Biological effects of heparan sulfates and regioselectively modified heparin-heparan mimetics

Journal of Bioactive and Compatible Polymers

Volumn 18, Issue 1, 2003, Pages 59-81

  Baumann, H ^a  

^a RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Anticoagulants; Antiproliferation; Athrombogenity; Biomaterials; Growth factors; Heparan sulfate; Heparin; Heparin heparan mimetics; Oligo and polysaccharides; Plasma protein adhesion

Indexed keywords

BIOMIMETIC MATERIALS; CELLS; CHEMICAL ACTIVATION; ENZYME INHIBITION; FUNCTIONAL POLYMERS; POLYSACCHARIDES; STEREOCHEMISTRY;

HEPARAN;

BIOPOLYMERS;

ACETIC ACID DERIVATIVE; AMINE; BIOPOLYMER; CARBOXYL GROUP; CHEMOKINE; GROWTH FACTOR; HEPARAN; HEPARAN SULFATE; HEPARIN; HEPARIN DERIVATIVE; HEPARINOID; MORPHOGEN; POLYSACCHARIDE; PROTEINASE INHIBITOR; SULFATE;

ANTICOAGULATION; ARTICLE; CELL MATURATION; CHEMICAL MODIFICATION; CONCENTRATION (PARAMETERS); DRUG ACTIVITY; DRUG STRUCTURE; ENDOTHELIUM CELL; EXTRACELLULAR MATRIX; MOLECULAR WEIGHT; SEQUENCE ANALYSIS; STEREOCHEMISTRY; THROMBOCYTE ADHESION;

EID: 0038024248     PISSN: 08839115     EISSN: None     Source Type: Journal    
DOI: 10.1177/0883911503018001006     Document Type: Article

References (51)

