Structural characterization of low molecular weight heparins

Seminars in Thrombosis and Hemostasis

Volumn 25, Issue SUPPL. 3, 1999, Pages 17-25

  Casu, Benito ^a   Torri, Giangiacomo ^a  

^a Istituto di Ricerche Chimiche e Biochimiche G Ronzoni   (Italy)

Author keywords

Antithrombin binding sequence; Endresidues; Linkage region; Low molecular weight heparins; Nmr spectra; Sulfation patterns

Indexed keywords

ENOXAPARIN; HEPARIN; LOW MOLECULAR WEIGHT HEPARIN; TINZAPARIN;

CONFERENCE PAPER; DEPOLYMERIZATION; DRUG CONFORMATION; DRUG PROTEIN BINDING; DRUG STRUCTURE; DRUG SULFATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ANIMALS; BINDING SITES; DISACCHARIDES; HEPARIN, LOW-MOLECULAR-WEIGHT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR STRUCTURE;

EID: 0032721258     PISSN: 00946176     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (34)

1. Casu B. Structure and biological activity of heparin. Adv CarbohydrChemBiochem 1985;43:51-134
2. Lindahl U, Kusche-Gullberg M, Kjellén L. Regulated diversity of heparan sulfate. J Biol Chem 1998;273:24979-24982
3. Dietrich CP, Tersariol IL, Toma L, et al. Structure of heparan sulfate: Identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origin. Cell Mol Biol 1998;44:417-429
4. Linhardt RJ, Loganathan D, Al-Hakim A, et al. Oligosaccharide mapping of low molecular weight heparins: Structural differences and their relation to activity. J Med Chem 1990;33:1639-1645
5. Casu B. Methods of structural analysis. In: Lane DA, Lindahl U, eds. Heparin: Chemistry and Biology. London: Arnold; 1989: 25-49
6. Linhardt RJ, Wang H, Ampofo SA. New methodologies in heparin structure analysis and the generation of LMW heparins. In: Lane DA, Björk I, Lindahl U. eds. Heparin and Related Polysaccharides. New York, NY; Plenum Press; 1992:37-47
7. Casu B. Heparin structure. Haemostasis 1990;20(Suppl l):62-73
8. Desai UR, Linhardt RJ. Molecular weight of low molecular weight heparins by 13C nuclear magnetic resonance spectroscopy. Carbohydr Res 1994;255:193-212
9. Torn G, et al. I3C and 'H-NMR characterization of low molecular weight heparins. Manuscript in preparation
10. Casu B. Structure of heparins and their fragments. Nouv Rev Fr Hematol 1984;26:211-219
11. Ragazzi M, Ferro DR, Provasoli A, et al. Confirmation of the unsaturated uronic acid residues of glucosaminoglycan disaccharides. J Carbohydr Chem 1993;12:523-535
12. Bazin HG, Capila I, Linhardt RJ. Conformational study of synthetic A4-uronate monosaccharides and glycosaminoglycanderived disaccharides. Carbohydr Res 1998:309:135-144
13. Casu B, Guerrini M, Naggi A, Toni G. NMR spectroscopic differentiation between beef and pig mucosal heparins. Thromb Haemost 1995;74:1205
14. Casu B, Guerrini M, Naggi A, et al. Characterization of sulfation patters of beef and pig mucosal heparins by nuclear magnetic resonance spectroscopy. Arzneim-Forsch/Drug Res 1966;46: 472-477
15. Casu B, Oreste P, Torn G, et al. The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin Ill-binding sequence. Chemical and C-NMR studies. Biochem J 1981:197:599-609
16. Mulloy B, Johnson EA. Assignment of the 'H-NMR spectra of heparin and heparansulfate. Carbohydr Res 1987;170:151-165
17. Kusche M, Torri G, Casu B, Lindahl U. Biosynthesis of heparin. Availability of glucosaminyl 3-O-sulfation sites. J Biol Chem 1990:265:7292-7300
18. Bisio A, Guerrini M, Yates EA, Torri G, Casu B. NMR identification of structural environments for 2,3 or 2,3,6 tri-sulfated glucosamine residues in heparin with high and no affinity for antithrombin. Glycoconj J 1997;14 (Suppl 1):S89
19. lacomini M, Casu B, Guerrini M, et al. Linkage region sequences of heparins and heparan sulfates. Detection and quantification by NMR spectroscopy. Anal Biochem 1999; in press
20. Casu B, Naggi A, Oreste P, et al. Bleeding associated with heparin contaminants. Lancet 1987;1088
21. Jaseja M, Rey RN, Sauriol F, Perlin AS. Novel regio- and stereoselective modifications of heparin in alkaline solution. NMR spectroscopic evidence. Can J Chem 1989;67:1449-1458
22. Key N, Perlin AS. Base-catalized conversion of the a-L-iduronic acid 2-sulfate unit of heparin into a unit of ct-L-galacturonic acid, and related reactions. Carbohydr Res 1990;200:437-447
23. Piani S, Casu B, Marchi EG, Torn G, Ungarelli FJ. Alkali-induced optical rotation changes in heparins and heparan sulfates, and their relation to iduronic acid-containing sequences. Carbohydr Chem 1993; 12:507-521
24. Yates EA, Santini F, Bisio A, Cosentino C. Evidence for a heparin derivative containing an N-sulfated aziridine ring. Carbohydr Res 1997;298:335-340
25. Yates EA, Santini F, Guerrini M, et al. A method for the quantification of 2,3- and 2,3,6-suIfated D-glucosamine units in natural and chemically-modified heparins. Abstract Eurocarb-9 1997;D40
26. Toida T, Vlahov IR, Smith AE, Hileman RE, Linhardt RJ. C-2 epimerization of N-acetylglucosamine in an oligosaccharide derived from heparan sulfate. J Carbohydr Chem 1996:15:351-360
27. Yamada S, Watanabe M, Sugahara K. Conversion of N-sulfated glucosamine to N-sulfated mannosamine in an unsturated heparin disaccharide by non-enzymatic, base-catalyzed C-2 epimerization during enzymatic oligosaccharide preparation. Carbohydr Res 1998;309:261-268
28. Mulloy B, Forster MJ, Jones C, Davies DB. NMR and molecularmodelling studies of the solution conformation of heparin. BiochemJ 1993 ;293:849-858
29. Ragazzi M, Ferro RD, Perly B, et al. Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III. Carbohydr Res 1990;195:169-185
30. Casu B. Protein binding of sulfated glycosaminoglycans: searching for specificity. In: Nonanticoagulant action of glycosaminoglycans. Harenberg J, Casu B, eds. New York: Plenum Press; 1996:89-99
31. Ferro DR, Provasoli A, Ragazzi M, et al. Evidence for conformational equilibrium of the sulfated L-iduronate residue in heparin and in synthetic heparin mono- and oligosaccharides: NMR and force-field studies. J Amer Chem Soc 1986; 108:6773-6778
32. Casu B, Petitou M, Provasoli M, Sinay P. Conformational flexibility: A concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends BiochemScil988;13:221-225
33. Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. Heparin structure and interactions with basic fibroblast growth factor. Science 1996;271:1116-1120
34. Hileman RE, Fromm JR, Weiler JM, Linhardt RJ. Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins. BioEssays 1998;20:156-167