Abstract
Post-translational covalent modifications are powerful tools to regulate protein functions. Modifications may occur e. g. via acylation, hydroxylation, methylation, thiolation, glycosylation, ADP (adenosine diphosphate) ribosylation and phosphorylation. Among these modifications, protein phosphorylation seems to be a principal mechanism involved in signal transduction processes. There is increasing evidence that other modifications like mono-ADP-ribosylation also contribute to signaling events (Wang et al. 1996; Vedia et al. 1992). Mono-ADP-ribosylation catalyzed by ADP-ribosyltransferases involves the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD)+ to a specific amino acid in a target protein while the nicotinamide moiety is released. The best understood ADP-ribosyltransferases are bacterial toxins including cholera and pertussis toxin that interfere with signal transduction in human host cells by ADP-ribosylating regulatory G-proteins.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Dong Z, Qi X, Fidler IJ (1993) Tyrosine phosphorylation of mitogen activated protein kinases is necessary for activation of murine macrophages and synthetic bacterial products. J Exp Med 177: 1071 – 1077
Gallay P, Jongeneel CV, Barras C, Burnier M, Baumgartner JD, Glauser MP, Heu- mann D (1993) Short time exposure to lipopolysaccharide is sufficient to activate human monocytes. J Immunol 150: 5086 – 5093
Han J, Lee JD, Bibbs L, Ulevitch RJ (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265: 808 – 811
Hauschildt S, Scheipers P, Bessler WG (1991) Inhibitors of poly (ADP–ribose) polymerase suppress lipopolysaccharide-induced nitrite formation in macrophages. Biochem Biophys Res Commun 179: 865 – 871
Hauschildt S, Schwarz C, Heine H, Ulmer AJ, Flad HD, Rietschel ET, Jensen ON, Mann M (1997) Actin: a target of lipopolysaccharide–induced phosphorylation in human monocytes. Biochem Biophys Res Commun 241: 670 – 674
Heine H, Ulmer AJ, Flad HD, Hauschildt S (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
Kang YH, Dwivedi RS, Lee CH (1990) Ultrastructural and immunocytochemical study of the uptake and distribution of bacterial lipopolysaccharide in human monocytes. J Leuk Biol 43: 316 – 332
Kovach NL, Yee E, Munford RS, Raetz CRH, Harlan JM (1990) Lipid IVA inhibits synthesis and release of tumor necrosis factor induced by lipopolysaccharide in human whole blood ex vivo. J Exp Med 172: 77 – 84
Luchi M, Munford RS (1993) Binding, internalization, and deacylation of bacterial lipopolysaccharide by human neutrophils. J Immunol 151: 959 – 969
Mc Manon KK, Piron KJ, Ha VT, Fullerton AT (1993) Developmental and biochemical characteristics of the cardiac membrane-bound arginine-specific mono ADP- ribosyltransferase. Biochem J 293: 789 – 793
Novogrodsky A, Vanichkin A, Patya M, Gazit A, Osherov N, Levitzki A (1994) Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors. Science 27: 1319 – 1322
Rankin PW, Jacobson EL, Benjamin RC, Moss J, Jacobson MK (1989) Quantitative studies of inhibitors of ADP-ribosylation in vitro and in vivo. J Biol Chem 264: 4312 – 4317
Schuman EM, Meffert MK, Schulman H, Madison DV (1994) An ADP ribosyltrans- ferase as a potential target for nitric oxide action in hippocampal long–term potential. Proc Natl Acad Sci USA 91: 11958 – 11962
Sung S, Walters JA, Fu SM (1992) Stimulation of tumor necrosis factor alpha production in human monocytes by inhibitors of protein phosphatase 1 and 2A. J Exp Med 176: 897 – 901
Tsuchiya M, Hara N, Yamada K, Osago H, Shimoyama M (1994) Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells. J Biol Chem 269: 27451 – 27457
Ulevitch RJ, Tobias PS (1994) Recognition of endotoxin by cells leading to transmembrane signaling. Curr Opin Immunol 6: 125 – 130
Vedia ML, Mc Donald LB, Reep B, Brüne B, Di Silvio M, Billiar TR, Lapetina EG (1992) Nitric oxide induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogeneous ADP-ribosylation. J Biol Chem 267: 24929 – 24932
Wang J, Nemoto E, Dennert G (1996) Regulation of CTL by ecto-nicotinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein. J Immunol 156: 2819 – 2827
Weinstein SL, Gold MR, De Franco AL (1991) Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages. Proc Natl Acad Sci USA 88: 4148 – 4152
Weinstein SL, Sanghera JS, Lemke K, DeFranco AL, Pelech SL (1992) Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen activated protein kinases in macrophages. J Biol Chem 267: 14955 – 14962
Zolkiewska A, Moss J (1993) Integrin a7 as substrate for a glycosylphosphatidylinos- itol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J Biol Chem 268: 25273 – 25276
Zolkiewska A, Nightingale MS, Moss J (1992) Molecular characterization of NAD: arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc Natl Acad Sci USA 89: 11352 – 11356
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Hauschildt, S., Heine, H. (1999). Intracellular Protein Modification and Signal Transduction in Response to Lipopolysaccharide. In: Eibl, M.M., Huber, C., Peter, H.H., Wahn, U. (eds) Symposium in Immunology VIII. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59947-7_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-59947-7_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-64722-5
Online ISBN: 978-3-642-59947-7
eBook Packages: Springer Book Archive