1. Gallagher, J.T. (2001). Heparan Sulfate: Growth Control with a Restricted Sequence Menu, J. Clin. Invest., 108: 357-361.
2. Tumova, S., Woods, A. and Couchman, J.R. (2000). Heparan Sulfate Proteoglycans on the Cell Surface: Versatile Coordinators of Cellular Functions, Int. J. Biochem. Cell. Biol., 32: 269-288.
3. Sasisekharan, R. and Venkataraman, G. (2000). Heparin and Heparan sulfate: Biosynthesis, Structure and Function, Curr. Opin. Chem. Biol., 4: 626-631.
4. Venkataraman, G., Shriver, Z., Davis, J.C. and Sasisekharan, R. (1999). Fibroblast Growth Factors 1 and 2 are Distinct in Oligomerization in the Presence of Heparin-like Glycosaminoglycans, In: Proc. Natl. Acad. Sci. USA, 96: 1892-1897.
5. Rong, J., Nordling, K., Bjork, I. and Lindahl, U. (1999). A Novel Strategy to Generate Biologically Active Neo-glycosaminoglycan Conjugates, Glycobiology, 9: 1331-1336.
6. Ornitz, D.M., Herr, A.B., Nilsson, M., Westman, J., Svahn, C.-M. and Waksman, G. (1995). FGF Binding and FGF Receptor Activation by Synthetic Heparan-derived Di- and Trisaccharides, Science, 268: 432-436.
7. Vlodavsky, I. and Friedmann, Y. (2001). Molecular Properties and Involvement of Heparanase in Cancer Metastasis and Angiogenesis, J. Clin. Invest., 108: 341-347.
8. Van Boeckel, C.A.A. and Petitou, M. (1993). Die charakteristische AT-III-Bindungsregion in Heparin: eine Leitstruktur für neue synthetische Antithrombotica, Angew. Chem., 105: 1741-1761.
9. Petitou, M., Hérault, J.-P., Bernat, A., Driguez, P.-A., Duchaussoy, P., Lormeau, J.-C. and Herbert, J.-M. (1999). Synthesis of thrombin-inhibiting Heparin Mimetics without Side Effects, Letters to Nature, 398: 417-422.
10. Petitou, M., Duchaussoy, P., Herbert, J.-M., Duc, G., El Hajji, M., Branellec, J.F., Donat, F., Necciari, J., Cariou, R., Bouthier, J. and Garrigou, E. (2002). The Synthetic Pentasaccharide Fondaparinux: First in the Class of Antithrombotic Agents that Selectively Inhibit Coagulation Factor Xa, Semin. Thromb. Hemost., 28: 393-402.
11. Wessel, H.P. (1997). Heparinoid Mimetics. In: Driguez, H. and Thiem, J. (Eds.), Topics in Current Chemistry, Vol. 187, pp. 216-237, Springer Verlag, Berlin.
12. Conrad, H.E. (1998). Heparin-Binding Proteins, Academic Press, San Diego, California.
13. Gallagher, J.T. (1998). The Interaction and Regulation of Basic and Acidic Fibroblast Growth Factors by Heparan Sulfate, Trends Glycosci. Glycobiol., 10: 137-144.
14. Baumann, H., Huppertz, B., Sharon, R., Tessler, S. and Neufeld, G. (1999). The Influence of Functional Groups on Semisynthetic Heparin Like Molecules on Binding to Vascular Endothelial Growth Factor (VEGF). In: Ottenbrite, R., Chiellini, E., Cohn, D., Miglaresi, C. and Sunamoto, I. (Eds.), Frontiers in Biomedical Polymer Applications, Vol. 2, pp. 115-129, Technomic, Lancaster.
15. Baumann, H. (2002). The Influence of Synthetic Heparin and Heparan Mimetics or Analoga for Drug Design, Preprints ACS Meeting Boston, Poly 712; 224.
16. Migdal, M., Huppertz, B., Tessler, S., Comforti, A., Shibuya, M., Reich, R., Baumann, H. and Neufeld, G. (1998). Neuropilin-1 is a Placenta Growth Factor-2 Receptor, J. Biol. Chem., 273: 22272-22278.
17. Lyon, M. and Gallagher, J.T. (1998). Bio-specific Sequences and Domains in Heparan Sulphate and the Regulation of Cell Growth and Adhesion, Matrix Biol., 17: 485-493.
18. Pye, D. A., Vives, R.R., Hyde, P. and Gallagher, J.T. (2000). Regulation of FGF-1 Mitogenic Activity by Heparan Sulfate Oligosaccharides is Dependent on Specific Structural Features: Differential Requirements for the Modulation of FGF-1 and FGF-2, Glycobiology, 10: 1183-1192.
19. Pye, D.A. and Gallagher, J.T. (1999). Monomer Complexes of Basic Fibroblast Growth Factor and Heparan Sulfate Oligosaccharides are the Minimal Functional Unit for Cell Activation, J. Biol. Chem., 274: 13456-13461.
20. Guimond, S.E., Maccarana, M., Olwin, B.B., Lindahl, U. and Rapraeger, A.C. (1993). Activating and Inhibitory Heparin Sequences for FGF-2 (Basic FGF). Distinct Requirements for FGF-1, FGF-2 and FGF-4. J. Biol. Chem., 268: 23906-23914.
21. Guimond, S.E. and Turnbull, J.E. (1999). Fibroblast Growth Factor Receptor Signaling is Dictated by Specific Heparan Sulfate Saccharides, Curr. Biol., 9: 1343-1346.
22. Ishihara, M., Shaklee, P.N., Yang, Z., Liang, W., Wei, Z., Stack, R.J. and Holme, K. (1994). Structural Features in Heparin which Modulate Specific Biological Activities Mediated by Basic Fibroblast Growth Factor, Glycobiology, 4: 451-458.
23. Baumann, H. (2001). The Role of Regioselectively Sulphated and Acetylated Polysaccharide Coatings of Biomaterials for Reducing Platelet and Plasma Protein Adhesion, Sem. Thromb. Hemost. 27: 445-463.
24. Kariya, Y., Kyogashima, M., Suzuki, K., Isomura, T., Sakamoto, T., Horie, K., Ishihara, M., Takano, R., Kamei, K. and Hara, S. (2000). Preparation of Completely 6-O-desulfated Heparin and its Ability to Enhance Activity of Basic Fibroblast Growth Factor, J. Biol. Chem., 275: 25949-25958.
25. Maccarana, M., Casu, B. and Lindahl, U. (1993). Minimal Sequence in Heparin/Heparan Sulfate Required for Binding of Basic Fibroblast Growth Factor, J. Biol. Chem., 268: 23898-23905.
