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Marine Biology

, Volume 152, Issue 4, pp 1003–1007 | Cite as

Characterization of a low-sulfated chondroitin sulfate isolated from the hemolymph of the freshwater snail Planorbarius corneus

  • Nicola Volpi
  • Francesca Maccari
Research Article

Abstract

Glycosaminoglycans (GAGs) from the hemolymph of the freshwater snail Planorbarius corneus were recovered at about 0.9 μg/mL, being composed of a unique species characterized as chondroitin sulfate (CS) with a molecular mass of approximately 31,000 and having glucuronic acid as hexuronic acid. This macromolecule was determined to be composed of a low-sulfated polysaccharide made up of approximately 25% of the nonsulfated disaccharide, 17% of the 6-sulfated disaccharide, and about 58% of the 4-sulfated disaccharide, with a charge density value of 0.75 and a 4-sulfated/6-sulfated ratio of approximately 3.4. The data obtained suggest that the CS recovered in the Planorbarius corneus hemolymph is similar to the main human plasma polysaccharide and it may be generated as a main product of the catabolic processes.

Keywords

Hyaluronic Acid Chondroitin Sulfate Dermatan Sulfate Hexuronic Acid Iduronic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

CS

Chondroitin sulfate

DS

Dermatan sulfate

GAG

Glycosaminoglycan

References

  1. Cassaro CM, Dietrich CP (1977) Distribution of sulfated mucopolysaccharides in invertebrates. J Biol Chem 252:2254–2261PubMedGoogle Scholar
  2. Calatroni A, Vinci R, Ferlazzo AM (1992) Characteristics of the interactions between acid glycosaminoglycans and proteins in normal human plasma as revealed by the behaviour of the protein-polysaccharide complexes in ultrafiltration and chromatographic procedures. Clin Chim Acta 206:167–180CrossRefGoogle Scholar
  3. Cesaretti M, Luppi E, Maccari M, Volpi N (2004) Isolation and characterization of a heparin with high anticoagulant activity from the clam Tapes phylippinarum. Evidence for the presence of a high content of antithrombin III-binding site. Glycobiology 14:1275–1284CrossRefGoogle Scholar
  4. Crescenzi V, Dea ICM, Paoletti S, Stivala SS, Sutherland IW (eds) (1989) Biomedical and biotechnological advances in industrial polysaccharides. Gordon and Breach Sc Pub, New YorkGoogle Scholar
  5. Chavante SF, Santos EA, Oliveira FW, Guerrini M, Torri G, Casu B, Dietrich CP, Nader HB (2000) A novel heparan sulphate with high degree of N-sulphation and high heparin cofactor-II activity from the brine shrimp Artemia franciscana. Int J Biol Macromol 27:49–57CrossRefGoogle Scholar
  6. Dietrich CP, de-Paiva JF, Moraes CT, Takahashi HK, Porcionatto MA, Nader HB (1985) Isolation and characterization of a heparin with high anticoagulant activity from Anomalocardia brasiliana. Biochim Biophys Acta 843:1–7CrossRefGoogle Scholar
  7. Edens RE, al-Hakim A, Weiler JM, Rethwisch DG, Fareed J, Linhardt RJ (1992) Gradient polyacrylamide gel electrophoresis for determination of molecular weights of heparin preparations and low-molecular-weight heparin derivatives. J Pharm Sci 81:823–827CrossRefGoogle Scholar
  8. Guo YC, Conrad HE (1989) The disaccharide composition of heparins and heparan sulfates. Anal Biochem 176:96–104CrossRefGoogle Scholar
  9. Hardingham TE, Fosang AJ (1992) Proteoglycans: many forms and many functions. FASEB J 6:861–870CrossRefGoogle Scholar
  10. Hovingh P, Linker A (1982) An unusual heparan sulfate isolated from lobsters (Homarus americanus). J Biol Chem 257:9840–9844PubMedGoogle Scholar
  11. Jackson RJ, Busch SJ, Cardin AD (1991) Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol Rev 71:481–539CrossRefGoogle Scholar
  12. Jordan RE, Marcum JA (1986) Anticoagulantly active heparin from clam (Mercenaria mercenaria). Arch Biochem Biophys 248:690–695CrossRefGoogle Scholar
  13. Juvani M, Friman C, Ranta H, Wegelius O (1975) Isolation and characterization of undersulphated chondroitin-4-sulphate from normal human plasma. Biochim Biophys Acta 411:1–10CrossRefGoogle Scholar
  14. Lindahl U, Kusche-Gullberg M, Kjellen L (1998) Regulated diversity of heparan sulfate. J Biol Chem 273:24979–24982CrossRefGoogle Scholar
