Advertisement

Role of ADP-Ribosylation in Activated Monocytes/Macrophages

  • Sunna Hauschildt
  • Peter Scheipers
  • Wolfgang Bessler
  • Klaus Schwarz
  • Artur Ullmer
  • Hans-Dieter Flad
  • Holger Heine
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 419)

Abstract

Stimulating monocytes/macrophages with bacterial lipopolysaccharide (LPS) results in TNF-α, IL-1, IL-6 and nitrite (NO2 -) formation. Inhibitors of poly(ADP-ribose)polymerase inhibit release of these mediators by preventing mRNA expression indicating that ADP-ribosylation plays a crucial role in the synthesis of these mediators. Furthermore we present evidence that ADP-ribosylation is involved in modifying cellular proteins. In murine macrophages a 33 kDa cytosolic protein could be identified that in response to LPS changed its state of ADP-ribosylation, and in human monocytes we showed that the inhibitor nicotinamide prevents LPS induced phosphorylation of two cytosolic proteins of 36 kDa and 38 kDa (p36/38) LPS. Taken together these data indicate that protein modification by ADP-ribosylation may control cellular processes involved in distinct steps of monocyte/macrophage activation.

Keywords

Human Monocyte Nicotinamide Adenine Dinucleotide Cytosolic Protein Nicotinamide Adenine Dinucleotide Specific Amino Acid Residue 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Hayaishi, O. & K. Ueda eds. 1982. ADP-Ribosylation Reactions: Biology and Medicine. Academic Press, New York.Google Scholar
  2. 2.
    Tanuma, S., K. Kawashima & H. Endo. 1988. Eukaryotic mono(ADP-ribosyl)transferase that ribosylates GTP-binding regulatory Gi protein. J. Biol. Chem. 263: 5485–5489.PubMedGoogle Scholar
  3. 3.
    Molina Y Vedia, L.B. McDonald, B. Reep, B. Brüne, M. Di Silvio, T.R. Billiar & E.G. Lapetina. 1992. Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehy-drogenase inhibits enzymatic activity and increases endogeneous ADP-ribosylation. J. Biol. Chem. 267: 24929–24932.Google Scholar
  4. 4.
    Wang, J., E. Nemoto, A.Y. Kots, H. Kaslow & G. Dennert. 1994. Regulation of cytotoxic T cells by ectonicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI anchored/arginine ADP-ribosyltransferase. J. Immunol., 153: 4048–4058.PubMedGoogle Scholar
  5. 5.
    Hauschildt, S., P. Scheipers & W.G. Bessler. 1991. Inhibitors of poly(ADP-ribose)poly-merase suppress lipopolysaccharide-induced nitrite formation in macrophages. Biochem. Biophys. Res. Commun. 179: 865–871.PubMedCrossRefGoogle Scholar
  6. 6.
    Hauschildt, S., P. Scheipers & W.G. Bessler. 1994. Lipopolysaccharide-induced change of ADP-ribosylation of cytosolic protein in bone marrow derived macrophages. Biochem. J.297: 17–20.PubMedGoogle Scholar
  7. 7.
    Heine, H., A.J. Ulmer, H.D. Flad & S. Hauschildt. 1995. Lipopolysaccharide-induced change of phosphorylation of two cytosolic proteins in human monocytes is prevented by inhibitors of ADP-ribosylation. J. Immunol. 155: 4899–4908.PubMedGoogle Scholar
  8. 8.
    Pellat-Deceunynek, C, J. Wietzerbin & J.C. Drapier. 1994. Nicotinamide inhibits nitric oxide synthase mRNA induction in activated macrophages. Biochem. J. 297: 53–58.Google Scholar
  9. 9.
    Agarwal, S., B.E. Drysdale & H.S. Shin. 1988. Tumor necrosis factor-mediated cytotoxicity involves ADP-ribosylation. J. Immunol. 140: 4187–4192.PubMedGoogle Scholar
  10. 10.
    Schraufstatter, I.U., PA. Hyslop, D.B. Hinshaw, R.G. Spragg, L.A. Sklar & C.G. Cochrane. 1986. Hydrogen peroxid-induced injury of cells and its prevention by inhibitors of poly(ADP-ribose)polymerase. Proc. Natl. Acad. Sci. 83: 4908–4912.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Sunna Hauschildt
    • 1
  • Peter Scheipers
    • 2
  • Wolfgang Bessler
    • 2
  • Klaus Schwarz
    • 1
  • Artur Ullmer
    • 3
  • Hans-Dieter Flad
    • 3
  • Holger Heine
    • 3
  1. 1.Universität Leipzig Institut für Zoologie ImmunbiologieLeipzigGermany
  2. 2.Universität Freiburg Institut für ImmunbiologieFreiburgGermany
  3. 3.Forschungszentrum BorstelBorstelGermany

Personalised recommendations