Traquina P. R., Eessalu T. E. Modulation of receptors and cytotoxic response of tumor necrosis factor-alpha by various lectins. J Biol Chem. 1986 Oct 15;261(29):13652–13656. [PubMed] [Google Scholar]
  3. Bachwich P. R., Chensue S. W., Larrick J. W., Kunkel S. L. Tumor necrosis factor stimulates interleukin-1 and prostaglandin E2 production in resting macrophages. Biochem Biophys Res Commun. 1986 Apr 14;136(1):94–101. doi: 10.1016/0006-291x(86)90881-8. [DOI] [PubMed] [Google Scholar]
  4. Beutler B., Cerami A. Cachectin and tumour necrosis factor as two sides of the same biological coin. Nature. 1986 Apr 17;320(6063):584–588. doi: 10.1038/320584a0. [DOI] [PubMed] [Google Scholar]
  5. Bonneau A. M., Sonenberg N. Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis. J Biol Chem. 1987 Aug 15;262(23):11134–11139. [PubMed] [Google Scholar]
  6. Buckley B., Ehrenfeld E. Two-dimensional gel analyses of the 24-kDa cap binding protein from poliovirus-infected and uninfected HeLa cells. Virology. 1986 Jul 30;152(2):497–501. doi: 10.1016/0042-6822(86)90155-8. [DOI] [PubMed] [Google Scholar]
  7. Carswell E. A., Old L. J., Kassel R. L., Green S., Fiore N., Williamson B. An endotoxin-induced serum factor that causes necrosis of tumors. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3666–3670. doi: 10.1073/pnas.72.9.3666. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Darlington G. J., Wilson D. R., Lachman L. B. Monocyte-conditioned medium, interleukin-1, and tumor necrosis factor stimulate the acute phase response in human hepatoma cells in vitro. J Cell Biol. 1986 Sep;103(3):787–793. doi: 10.1083/jcb.103.3.787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Duncan R., Milburn S. C., Hershey J. W. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F. J Biol Chem. 1987 Jan 5;262(1):380–388. [PubMed] [Google Scholar]
  10. Greengard P. Phosphorylated proteins as physiological effectors. Science. 1978 Jan 13;199(4325):146–152. doi: 10.1126/science.22932. [DOI] [PubMed] [Google Scholar]
  11. Helson L., Green S., Carswell E., Old L. J. Effect of tumour necrosis factor on cultured human melanoma cells. Nature. 1975 Dec 25;258(5537):731–732. doi: 10.1038/258731a0. [DOI] [PubMed] [Google Scholar]
  12. Hepburn A., Demolle D., Boeynaems J. m., Fiers W., Dumont J. E. Rapid phosphorylation of a 27 kDa protein induced by tumor necrosis factor. FEBS Lett. 1988 Jan 25;227(2):175–178. doi: 10.1016/0014-5793(88)80892-5. [DOI] [PubMed] [Google Scholar]
  13. Kaur P., Saklatvala J. Interleukin 1 and tumour necrosis factor increase phosphorylation of fibroblast proteins. FEBS Lett. 1988 Dec 5;241(1-2):6–10. doi: 10.1016/0014-5793(88)81019-6. [DOI] [PubMed] [Google Scholar]
  14. Kohase M., Henriksen-DeStefano D., May L. T., Vilcek J., Sehgal P. B. Induction of beta 2-interferon by tumor necrosis factor: a homeostatic mechanism in the control of cell proliferation. Cell. 1986 Jun 6;45(5):659–666. doi: 10.1016/0092-8674(86)90780-4. [DOI] [PubMed] [Google Scholar]
  15. Kull F. C., Jr, Jacobs S., Cuatrecasas P. Cellular receptor for 125I-labeled tumor necrosis factor: specific binding, affinity labeling, and relationship to sensitivity. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5756–5760. doi: 10.1073/pnas.82.17.5756. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Mackiewicz A., Ganapathi M. K., Schultz D., Samols D., Reese J., Kushner I. Regulation of rabbit acute phase protein biosynthesis by monokines. Biochem J. 1988 Aug 1;253(3):851–857. doi: 10.1042/bj2530851. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Munker R., Gasson J., Ogawa M., Koeffler H. P. Recombinant human TNF induces production of granulocyte-monocyte colony-stimulating factor. Nature. 1986 Sep 4;323(6083):79–82. doi: 10.1038/323079a0. [DOI] [PubMed] [Google Scholar]
  19. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  20. Old L. J. Tumor necrosis factor (TNF). Science. 1985 Nov 8;230(4726):630–632. doi: 10.1126/science.2413547. [DOI] [PubMed] [Google Scholar]
  21. Schütze S., Scheurich P., Pfizenmaier K., Krönke M. Tumor necrosis factor signal transduction. Tissue-specific serine phosphorylation of a 26-kDa cytosolic protein. J Biol Chem. 1989 Feb 25;264(6):3562–3567. [PubMed] [Google Scholar]
  22. Sonenberg N. Cap-binding proteins of eukaryotic messenger RNA: functions in initiation and control of translation. Prog Nucleic Acid Res Mol Biol. 1988;35:173–207. doi: 10.1016/s0079-6603(08)60614-5. [DOI] [PubMed] [Google Scholar]
  23. Sugarman B. J., Aggarwal B. B., Hass P. E., Figari I. S., Palladino M. A., Jr, Shepard H. M. Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro. Science. 1985 Nov 22;230(4728):943–945. doi: 10.1126/science.3933111. [DOI] [PubMed] [Google Scholar]
  24. Torti F. M., Dieckmann B., Beutler B., Cerami A., Ringold G. M. A macrophage factor inhibits adipocyte gene expression: an in vitro model of cachexia. Science. 1985 Aug 30;229(4716):867–869. doi: 10.1126/science.3839597. [DOI] [PubMed] [Google Scholar]
  25. Vilcek J., Palombella V. J., Henriksen-DeStefano D., Swenson C., Feinman R., Hirai M., Tsujimoto M. Fibroblast growth enhancing activity of tumor necrosis factor and its relationship to other polypeptide growth factors. J Exp Med. 1986 Mar 1;163(3):632–643. doi: 10.1084/jem.163.3.632. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Webb N. R., Chari R. V., DePillis G., Kozarich J. W., Rhoads R. E. Purification of the messenger RNA cap-binding protein using a new affinity medium. Biochemistry. 1984 Jan 17;23(2):177–181. doi: 10.1021/bi00297a001. [DOI] [PubMed] [Google Scholar]
  27. Yamada K., Lipson K. E., Marino M. W., Donner D. B. Effect of growth hormone on protein phosphorylation in isolated rat hepatocytes. Biochemistry. 1987 Feb 10;26(3):715–721. doi: 10.1021/bi00377a009. [DOI] [PubMed] [Google Scholar]

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