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Signal Paths and Regulation of Superoxide, Eicosanoid and Cytokine Formation in Macrophages of Rat Liver

  • Karl Decker
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 283)

Abstract

Biological signal molecules mediate information between different cells. They are usually elicited by stimuli that include toxins, stress factors, nerve stimulation and metabolic deficiences. Like neurotransmitters they are in most cases shortlived and narrow-(or medium-)-ranged; unlike neurotransmitters and some hormones they are not stored within the producer cells. Some of them also differ from neurotransmitters and hormones in that they are autostimulatory, i.e. eliciting the same cells which produce them. Signal molecules show a high to medium specificity with respect to the elicitation of synthesis and secretion, to producer and target cells and to the mechanism of action.

Keywords

Arachidonic Acid Kupffer Cell Newcastle Disease Virus Phorbol Ester Sinusoidal Endothelial Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Aarden, L., Lansdorp, P. and De Groot, E. (1985). A growth factor for B cell hybridomas produced by human monocytes. Lymphokines 10, 175–185.Google Scholar
  2. Adams, D.O. and Hamilton, T.A. (1984). The cell biology of macrophage activation. Ann. Rev. Immunol. 2, 283–318.CrossRefGoogle Scholar
  3. Andus, T., Geiger, T., Hirano, T., Kishimoto, T., Tran-Thi, T.A., Decker, K. and Heinrich, P.C. (1988). Regulation of synthesis and secretion of major rat acute-phase proteins by recombinant human interleukin-6 (BSF-2/IL-6) in hepatocyte primary cultures. Eur. J. Biochem. 173, 287–293.CrossRefPubMedGoogle Scholar
  4. Bhatnagar, R., Schirmer, R., Ernst, M. and Decker, K. (1981). Superoxide release by zymosan-stimulated rat Kupffer cells in vitro. Eur. J. Biochem. 119, 171–175.CrossRefPubMedGoogle Scholar
  5. Bhatnagar, R., Schade, U., Rietschel, T.E. and Decker, K. (1982). Involvement of prostaglandin E and cyclic adenosine 3’,5’-monophosphate in lipopolysaccharidestimulated collagenase release by rat Kupffer cells. Eur. J. Biochem. 125, 125–130.Google Scholar
  6. Birmelin, M. and Decker, K. (1983). Ca2+ flux as an initial event in phagocytosis by rat Kupffer cells. Eur. J. Biochem. 131, 539–543.CrossRefGoogle Scholar
  7. Birmelin, M. and Decker, K. (1984). Synthesis of prostanoids and cyclic nucleotides by phagocytosing rat Kupffer cells. Eur. J. Biochem. 142, 219–225.CrossRefPubMedGoogle Scholar
  8. Brouwer, A., Barelds, R.J. and Knook, D.L. (1984). Centrifugal separation of mammalian cells. In Centrifugation, a Practical Approach ( D.Rickwood, Ed.) pp. 183–218. IRL Press, Oxford, UK.Google Scholar
  9. Busam,K., Bauer, T., Bauer, J., Gerok, W. and Decker, K. (1989). Regulation of interleukin-6 secretion by rat Kupffer cells. J.Hepatol. 9 (suppl.1), S 13CrossRefGoogle Scholar
  10. Decker, K. (1987). Eicosanoids as signal molecules between hepatocytes and sinusoidal cells. In Modulation of liver cell expression ( W. Reutter, H. Popper, I.M. Arias, P.C. Heinrich, D. Keppler and L. Landmann, Eds.) pp. 397–409. MTP Press, Lancaster, UK.Google Scholar
  11. Decker, K. and Dieter, P. (1987). The stimulus-activated Na+/14+ exchange in macrophages, neutrophils and platelets. In pH Homeostasis, Mechanism and Control ( D. Häussinger, Ed.) pp. 79–96, Academic Press, London, UK.Google Scholar
