Role of glycosaminoglycans in inflammation
Purchase on Springer.com
$39.95 / €34.95 / £29.95*
Rent the article at a discountRent now
* Final gross prices may vary according to local VAT.
Glycosaminoglycans (GAGs) are large, polyanionic molecules expressed throughout the body, either in association with cell surfaces and extracellular matrices, or stored within intracellular compartments. The GAG heparin is synthesised by and stored exclusively in mast cells, which are strongly associated with allergy and inflammation and is co-released with histamine upon cellular degranulation. The closely related GAG heparan sulphate is expressed, as part of a proteoglycan, on cell surfaces. Most notably, heparan sulphate is associated with the surfaces of vascular endothelial cells, known to be pivotally involved in the control of inflammatory cell adhesion and extravasation. The physiological role of these molecules is not well understood but evidence suggests that they may be involved in limitation of the inflammatory response and, in particular, regulation of cell adhesion and trafficking.
- Bar-Ner, M., Eldor, A., Wasserman, L., et al. (1987). Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin, Blood 70, 551–557.
- Bartlett, M. R., Underwood, P. A. and Parish, C. R. (1995). Comparative analysis of the ability of leucocytes, endothelial cells and platelets to degrade the subendothelial basement membrane: Evidence for cytokine dependence and detection of a novel sulfatase, Immunol. Cell Biol. 73, 113–124.
- Bârzu, T., Van Rijn, J. L. M. L., Petitou, M., et al. (1986). Endothelial binding sites for heparin. Specificity and role in heparin neutralization, Biochem. J. 238, 847–854.
- Bazzoni, G., Nuñez, A. B., Mascellani, G., et al. (1992). Effect of heparin, dermatan sulfate, and related oligo-derivatives on human polymorphonuclear leukocyte functions, J. Lab. Clin. Med. 121, 268–275.
- Choay, J., Lormeau, J. C., Petitou, M., et al. (1983). Structure activity relationship in heparin: A synthetic pentasaccharidewith high affinity for antithrombin III and eliciting high anti-Xa activity, Biochem. Biophys. Res. Com. 116, 492.
- Damus, P. S., Hicks, M. and Rosenberg, R. D. (1973). Anticoagulant action of heparin, Nature 246, 355–357.
- Diamond, M. S., Alon, R., Parkos, C. A., et al. (1995). Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/ CD18), J. Cell Biol. 130, 1473–1482.
- Dolowitz, D. A. and Dougherty, T. F. (1960). The use of heparin as an anti-inflammatory agent, Laryngoscope 70, 873–874.
- Giuffrè, L., Cy, A.-S., Monai, N., et al. (1997). Monocyte adhesion to activated aortic endothelium: Role of L-selectin and heparan sulfate proteoglycans, J. Cell Biol. 136, 945–956.
- Jaques, L. B. (1979). Heparins —anionic polyelectrolyte drugs, Pharmacol. Rev. 31, 99–167.
- Klein, N. J., Shennan, G. I., Heyderman, R. S., et al. (1992). Alteration in glycosaminoglycan metabolism and surface charge on human umbilical vein endothelial cells induced by cytokines, endotoxin and neutrophils, J. Cell Sci. 102, 821–832.
- Koenig, A., Norgard-Sumnicht, K., Linhardt, R., et al. (1998). Differential interactions of heparin and heparan sulfate glycosaminoglycans with the selectins, J. Clin. Invest. 101, 877–889.
- Kraemer, P. M. (1977). Heparin releases heparan sulfate from the cell surface, Biochem. Biophys. Res. Comm. 78, 1334–1340.
- Lasser, E. C., Lang, J. H., Curd, J. G., et al. (1983). The plasma contact system in atopic asthma, J. Allergy Clin Immunol. 72, 83–88.
- Lasser, E. C., Simon, R. A., Lyon, S. G., et al. (1987). Heparin-like anticoagulants in asthma, Allergy 42, 619–625.
