Bulletin of Experimental Biology and Medicine

, Volume 142, Issue 5, pp 591–593 | Cite as

Pharmacodynamic parameters of anticoagulants based on sulfated polysaccharides from marine algae

  • N. N. Drozd
  • A. S. Tolstenkov
  • V. A. Makarov
  • T. A. Kuznetsova
  • N. N. Besednova
  • N. M. Shevchenko
  • T. N. Zvyagintseva
Article
Received:

Abstract

Fucoidans isolated from Fucus evanescens and Laminaria cichorioides kelp can inhibit thrombin and factor Xa of the blood coagulation system. In rats, intravenous injection of fucoidans dose-dependently increased anticoagulant activity of the plasma. Fucoidans can form complexes with protamine sulfate. The observed quantitative differences in the action of fucoidans can result from different sulfation degree and the presence of various types of glycoside bonds in polysaccharide molecules.

Key Words

fucoidans thrombin inhibition Xa factor inhibition pharmacodynamics protamine sulfate 
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    N. A. Zorin and O. A. Sebeleva, Vopr. Med. Khim., 32, No. 2, 134–137 (1986).PubMedGoogle Scholar
  2. 2.
    T. A. Kuznetsova, N. N. Besednova, A. N. Mamaev, et al., Byull. Eksp. Biol.Med., 136, No. 11, 532–534 (2003).Google Scholar
  3. 3.
    M. I. Kusaikin, A. O. Chizhov, S. A. Alekseeva, et al., Dokl. Ross. Akad. Nauk, 396, No. 5, 1–3 (2004).Google Scholar
  4. 4.
    E. V. Arzamastsev, Ed., Textbook on Experimental Study of Novel Pharmacological Agents [in Russian], Moscow (2000).Google Scholar
  5. 5.
    V. Grauffel, B. Kloareg, S. Mabeau, et al., Biomaterials, 10, No. 6, 363–368 (1998).CrossRefGoogle Scholar
  6. 6.
    S. Mauray, C. Sternberg, J. Theveniaux, et al., Thromb. Haemost., 74, No. 5, 1280–1285 (1995).PubMedGoogle Scholar
  7. 7.
    T. Nagumo, T. Nishino, Polysaccharides in Medicinal Applications, Ed. S. Dumitriu, New York, Basel, Hong-Kong (1997), pp. 545–574.Google Scholar
  8. 8.
    M. S. Pereira, Â. Mulloy, and P. A. Mahirao, J. Âiol. Chem., 274, No. 12, 7656–7667 (1999).CrossRefGoogle Scholar
  9. 9.
    C. H. Pletcher, M. Cunningham, and G. L. Nelsestuen, Biochim. Biophys. Acta, 838, No. 1, 106–113 (1985).PubMedGoogle Scholar
  10. 10.
    N. Ramamurthy, N. Baliga, T. W. Wakefield, et al., Anal. Biochem., 266, No. 1, 116–124 (1999).PubMedCrossRefGoogle Scholar
  11. 11.
    B. P. Schick, D. Maslow, A. Moshinski, and J.D. San Antonio, Blood, 103, No. 4, 1356–1363 (2004).PubMedCrossRefGoogle Scholar
  12. 12.
    J. M. Walenga and J. Fareed, Semin. Thromb. Hemost., 11, No. 2, 89–99 (1985).PubMedCrossRefGoogle Scholar
  13. 13.
    T. N. Zvyagintseva, N. M. Shevchenko, A. O. Chizhov, et al., J. Exp. Mar. Biol. Ecol., 294, Iss. 1, 1–13 (2003).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • N. N. Drozd
    • 1
  • A. S. Tolstenkov
    • 1
  • V. A. Makarov
    • 1
  • T. A. Kuznetsova
    • 2
  • N. N. Besednova
    • 2
  • N. M. Shevchenko
    • 3
  • T. N. Zvyagintseva
    • 3
  1. 1.Department of Pathology and Pharmacology of Hemostasis, Hematology Research CenterRussian Academy of Medical SciencesMoscow
  2. 2.Department of Immunology, Institute of Epidemiology and MicrobiologySiberian Division of the Russian Academy of Medical SciencesVladivostok
  3. 3.Department of Enzyme Chemistry, Pacific Institute of Bioorganic ChemistryFar East Division, Russian Academy of SciencesVladivostok

Personalised recommendations