Abstract
Tissue injury, infection, various inflamatory processes or tumor growth cause the activation of a large number of cells responsible for host protection (1). These cells secrete factors which in turn have the ability to stimulate effector cells. One group of these factors is referred to as cytokines. The cytokines involved in stimulation of anti or pro-inflammatory mechanisms are more specifically termed inflammatory cytokines. There is increasing evidence demonstrating that biological effects of these factors do not result from an action of a single cytokine but rather result from coordinated cooperation of a number of cytokines and other factors such as glucocorticoids (2).
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
Kushner, I., Mackiewicz A., 1993, The Acute Phase Response; An Overview, In: Acute Phase Proteins: Molecular Biology, Biochemistry and Clinical Applications, Mackiewicz, A., Kushner, I., Baumann, H., (eds.). CRC Press, Boca Raton 1993, pp. 4–19.
Mackiewicz, A., Speroff, T., Ganapathi, M.K., Kushner, I., 1991, Effects of cytokine combinations on acute phase protein production in two human hepatoma cell lines, J. Immunol. 146:3032–3037,
Baumann, H., Held, W.A., 1981, Biosynthesis and hormone regulated expression of secretory glycoproteins in rat liver and hepatoma cells. Effects of glucocorticoids and inflammation, J. Biol. Chem. 256:10145–10151.
Van Dijk, W., Turner, G.A., Mackiewicz, A., 1994, Changes in glycosylation of acute phase proteins in health and disease: occurrence, regulation and function, Glycosyl. Dis. 1:5–14.
Mackiewicz, A., Kushner, I., 1989, Affinity electrophoresis for studies of mechanisms regulating glycosylation of plasma proteins, Electrophoresis 10:830–835.
Nicollet, I., Lebreton, J.P., Fontaine, M., Hiron, M., 1981, Evidence for α-1-acid glycoprotein populations of different pI values after Concanavalin A affinity chromatography: study of their evolution during inflammation in man, Biochim. Biophys. Acta 668:235–245.
Raynes, J., 1982, Variations in the relative proportions of microheterogenious forms of plasma glycoproteins in pregnancy and disease, Biomedicine 36:77–86.
Mackiewicz, A., Marcinkowska-Pieta, R., Ballou, S., Mackiewicz, S., Kushner, I., 1987, Microheterogeneity of α1-acid glycoprotein in the detection of intercurrent infection in systemic lupus erythematosus, Arthritis Rheum. 30:513–518.
Pawlowski, T., Mackiewicz, S., Mackiewicz A., 1989, Microheterogeneity of α1-acid glycoprotein in the detection of intercurrent infection in rheumatoid arthritis, Arthritis Rheum. 32:347–351.
Pos, O., Van der Stelt, M.E., Wolbink, G.-J., Nijsten, M.W.N., Van der Tempel, G.L., Van Dijk, W., 1990, Changes in the serum concentration and the glycosylation of human α1-acid glycoprotein and α1-protease inhibitor in severely burned persons: relation to interleukin-6 levels, Clin. Exp. Immunol. 82:579–582,
Fassbender, K., Zimmerli, W., Kissling, R., Sobieska, M., Aeschlimann, A., Kellner, M., Muller, W., 1991, Glycosylation of α1-acid glycoprotein in relation to duration of disease in acute and chronic infection and inflammation, Clin. Chim. Acta 203:315–321.
Breborowicz, J., Mackiewicz, A., (eds,), 1992, Affinity Electrophoresis: Principles and Application, CRC Press, Boca Raton 1992.
Debray, H., Montreuil, J., 1993, Specificity of lectins toward oligosaccharidic sequences belonging to N-and O-glycoproteins, In: Acute Phase Proteins: Molecular Biology, Biochemistry and Clinical Applications, Mackiewicz, A., Kushner, I., Baumann, H., (eds.), CRC Press, Boca Raton 1993, pp. 4–19.
Bierhuizen, M., De Wit, M.,Govers, C., Ferwerda, W., Koeleman, C., Pos, O., Van Dijk W., 1988, Glycosylation of three molecular forms of human α1-acid glycoprotein having different interactions with Concanavalin A. Variations in the occurrence of di-, tri-, and tetraantennary glycans and the degree of sialylation, Eur. J. Biochem. 175:387–394,
Mackiewicz, A., Ganapathi, M.K., Schultz, D., Kushner, I., 1987, Monokines regulate glycosylation of acute phase proteins, J. Exp. Med. 166:253–258,
Mackiewicz, A., Schultz, D., Mathison, J., Ganapathi, M.K., Kushner, I., 1989, Effect of cytokines on glycosylation of acute phase proteins in human hepatoma cell lines, Clin. Exp. Immunol. 75:70–75,
Mackiewicz, A., Kushner, I., 1989, Interferon ß2/BSF/IL-6 effects glycosylation of acute phase proteins in human hepatoma cell lines, Scand. J. Immunol. 29:265–271.