- Lever, R., Hoult, J. R. S. and Page, C. P. (2000). The effects of heparin and related molecules upon the adhesion of human polymorphonuclear leucocytes to vascular endothelium in vitro, Brit. J. Pharmacol. 129, 533–540.
- Ley, K., Cerrito, M. and Arfors, K.-E. (1991). Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules, Amer. J. Physiol. 260, H1667–H1673.
- Lindahl, U., Backstrom, G., Thunberg, L., et al. (1980). Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin, Proc. Natl. Acad. Sci. USA 77, 6551–6555.
- Lindahl, U., Thunberg, L., Bäckström, G., et al. (1984). Extension and structural variability of the antithrombin-bindingsequence in heparin, J. Biol. Chem. 259, 12368–12376.
- Murch, S. H., MacDonald, T. T., Walker-Smith, J. A., et al. (1993). Disruption of sulphated glycosaminoglycans in intestinal inflammation, Lancet 341, 711–714.
- Ofosu, F. A., Modi, G. J., Blajchman, M. A., et al. (1987). Increased sulphation improves the anticoagulant activities of heparan sulphate and dermatan sulphate, Biochem. J. 248, 889–896.
- Salas, A., Sans, M., Soriano, A., et al. (2000). Heparin attenuates TNF-alpha induced inflammatory response through a CD11b dependent mechanism, Gut 47, 88–96.
- Shute, J.K., Parmar, J., Holgate, S.T., et al. (1997). Urinary glycosaminoglycan levels are increased in acute severe asthma — a role for eosinophil-derived gelatinase B? Int. Arch. Allergy Immunol. 113, 366–367.
- Silvestro, L., Viano, I., Macario, M., et al. (1994). Effects of heparin and its desulfated derivatives on leukocyte-endothelialadhesion, Sem. Thromb. Haemost. 20, 254–258.
- Skinner, M. P., Lucas, C. M., Burns, G. F., et al. (1991). GMP-140 binding to neutrophils is inhibited by sulfated glycans, J. Biol. Chem. 266, 5371–5374.
- Smailbegovic, A., Lever, R. and Page, C. P. (2000). Heparin increases the adhesion of human peripheral blood mononuclear cells to pre-stimulated human umbilical vein endothelial cells without upregulating adhesion molecule expression, Amer. J. Respir. Crit. Care Med. 161, A773.
- Smailbegovic, A., Page, C. P. and Lever, R. (1999). Effects of heparin upon adhesion of human peripheral blood mononuclear cells to human stimulated umbilical vein endothelial cells and adhesion molecule expression in vitro, Brit. J. Pharmacol. 128, 249P.
- Tangelder, G. J. and Arfors, K.-E. (1991). Inhibition of leukocyte rolling in venules by protamine and sulfated polysaccharides, Blood 7, 1565–1571.
- Thunberg, L., Bäckström, G. and Lindahl, U. (1982). Further characterisation of the antithrombin-binding sequence in heparin, Carbohydr. Res. 100, 393–410.
- Tyrrell, D. J., Horne, A. P., Holme, K. R., et al. (1999). Heparin in inflammation: Potential therapeutic applications beyond anticoagulation, Adv. Pharmacol. 46, 151–208.
- Vlodavsky, I., Mohsen, M., Lider, O., et al. (1994). Inhibition of tumour metastasis by heparanase inhibiting species of heparin, Invasion Metastasis 14, 290–302.
- Watt, S. M., Williamson, J., Genevier, H., et al. (1993). The heparin binding PECAM-1 adhesion molecule is expressed by CD34 C hematopoietic precursor cells with early myeloid and B-lymphoid cell phenotypes, Blood 82, 2649–2663.
- Xie, X., Thorlacius, H., Raud, J., et al. (1997). Inhibitory effect of locally administered heparin on leukocyte rolling and chemoattractant-induced firm adhesion in rat mesenteric venules in vivo, Brit. J. Pharmacol. 122, 906–910.
- Role of glycosaminoglycans in inflammation
Volume 9, Issue 1-2 , pp 165-169
- Cover Date
- Print ISSN
- Online ISSN
- Brill Academic Publishers
- Additional Links