  12. Decker, T., Lohmann-Matthes, M.-L., Karck, U., Peters, T. and Decker, K. (1989). Cytotoxicity, tumor necrosis factor and prostaglandin release after stimulation: an interspecies comparison of rat Kupffer cells, murine Kupffer cells and murine inflammatory liver macrophages. J. Leukocyte Biol. 45, 139–147.PubMedGoogle Scholar
  13. Dieter, P., Schulze-Specking, A. and Decker, K. (1986). Differential inhibition of prostaglandin and superoxide production by dexamethasone in primary cultures of rat Kupffer cells. Eur. J. Biochem. 159, 451–457.CrossRefPubMedGoogle Scholar
  14. Dieter, P., Altin, J.G., Decker, K. and Bygrave, F.L. (1987a). Possible involvement of eicosanoids in the zymosan-and arachidonic acid-induced oxygen uptake, glycogenolysis and Ca2+ mobilisation in the perfused rat liver. Eur. J. Biochem. 165, 455–460.Google Scholar
  15. Dieter, P., Schulze-Specking, A., Karck, U. and Decker, K. (1987b). Prostaglandin release but not superoxide production by rat Kupffer cells in vitro depends on Neill+ exchange. Eur. J. Biochem. 170, 201–206.CrossRefPubMedGoogle Scholar
  16. Dieter, P., Schulze-Specking, A. and Decker, K. (1988). Ca2+ requirement of prostanoid but not of superoxide production by rat Kupffer cells. Eur. J. Biochem. 177, 61–67.CrossRefPubMedGoogle Scholar
  17. Dieter, P., Peters, T., Schulze-Specking, A. and Decker, K. (1989a). Independent regulation of thromboxane and prostaglandin synthesis in liver macrophages. Biochem. Pharmacol. 38, 1577–1581.CrossRefPubMedGoogle Scholar
  18. Dieter, P., Schulze-Specking, A. and Decker, K. (1989b). Signal transduction during stimulus-induced synthesis of prostanoids and superoxide in liver macrophages. In Cells or the Hepatic Sinusoid. ( E. Wisse, D.L. Knook and K. Decker, Eds.) Vol. II,pp. 190–193, Kupffer Cell Foundation, Rijswijk, The Netherlands.Google Scholar
  19. Dieter, P., Schulze-Specking, A. and Decker, K. (1989b). Signal transduction during stimulus-induced synthesis of prostanoids and superoxide in liver macrophages. In Cells or the Hepatic Sinusoid. ( E. Wisse, D.L. Knook and K. Decker, Eds.) Vol. II,pp. 190–193, Kupffer Cell Foundation, Rijswijk, The Netherlands.Google Scholar
  20. Eyhorn, S., Schlayer, H.-J., Henninger, H.P., Dieter, P., Hermann, R., Woort-Menker, M., Becker, H., Schaefer, H.E. and Decker, K. (1988). Rat hepatic sinusoidal endothelial cells in monolayer culture. Biochemical and ultrastructural characteristics. J. Hepatol. 6, 23–35.CrossRefPubMedGoogle Scholar
  21. Grewe, M., Schulze-Specking, A. and Decker, K. (1989). Prostaglandin H2 synthase of rat Kupffer cells. In Cells of the Hepatic Sinusoid ( E. Wisse, D.L. Knook and K. Decker, Eds.) Vol. II, pp. 206–207, Kupffer Cell Foundation, Rijswijk, The Netherlands.Google Scholar
  22. Häussinger, D., Stehle, T., Tran-Thi, T.-A., Decker, K. and Gerok, W. (1987). Prostaglandin responses in isolated perfused rat liver: Ca2+ and K+ fluxes, hemodynamics and metabolic effects. Biol. Chem. Hoppe-Seyler 368, 1509–1513.CrossRefPubMedGoogle Scholar
  23. Häussinger, D. (1989). Regulation of hepatic metabolism by extracellular nucleotides and eicosanoids. The role of cell heterogeneity. J. Hepatol. 8, 259–266.CrossRefPubMedGoogle Scholar
  24. Irvine, R.F. (1982). How is the level of free arachidonic acid controlled in mammalian cells? Biochem. J. 204, 3–16.PubMedGoogle Scholar
  25. Karck, U., Peters, T. and Decker, K. (1988). The release of tumor necrosis factor from endotoxin-stimulated rat Kupffer cells is regulated by prostaglandin E2 and dexamethasone. J. Hepatol. 7, 352–361.CrossRefPubMedGoogle Scholar
