Anticoagulant activity of fucoidans from brown algae
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The anticoagulant activity of polysaccharide fucoidans from 11 species of brown algae was studied. The anticoagulant activity was measured by the activated partial thromboplastin time (APTT), prothrombin time, and thrombin time. Inhibitory action of these fucoidans significantly varied from one species to another. Fucoidans from Laminaria saccharina and Fucus distichus exhibited high anticoagulant activity, while fucoidans from Cladosiphon okamuranus and Analipus japonicus were almost inactive. Other fucoidans exhibited intermediate inhibitory activity. The inhibitory effect of fucoidans on thrombin and factor Xa was investigated in the presence or in the absence of natural thrombin inhibitor, antithrombin III (AT III). In contrast to the best-studied anticoagulant, heparin, most of these fucoidans inhibited thrombin in the absence of AT III. In the presence of AT III the inhibitory effect of fucoidans considerably increased. In contrast to heparin, fucoidans weakly influenced factor Xa activity in the presence of AT III and their inhibitory effect was not observed in the absence of AT III. There was no correlation between the anticoagulant activities of this series of fucoidans and their anti-inflammatory action, studied earlier. It is suggested that these two types of fucoidan activities depend on different structural features of fucoidans. Results of this study demonstrate a possibility of preparation of fucoidans with high anti-inflammatory activity but low anticoagulant activity. Anticoagulant activity of the fucoidans did not exhibit direct dependence on the content of fucose, the other neutral sugars and sulfates; no dependence was also found between the anticoagulant activity and the structure of the backbone of their molecules.
Key wordsfucoidan heparin blood coagulation thrombin factor Xa antithrombin
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- 4.Kuznetsova, T.A., Shevchenko, N.M., Zvyagintseva, T.N., and Besednova, N.N., Antibiot. Khemoter., 2004, vol. 49, no. 5, pp. 24–30.Google Scholar
- 5.Semenov, A.V., Mazurov, A.V., Preobrazhenskaya, M.E., Ushakova, N.A., Mikhailov, V.I., Berman, A.E., Usov, A.I., Nifant’ev, N.E., and Bovin N.V., Vopr. Med. Khim., 1998, vol. 44, pp. 135–144.Google Scholar
- 8.Granert, C., Raud, J., Waage, A., and Lindquist, L., Infect. Immun., 1999, vol. 67, pp. 2071–2074.Google Scholar
- 9.Preobrazhenskaya, M.E., Berman, A.E., Mikhailov, V.I., Ushakova, N.A., Mazurov, A.V., Semenov, A.V., Usov, A.I., Nifant’ev, N.E., and Bovin, N.V., Biochem. Mol. Biol. Int., 1997, vol. 43, pp. 443–451.Google Scholar
- 10.Cumashi, A., Ushakova, N.A., Preobrazhenskaya, M.E., D’Incecco, A., Piccoli, A., Totani, L., Tinari, N., Morozevich, G.E., Berman, A.E., Bilan, M.I., Usov, A.I., Ustyuzhanina, N.E., Grachev, A.A., Sanderson, C.J., Kelly, M., Rabinovich, G.A., Iacobelli, S., and Nifantiev, N.E., Glycobiology, 2007, vol. 17, pp. 541–552.CrossRefGoogle Scholar
- 11.Church, F.C., Meade, J.B., Treanor, R.E., and Whinna, H., J. Biol. Chem., 1989, vol. 264, pp. 3618–3623.Google Scholar
- 14.Vestweber, D. and Blank, J.E., Physiol. Reviews, 1999, vol. 79, pp. 181–213.Google Scholar
- 15.Warkentin, T.E., Thromb. Haemost., 1999, vol. 82, pp. 439–447.Google Scholar
- 17.Usov, A.I., Smirnova, G.P., Bilan, M.I., and Shashkov, A.S., Bioorgan. Khim., 1998, vol. 24, pp. 437–445.Google Scholar
- 22.Bilan, M.I., Zakharova, A.N., Grachev, A.A., Sashkov, A.S., Nifant’ev, N.E., and Usov, A.I., Bioorgan. Khim., 2007, vol. 33, pp. 44–53.Google Scholar
- 25.Gao, Y., Li, N., Fei, R., Chen, Z., Zheng, S., and Zeng, X., Mol. Cells, 2005, vol. 19, pp. 350–355.Google Scholar