Abstract
Inflammation may be acute or chronic, and may occur as a primary event or secondary to another disease process. Common to all forms of inflammation is endothelial injury followed by recruitment of phagocytes and immunocytes. Carbohydrates are key to the ensuing cellular response. Sialyl-Lex has been recognized as a critical cell surface ligand in inflammatory reactions since it can bind to selectins that participate in early leukocyte-endothelial interactions1 and may also participate in integrin-mediated interactions. E-selectin is induced on endothelial cells in a variety of acute inflammatory conditions such as tonsillitis, appendicitis and delayed hypersensitivity reactions and its appearance correlates with the extravasation of neutrophils. P-selectin is expressed in Grave’s disease and rheumatoid arthritits.
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
Welply JK, Keene JL, Schmuke JJ et al. Selectins as potential targets of therapeutic intervention in inflammatory diseases. Biochim Biophys Acta 1994; 1197: 215–226.
Etzioni A, Frydman M, Pollack S et al. Brief report:recurrent severe infections caused by a novel leukocyte adhesion deficiency. New Eng J Med 1992; 327: 1789–1792.
von Andrian UH, Berger EM, Ramezani L et al. In vivo behavior of neutrophils from two patients with distinct inherited leukocyte adhesion deficiency syndrome. J Clin Invest 1993; 91: 2893–2897.
Stocks SC, Hopwood D, Sanders DSA et al. The expression of Lewisx on carcinoembryonic antigen (CEA)-related glycoproteins of normal and inflamed oesophageal squamous mucosa. Glycosyl Dis 1994; 1: 279–286.
van Dijk W, Havenaar EC, Brinkman-van der Linden ECM. al-Acid glycoprotein (orosomucoid):pathophysiological changes in glycosylation in relation to its function. Glyconconj J 1995; 12: 227–233.
Sarkar M, Moorkerjea S. Effect of dexamethasone on the synthesis of dolichollinked saccharides and glycoproteins in hepatocytes prepared from control and inflamed rats. Biochem J 1985; 227: 675–682.
Mulligan MS, Lowe JB, Larsen RD et al. Protected effects of sialylated oligosaccharides in immune complex-induced acute lung injury. J Exp Med 1993; 178: 623–631.
Skurk C, Buerke M, Guo J-P et al. Sialyl Lewisx-containing oligosaccharide exerts beneficial effects in murine traumatic shock. Am J Physiol 1994; 267: H2124–2131.
Bazzoni G, Nunez AB, Mascellani G et al. Effect of heparin, dermatan sulfate and related oligo-derivatives on human polymor-phonuclear functions. J Lab Clin Med 1993; 121: 268–275.
Arfors K, Ley K. Sulfated polysaccharides in inflammation. J Lab Clin Med 1993; 121: 201–202.
Slomiany BL, Murty VLN, Piotrowski J et al. Glycosulfatase activity of Helicobacter pylori toward gastric mucin. Biochem Biophys Res Comm 1992; 183: 506–513.
Slomiany BL, Murty VLN, Piotrowski J et al. Glycosulfatase activity of Porphyromonas gingivalis, a bacterium associated with peridontal disease. Biochem Mol Biol Int 1993; 29: 973–980.
Parekh RB, Dwek RA, Sutton BJ et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 1985; 316: 452–457.
Tsuchiya N, Endo T, Matsuta K et al. Effects of galactose depletion from oligosaccharide chains on immunological activities of human IgG. J Rheumatol 1989; 16: 285–290.
Malhotra R, Wormald MR, Rudd PM et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nature Med 1995; 1: 237–243.
Furukawa K, Kobata A. IgG galactosylation-its biological significance and pathology. Mol Immun 1991; 28: 1333–1340.
Rademacher TW, Williams P, Dwek RA. Agalactosyl glycoforms of IgG autoantibodies are pathogenic. Proc Natl Acad Sci USA 1994; 91: 6123–6127.
Jones MG, Dilly SA, Bond A et al. Changes in the glycosylation of IgG in the collagen-induced model of arthritis. Glycosyl Dis 1994; 1: 105–110.
Gleeson PA. Glycoconjugates in autoimmunity. Biochim Biophys Acta 1994; 1197: 237–255.
Allen D, Connolly N, Biggart J. Mucin profiles in ulcerative colitis with dysplasia and carcinoma. Histopathology 1988; 13: 413–424.
Jacobs LR, Huber PW. Regional distribution and alterations of lectin binding to colorectal mucin in mucosal biopsies from control and subjects with inflammatory bowel disease. J Clin Invest 1985; 75: 112–118.