Mackiewicz, A., Kushner, I., 1990, Transforming growth factor ß1 influences glycosylation of α1-proteinase inhibitor in human hepatoma cell lines, Inflammation 14:485–495.
Mackiewicz, A., Dewey, M.J., Berger, F., Baumann, H., 1991, Acute phase mediated changes in glycosylation of rat α1-acid glycoprotein in transgenic mice, Glycobiology. 1:265– 269.
Van Dijk, W., Pos, O., Van der Stelt, M.E., Moshage, H.J., Yap, S.-H., Dente, L., Baumann, P., Eap, C.B., 1991, Inflammation-induced changes in expression and glycosylation of genetic variants of α1-acid glycoprotein. Studies with human sera, primary cultures of human hepatocytes and transgenic mice, Biochem. J. 276:343–347.
Pos, O., Moshage, H.J., Yap, S.H., Schnieders, J.P.M., Aarden, L.A., Van Gool, J., Boers, W., Brugman, A.M., Van Dijk, W., 1989, Effects of monocytic products, recombinant interleukin-1, and recombinant interleukin-6 on glycosylation of α1-acid glycoprotein; studies with primary human hepatocyte cultures and rats, Inflammation 13:415–427.
Pos, O., Van Dijk, W., Ladiges, N., Linthorst, C., Sala, M., Van Tiel, D., Boers, D., 1988, Glycosylation of four acute-phase glycoproteins secreted by rat liver cells in vivo and in vitro: effects of inflammation and dexamethasone, Eur. J. Cell. Biol. 46:121–128.
Mackiewicz, A., Laciak, M., Górny, A., Baumann, H., 1993, Leukemia inhibitory factor, interferon gamma and dexamethasone regulate N-glycoslyation of α1-protease inhibitor in human hepatoma cells, Eur. J. Cell Biol. 60:331–336.
Mackiewicz, A., Rose-John, S., Schooltink, H., Laciak, M., Górny, A., Heinrich, P.C., 1992, Soluble human interleukin-6-receptor modulates interelukin-6-dependent N-glycosylation of α1-proteinase inhibitor secreted by Hep G2 cells, FEBS Lett. 306:257–261.
Rose-John, S., Schooltink, H., Lenz, D., Hipp, E., Dufhues, G., Schmitz, H., Schiel, X., Hirano, T., Kishimoto, T., Heinrich, P.C., 1990, Studies on the structure and regulation of the human hepatic interleukin-6 receptor, Eur. J. Biochem. 190:79–83.
Schachter, H., Narasimhan, S., Gleeson, P., Vella, G., 1983, Control of branching during the biosynthesis of asparagine-linked oligosaccharide, Can. J. Biochem. Cell Biol. 16:1049–1066.
Wang, X.C., O’Hanlon, T.P., Lau, J.T.Y., 1989, Regulation of ß-galactoside α2,6-sialyltransferase gene expression by dexamethasone, J. Biol. Chem. 264:1854–1860.
Woloski, B.M., Fuller, G.M., Jamieson, J.C., Gospodarek, E., 1986, Studies on the effect of the hepatocyte-stimulating factor on galactose-ß-4-N-acetylglucosamine α2→6-sialyltransferase in cultured hepatocytes, Biochim. Biophys. Acta 885:185–191.
Nakao, H., Nishikawa, A., Karasuno, T., Nishiura, T., Iida, M., Kanayama, Y., Yonezawa, T., Tarui, S., Tanigushi, N., 1990, Modulation of N-acetyl-glucosaminyltransferase III, IV, and V activates and alteration of the surface oligosaccharide structure of a myeloma cell line by interleukin 6, Biochem. Biophys. Res. Comm. 172:1260–1266.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Gryska, K. et al. (1995). Inflammatory Cytokines Controlling Branching of N-Heteroglycans of Acute Phase Protein. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_26
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1885-3_26
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5768-1
Online ISBN: 978-1-4615-1885-3
eBook Packages: Springer Book Archive