  15. Luppi E, Cesaretti M, Volpi N (2005) Purification and characterization of heparin from the italian clam Callista chione. Biomacromolecules 6:1672–1678CrossRefGoogle Scholar
  16. Mammen EF (ed) (1991) Development of non-heparin glycosaminoglycans as therapeutic agents. Sem thromb hemost 17(Suppl 1–2):137–245Google Scholar
  17. Medeiros GF, Mendes A, Castro RA, Bau EC, Nader HB, Dietrich CP (2000) Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates. Biochim Biophys Acta 1475:287–294CrossRefGoogle Scholar
  18. Mucci A, Schenetti L, Volpi N (2000) 1H- and 13C-nuclear magnetic resonance identification and characterization of components of chondroitin sulfates of various origin. Carbohydr Polym 41:37–45CrossRefGoogle Scholar
  19. Nader HB, Ferreira TMPC, Paiva JF, Medeiros MGL, Jeronimo SMB, Paiva VMP, Dietrich CP (1984) Isolation and structural studies of heparan sulfates and chondroitin sulfates from three species of molluscs. J Biol Chem 259:1431–1435PubMedGoogle Scholar
  20. Ofosu FA, Danishefsky I, Hirsh J (eds) (1989) Heparin and related polysaccharides. Structure and activities, vol 556. N Y Acad Sci, New YorkGoogle Scholar
  21. Oliveira FW, Chavante SF, Santos EA, Dietrich CP, Nader HB (1994) Appearance and fate of a beta-galactanase, alpha, beta-galactosidases, heparan sulfate and chondroitin sulfate degrading enzymes during embryonic development of the mollusc Pomacea sp. Biochim Biophys Acta 1200:241–246CrossRefGoogle Scholar
  22. Pejler G, Danielsson A, Bjork I, Lindahl U, Nader HB, Dietrich CP (1987) Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides. J Biol Chem 262:11413–11421PubMedGoogle Scholar
  23. Ruoslahti E (1988) Structure and biology of proteoglycans. Ann Rev Cell Biol 4:229–255CrossRefGoogle Scholar
  24. Scott JE (ed) (1993) Dermatan sulfate proteoglycans. Portland Press, LondonGoogle Scholar
  25. Sugahara K, Mikami T, Uyama T, Mizuguchi S, Nomura K, Kitagawa H (2003) Recent advances in the structural biology of chondroitin sulfate and dermatan sulfate. Curr Opin Struct Biol 13:612–620CrossRefGoogle Scholar
  26. Toyoda H, Kobayashi S, Sakamoto S, Toida T, Imanari T (1993) Structural analysis of a low-sulfated chondroitin sulfate chain in human urinary trypsin inhibitor. Biol Pharm Bull 16:945–947CrossRefGoogle Scholar
  27. Toyoda H, Kinoshita-Toyoda A, Selleck SB (2000) Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo. J Biol Chem 275:2269–2275CrossRefGoogle Scholar
  28. Volpi N (ed) (2006) Chondroitin sulfate: structure, role and pharmacological activity. Academic, AmsterdamGoogle Scholar
  29. Volpi N, Bolognani L (1993) Glycosaminoglycans and proteins: different behaviours in high-performance size-exclusion chromatography. J Chromatogr 630:390–396CrossRefGoogle Scholar
  30. Volpi N, Maccari F (2002) Detection of submicrogram quantities of glycosaminoglycans on agarose-gels by sequential staining with toluidine blue and Stains-All. Electrophoresis 23:4060–4066CrossRefGoogle Scholar
  31. Volpi N, Maccari F (2005a) Glycosaminoglycans composition of the large freshwater mollusc bivalve Anodonta anodonta. Biomacromolecules 6:3174–3180CrossRefGoogle Scholar
  32. Volpi N, Maccari F (2005b) Microdetermination of chondroitin sulfate in normal human plasma by fluorophore-assisted carbohydrate electrophoresis (FACE). Clin Chim Acta 356:125–133CrossRefGoogle Scholar
  33. Volpi N, Maccari F (2006) Chondroitin sulfate in normal human plasma is modified depending on the age. Its evaluation in patients with pseudoxanthoma elasticum. Clin Chim Acta 370:196–200CrossRefGoogle Scholar
  34. Volpi N, Mucci A (1998) Characterization of a low-sulfated chondroitin sulfate from the body of Viviparus ater (Mollusca gastropoda). Modification of its structure by lead pollution. Glycoconj J 15:1071–1078CrossRefGoogle Scholar
  35. Zhuo L, Salustri A, Kimata K (2002) A physiological function of serum proteogluycan bikunin: the chondroitin sulfate moiety plays a central role. Glycoconj J 19:241–247CrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  1. 1.Dipartimento di Biologia AnimaleUniversity of Modena and Reggio EmiliaModenaItaly

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