Clamp JR, Fraser G, Read AE. Study of the carbohydrate content of mucus glycoproteins from normal and diseased colons. Clin Sci 1981; 61: 229–234.
Raouf AH, Tsai HH, Parker N et al. Sulphation of colonic and rectal mucin in inflammatory bowel disease:reduced sulphation of rectal mucus in ulcerative colitis. Clin Sci 1992; 83: 623–626.
Roberton A, McKenzie C, Sharfe N et al. A glycosulfatase that removes sulfate from mucus glycoprotein. Biochem J 1993; 293: 683–689.
Rhodes J, Black R, Gallimore R et al. Histochemical demonstration of desialation and desulfation of normal and inflammatory bowel disease rectal mucus by fecal extracts. Gut 1985; 26: 1312–1318.
Morita H, Kettlewell MGW, Jewell DP et al. Glycosylation and sulphation of colonic mucus glycoproteins in patients with ulcerative colitis and in healthy subjects. Gut 1993; 34: 926–932.
Boland CR, Lance P, Levin B et al. Abnormal goblet cell glycoconjugates in rectal biopsies associated with an increased risk of neoplasia in patients with ulcerative colitis:early results of a prospective study. Gut 1984; 25: 1364–1371.
Kim YS, Byrd JC. Ulcerative colitis:a specific mucin defect? Gastroenterology 1984; 87: 1193–1195.
Kim YS, Isaacs R. Glycoprotein metabolism in inflammatory and neoplastic diseases of the human colon. Cancer Res 1975; 35: 2092–2097.
Rankin BJ, Srivastava ED, Record CO et al. Patients with ulcerative colitis have reduced mucin polymer content in the adherent colonic mucus gel. Biochem Soc Trans 1995; 23: 1045.
Parker N, Tsai HH, Ryder SD et al. Increased rate of sialylation of colonic mucin by cultured ulcerative colitis mucosal ex-plants. Digestion 1995; 56: 52–56.
McMahon RFT, Jones CJP, Dutt S et al. Altered oligo-saccharide expression in ulcerative colitis with increasing grades of inflammation. Glycosyl Dis 1994; 1: 235–245.
Fenger C, Filipe MI. Mucin histochemistry of the anal canal epithelium. Studies of 38 normal anal mucosa and mucosa adjacent to carcinoma. Histochem J 1981; 13: 921–930.
Itzkowitz SH, Young E, Dubois D et al. Sialosyl-Tn antigen is prevalent and precedes dysplasia in ulcerative colitis:a retrospective case-control study. Gastroenterol 1996; 110: 694–704.
Reid PE, Culling CFA, Dunn WL et al. Chemical and histochemical study of normal and diseased human gastrointestinal tract. A comparison between histologically normal colon, colonic tumors, ulcerative 40. colitis and diverticular disease of the colon. Histochem J 1984; 16: 235–251.
Sasaki M, Kono N, Nakanuma Y. Membranous expression of Lewis Y antigen in clus- 41. tered hepatocytes in chronic viral, autoimmune, and alcoholic liver diseases but not in biliary diseases. Mod Path 1994; 7: 339–346.
Kim YS, Perdomo J, Whitehead JS et al., Glycosyltransferases in human blood. II. Study of serum galactosyltransferase and N- acetylgalactosaminyltransferase in patients with liver diseases. J Clin Invest 1972; 51: 2033–2039.
Lammers G, Jamieson JC. The role of a cathepsin D-like activity in the release of Ga1131–4G1cNAc a2–6-sialyltransferase from rat liver Golgi membranes during the acute-phase response. Biochem J 1988; 256: 623–631.
Lammers G, Jamieson JC. Cathepsin D-like activity in the release of Galbetal4G1cNAca2–6sialyltransferase from mouse and guinea pig liver Golgi membranes during the acute phase response. J Comp Biochem Physiol 1990; 95: 327–334.
Fraser IH, Coolbear T, Sakar M. Increase of sialytransferase activity in the serum and liver of inflamed rats. Biochim Biophys Acta 1984; 799: 102–105.
Kaplan HA, Woloski BMRNJ, Hellman M et al. Studies on the effect of inflammation on rat liver and serum sialyltransferase. Evidence that inflammation causes release of Galß1-*4G1cNAc a2–6 sialyltransferase from liver. J Biol Chem 1983; 258: 11505–11509.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Brockhausen, I., Kuhns, W. (1997). Inflammatory Diseases. In: Glycoproteins and Human Disease. Medical Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-21960-7_15
Download citation
DOI: https://doi.org/10.1007/978-3-662-21960-7_15
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-21962-1
Online ISBN: 978-3-662-21960-7
eBook Packages: Springer Book Archive