  26. Krause, H., Dieter, P., Schulze-Specking, A. and Decker, K. (1989). Regulation of phospholipase A2 in rat Kupffer cells. J. Hepatol. 9, Suppl. 1, S 178.CrossRefGoogle Scholar
  27. Latocha, G., Dieter, P.,Schulze-Specking, A. and Decker, K. (1989). Fe receptors mediate prostaglandin and superoxide synthesis in cultured rat Kupffer cells. Biol. Chem. Hoppe-Seyler 370, 1055–1061.CrossRefPubMedGoogle Scholar
  28. Nakagawara, A. and Minakami, S. (1975). Generation of superoxide by leukocytes treated with cytochalasin E. Biochem. Biophys. Res. Comm. 64, 760–767.CrossRefGoogle Scholar
  29. Palmer, R.M., Ferrige, A.G. and Moncada, S. (1987). Nitric oxide accounts for the biological activity of endothelium-derived relaxing factor. Nature (London) 327, 524–526.CrossRefGoogle Scholar
  30. Pestka, S. and Langer, J.A. (1987). Interferons and their action. Ann. Rev. Biochem. 15, 727–777.CrossRefGoogle Scholar
  31. Peters, T. and Decker, K. (1989). Recombinant mouse tumor necrosis factor alpha induces prostaglandin E2 synthesis in rat Kupffer cells. In Cells of the Hepatic Sinusoid ( E. Wisse, D.L. Knook and K. Decker, Eds.) Vol. II, pp. 182–185, Kupffer Cell Foundation, Rijswijk, The Netherlands.Google Scholar
  32. Pober, J.S., Gimbrone, Jr. M.A., Lapierre, L.A., Mendrick, D.L., Fiers, W., Rothlein, R. and Springer, T.A. (1986). Overlapping patterns of activation of human endothelial cells by interleukin 1, tumor necrosis factor and immune interferon. J. Immunol. 137, 1893–1896.PubMedGoogle Scholar
  33. Sakagami, Y., Mizoguchi, Y., Seki, S., Kobayashi, K., Morisawa, S.and Yamamoto, S. (1988). Release of peptide leukotrienes from rat Kupffer cells. Biochem. Biophys. Res. Commun. 156, 217–221.CrossRefPubMedGoogle Scholar
  34. Schlayer,H.-J., Karck, U., Ganter, U., Hermann, R. and Decker, K. (1987). Enhancement of neutrophil adherence to isolated rat liver sinusoidal endothelial cells by supernatants of lipopolysaccharide-activated monocytes–role of tumor necrosis factor. J. Hepatol. 5, 311–321.CrossRefPubMedGoogle Scholar
  35. Schlayer, H.-J., Laaf, H., Peters, T., Woort-Menker, M., Estler, C., Karck, U., Schaefer, H.E. and Decker, K. (1988). Involvement of tumor necrosis factor in endotoxin-triggered neutrophil adherence to sinusoidal endothelial cells of mouse liver and its modulation in acute phase. J. Hepatol. 7, 239–249.CrossRefPubMedGoogle Scholar
  36. Shirahama, M., Ishibashi, H., Tsuchiya, Y., Kurokawa, S., Hayashida, K., Okumura, Y. and Niho, Y. (1988). Kupffer cells may autoregulate interleukin 1 production by producing interleukin 1 inhibitor and prostaglandin E2. Scand. J. Immunol. 28, 719–725.Google Scholar
  37. Tran-Thi, T.-A., Gyufko, K., Henninger, H., Busse, R. and Decker, K. (1987). Studies on synthesis and degradation of eicosanoids by rat hepatocytes in primary culture. J. Hepatol. 5, 322–331.CrossRefPubMedGoogle Scholar
  38. Tran-Thi, T.-A., Gyufko, K., Häussinger, D. and Decker, K. (1988). Net prostaglandin release by perfused rat liver after stimulation with phorbol 12-myristate 13-acetate. J. Hepatol. 6, 151–157.CrossRefPubMedGoogle Scholar
  39. Zacharchuk, C.M., Drysdale, B.E., Mayer, M.M. and Shin, H.S. (1983). Macrophage-mediated cytotoxicity: role of a soluble macrophage cytotoxic factor similar to lymphotoxin and tumor necrosis factor. Proc. Natl. Acad. Sci. USA 80, 6341–6345.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Karl Decker
    • 1
  1. 1.Institute of BiochemistryAlbert-Ludwigs-UniversityFreiburgFederal Republic of Germany

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