26. Parish, C.R., Freeman, C., Brown, K.J. and Francis, D.J. and Cowden, W.B. (1999). Identification of Sulfated Oligosaccharide-based Inhibitors of Tumor Growth and Metastasis Using Novel in vitro Assays for Angiogenesis and Heparanase Activity, Cancer Res., 59: 3433-3441.
27. Perrimon, N. and Bernfield, M. (2000). Specificities of Heparan Sulphate Proteoglycans in Developmental Processes, Nature, 404: 725-728.
28. Gunay, N.S. and Linhardt, R.J. (1999). Heparinoids: Structure, Biological Activities and Therapeutic Applications, Semin. Thromb. Hemost., 25: 5-16.
29. Baumann, H. (2002). Concepts for Synthesis of Bioactive Regioselectively Sulfated and Acetylated Derivatives of Cellulose, Chitosan, Heparin and Heparansulfate with Highest Possible Completeness: Defined Polysaccharides for Drug Design. Part I and Part II, Bioac. Comp. Polym., in preparation.
30. Stringer, S.E. and Gallagher, J.T. (1997). Specific Binding of the Chemokine Platelet Factor 4 to Heparan Sulfate, J. Biol. Chem., 272: 20508-20514.
31. Brown, K.J. and Parish, C.R. (1994). Histidine-rich Glycoprotein and Platelet Factor 4 Mask Heparan Sulfate Proteoglycans Recognized by Acidic and Basic Fibroblast Growth Factor, Biochemistry, 33: 13918-13927.
32. Baumann, H., Scheen, H., Huppertz, B. and Keller, R. (1998). Novel Regioand Stereoselective O-6-desulfation of the Glucosamine Moiety of Heparin with N-Methylpyrrolidinone-Water or N,N-Dimethylformamide-Water Mixtures, Carbohydr. Res., 308: 381-388.
33. Baumann, H., Richter, A., Klemm, D. and Faust, V. (2000). Concepts for Preparation of Novel Regioselective Modified Cellulose Derivatives Sulphated, Aminated for Hemocompatible Ultrathin Coatings on Biomaterials, Macromol. Chem. Phys., 201: 1950-1962.
34. Baumann, H. and Faust, V. (2001). Concepts for Improved Regioselective Placement of O-Sulfo, N-Sulpho, N-Acetyl, and N-Carboxymethyl Groups in Chitosan Derivatives, Carbohydr. Res., 331: 43-57.
35. Liu, C. and Baumann, H. (2002). Exclusive and Complete Introduction of Amino Groups and their N-Sulfo and N-Carboxymethyl Groups into the 6-Position of Cellulose Without the Use of Protecting Groups. Carbohydr. Res., 337: 1297-1307.
36. Keiser, N., Venkataraman, G., Shriver, Z. and Sasisekharan, R. (2001). Direct Isolation and Sequencing of Specific Protein-binding Glycosaminoglycans, Nature Medicine, 7: 123-128.
37. Obadiah, J., Plante, J., Palmacci, E.R. and Seeberger, P.H. (2001). Automated Solid-phase Synthesis of Oligosaccharides, Science, 291: 1523-1527.
38. Mulloy, B., Forster, M.J., Jones, C. and Davies, D.B. (1993). N.M.R. and Molecular-modelling Studies of the Solution Conformation of Heparin, Biochem. J., 293: 849-858.
39. Mulloy, B. and Forster, M.J. (2000). Conformation and Dynamics of Heparin and Heparan Sulfate, Glycobiology, 10: 1147-1156.
40. Jin, L., Abrahams, J.P., Skinner, R., Petitou, M., Pike, R.N. and Carrel, R.W. (1997). The Anticoagulant Activation of Antithrombin by Heparin, In: Proc. Natl. Acad. Sci. USA, 94: 14683-14688.
41. Turnbull, J.E., Hopwood, J.J. and Gallagher, J.T. (1999). A Strategy for Rapid Sequencing of Heparan Sulfate and Heparin Saccharides, In: Proc. Natl. Acad. Sci. USA, 96: 2698-2703.
42. Vives, R.R., Pye, D.A., Salmivirta, M., Hopwood, J.J., Lindahl, U. and Gallagher, J.T. (1999). Sequence Analysis of Heparan Sulphate and Heparin Oligosaccharides, Biochem. J., 339: 767-773.
43. Rhomberg, A.J., Shriver, Z., Biemann, K. and Sasisekharan, R. (1998). Mass Spectrometric Evidence for the Enzymatic Mechanism of the Depolymerization of Heparin-like Glycosaminoglycans by Heparinase II, In: Proc. Natl. Acad. Sci. USA, 95: 12232-12237.
44. Rosenberg, R.D. and Lam, L. (1979). Correlation Between Structure and Function of Heparin, In: Proc. Natl. Acad. Sci. USA, 76: 1218-1222.
45. Lindahl, U., Thunberg, L., Backstrom, G., Riesenfeld, J., Nordling, K. and Bjork, J. (1984). Extension and Structural Variability of the Antithrombin-binding Sequence in Heparin, J. Biol. Chem., 259: 12368-12376.
46. Lato, L.H., Silbert, J.E. and Rosenberg, R.D. (1976). The Separation of Active and Inactive Forms of Heparin, Biochem. Biophys. Res. Commun., 69: 570-577.
47. De Boer, H.C., de Groot, P.G., Bouma, B.N. and Preissner, K.T. (1993). Ternary Vitronectin-thrombin-antithrombin III Complexes in Human Plasma, Detection and Mode of Association, J. Biol. Chem., 268: 1279-1283.
48. Prestrelski, S.J., Fox, G.M. and Arakawa, T. (1992). Binding of Heparin to Basic Fibroblast Growth Factor Induces a Conformational change, Arch. Biochem. Biophys., 293: 314-319.
49. Davis, J.C., Venkataraman, G., Shriver, Z., Raj, P.A. and Sasisekharan, R. (1999). Oligomeric Self-association of Basic Fibroblast Growth Factor in the Absence of Heparin-like Glycosaminoglycans, Biochem. J., 341: 613-620.
50. Kan, M., Wang, F., Xu, J., Crabb, J.W., Hou, J. and McKeehan, W.L. (1993). An Essential Heparin-binding Domain in the Fibroblast Growth Factor Receptor Kinase, Science, 259: 1918-1921.
51. Maccarana, M., Sakura, Y., Tawada, A., Yoshida, K. and Lindahl, U. (1996). Domain Structure of Heparan Sulfates from Bovine Organs, J. Biol. Chem., 271: 17804-17810.