Skip to main content
Log in

Sulfated polysaccharide purified from Ecklonia cava accelerates antithrombin III-mediated plasma proteinase inhibition

  • Published:
Journal of Applied Phycology Aims and scope Submit manuscript

Abstract

Surface plasmon resonance is an important technique for studying molecular interactions and was used to investigate the molecular interaction of anticoagulant sulfated polysaccharides purified from an enzymatic hydrolysate of the brown alga Ecklonia cava (ECA) with blood coagulation factors. In a direct binding assay, binding affinity between ECA/antithrombin III (ATIII) and activated blood coagulation factors was in the order: factor VIIa (FVIIa) > factor Xa (FXa) > thrombin (FIIa); kinetic analysis determined K D values of ECA for FVIIa, FXa, and FIIa of 15.1, 45.0 and 65.0 nM, respectively. Therefore, ECA strongly and selectively (FVII, FX, and FII) enhanced ATIII-mediated coagulation factor inhibition in both the extrinsic and common coagulation pathways. This may contribute to its high anticoagulant activity in vitro. The low cytotoxicity of ECA to venous endothelial cell line (ECV-304) also expands its value in future in vivo studies. However, to utilize it as a model for novel anticoagulant agents, its possible interference with other anticoagulant mechanisms must be addressed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  • Athukorala Y, Jung WK, Vasanthan T, Jeon YJ (2006a) An anticoagulative polysaccharide from an enzymatic hydrolysate of Ecklonia cava. Carbohydr Polym 66:184–191

    Article  CAS  Google Scholar 

  • Athukorala Y, Kim KN, Jeon YJ (2006b) Antiproliferative and antioxidant properties of an enzymatic hydrolysate from brown alga, Ecklonia cava. Food Chem Toxicol 44:1065–1074

    Article  PubMed  CAS  Google Scholar 

  • Carmichael J, DeGraff WG, Gazdar AF, Minna JD, Mitchell JB (1987) Evaluation of a tetrazolium-based semiautomatic colorimetric assay: assessment of chemosensitivity testing. Cancer Res 47:936–942

    PubMed  CAS  Google Scholar 

  • Davie EW, Fujikawa K, Kisiel W (1991) The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30:10363–10370

    Article  PubMed  CAS  Google Scholar 

  • Desai UR (2004) New antithrombin-based anticoagulants. Med Res Rev 24:151–181

    Article  PubMed  CAS  Google Scholar 

  • Griffith MJ (1986) In: Zwaal RFP, Hemker HC (eds) Blood coagulation, Elsevier, Amsterdam, pp 259–283

  • Jordan RE, Oosta GM, Gardner WT, Rosenberg RD (1980) The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. J Biol Chem 255:10081–10090

    PubMed  CAS  Google Scholar 

  • Lawson JH, Butenas S, Ribarik N, Mann KG (1993) Complex-dependent inhibition of factor VIIa by antithrombin III and heparin. J Biol Chem 268:767–770

    PubMed  CAS  Google Scholar 

  • Lundblad RL, Kingdon HS, Mann KG (1976) Thrombin. Methods Enzymol 45:156

    PubMed  CAS  Google Scholar 

  • Matsubara K, Matsuura Y, Bacic A, Liao ML, Hori K, Miyazawa K (2001) Antiangiogenic properties of a sulfated galactan isolated from a marine green alga, Codium cylindricum. J Appl Phycol 126:3715–3723

    Google Scholar 

  • Mossman T (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65:55–63

    Article  Google Scholar 

  • Nishino T, Aizu Y, Nagumo T (1991) Antithrombin activity of a fucan sulfate from the brown seaweed Ecklonia kurome. Thromb Res 62:765–773

    Article  PubMed  CAS  Google Scholar 

  • Okai Y, Higashi-Okai K (1994) Identification of antimutagenic activities in the extracts of an edible brown alga, Hijikia fusiforme (Hijiki) by umu gene expression system in Salmonella typhimurium (TA 1535/pSK 1002). J Sci Food Agric 66:103–109

    Article  CAS  Google Scholar 

  • Okai Y, Higashi-Okai K, Nakamura S (1993) Identification of heterogeneous antimutagenic activities in the extract of edible brown seaweeds, Laminaria japonica (Makonbu) and Undaria pinnatifda (Wakame) by umu gene expression system in Salmonella typhimurium (TA 1535/pSK 1002). Mutat Res 302:63–70

    Article  Google Scholar 

  • Olson ST, Bjork I, Shore JD (1993) Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol 222:525–559

    PubMed  CAS  Google Scholar 

  • Rosenberg RD, Rosenberg JS (1984) Natural anticoagulant mechanisms. J Clin Invest 74:1–6

    Article  PubMed  CAS  Google Scholar 

  • Shanmugam S, Mody KH (2000) Heparonid active sulfated polysaccharides from marine algae as potential blood coagulant agents. Curr Sci 79:1672–1683

    CAS  Google Scholar 

  • Shobe J, Dickinson CD, Edgington TS, Ruf W (1999) Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking. J Biol Chem 274:24171–24175

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgements

This research was supported by a grant (p-2004-03) from the Marine Bioprocess Research Center of the Marine Bio 21 Center funded by the Ministry of Maritime Affairs and Fisheries, Republic of Korea. This work was also supported by the Korea Research Foundation Grant (KRF-2004-908-F00005), Republic of Korea.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to You-Jin Jeon.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jung, WK., Athukorala, Y., Lee, YJ. et al. Sulfated polysaccharide purified from Ecklonia cava accelerates antithrombin III-mediated plasma proteinase inhibition. J Appl Phycol 19, 425–430 (2007). https://doi.org/10.1007/s10811-006-9149-0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10811-006-9149-0

Key words

Navigation