The Inhibitory Effect of Sialic Acid on Fibrinolysis

H Rubin; N. D Ritz

doi:10.1055/s-0038-1654081

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1967; 17(01/02): 023-030
DOI: 10.1055/s-0038-1654081

Originalarbeiten - Original Articles - Travaux Originaux

Schattauer GmbH

The Inhibitory Effect of Sialic Acid on Fibrinolysis

H Rubin M. A.

¹Division of Hematology, Department of Medicine, Maimonides Hospital, Brooklyn, New York

,

N. D Ritz M. A., M. D.

¹Division of Hematology, Department of Medicine, Maimonides Hospital, Brooklyn, New York

› Author Affiliations

Abstract

Summary

The inhibitory effect of N-acetylneuraminic acid and glycolyl neuramaminic acids on the hydrolysis of ⁵¹Cr tagged casein by plasmin and α-chymotrypsin has been demonstrated. N,O-diacetylneuraminic acid was ineffective. The inhibitory effect was increased by an increase in ionic strength of the reaction mixture. The two active sialic acids also inhibited the fibrinolytic action of human plasmin on heated and unheated bovine fibrin plates. The greater inhibition noted on heated plates may indicate a primary effect on plasmin rather than on activators of plasmin. The inhibitory effects of N-acetyl neuraminic acid appeared to be potentiated by normal serum inhibitors. Sialic acid did not influence the conversion of fibrin monomer to polymer.

N-acetylneuraminic acid may play an important role in preserving the integrity of fibrin deposits in the body.

Full Text

References

References
1 Blombäch B. On the properties of fibrinogen and fibrin. Arkiv Kemi 12: 99 1958;
2 Chandrasekhar N, Warren L, Osbahr A, Laki K. Role of sialic acid in fibrinogen. Biochim. biophys. Acta (Amst.) 63: 337 1962;
3 Laki K, Chandrasekhar N. Sialic acid in fibrinogen and vulcanization of the fibrin clot. Nature (Lond.) 197: 1267 1963;
4 Rosenberg A, Carman R. H. Release of carbohydrate from fibrin monomer during clotting. Nature (Lond.) 204: 994 1964;
5 Lorand L, Jacobsen A. Specific inhibitors and the chemistry of fibrin polymerization. Biochemistry 3: 1939 1964;
6 Ritz N. D, Rubin H. Use of Chromium⁵¹ tagged casein for the determination of proteolytic activity. J. Lab. Clin. Med 63: 344 1964;
7 Latallo Z, Fletcher A. P, Alkjaersig N, Sherry S. Influence of pH, ionic strength, neutral ions, and thrombin on fibrin polymerization. Amer. J. Physiol 202: 675 1962;
8 Astrup T, Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem 40: 346 1952;
9 Erlanger B. F, Cooper A. G, Bendich A. J. On the heterogeneity of three-times crystallized a-chymotrypsin. Biochemistry 3: 1880 1964;
10 Donnelly T. H, Laskowski Jr. M, Notley N, Scheraga H. A. Equilibria in the fibrinogen-fibrin conversion. II. Reversibility of the polymerization steps. Arch. Biochem 56: 369 1955;
11 Norman S. P. Studies of the plasmin system. II. Inhibition of plasmin by serum or plasma. J. exper. Med 108: 53 1958;
12 Koshland Jr. D. E. Application of theory of enzyme specificitiy to protein synthesis. Proc. nat. Acad. Sci. (Wash.) 44: 98 1958;
13 Cunningham L. W. Proposed mechanism of action of hydrolytic enzymes. Science 125: 1145 1957;
14 Laki K. “The Logic of Thrombin Action”, Fibrinogen and Fibrin, Turnover of Clotting Factors, Transaction of the Conference held under auspices of the I. C. B. C. G., Gleneagles, Scotland. F. Kohler, Ed., 1963.
15 Gibbons B. A. The sensitivity of the neuraminosidic linkage in mucosubstances towards acid and towards neuraminidase. Biochem. J 89: 380 1963;
16 Shidman S, Herwig W. C, Ferry J. D. The conversion of fibrinogen to fibrin. V. Influence of ionic strength and thrombin concentration on the effectiveness of certain reversible inhibitors. Arch. Biochem 32: 354 1951;
17 Madoff M. S, Ebbe S, Baldini M. Sialic acid of human blood platelets. J. clin. Invest 43: 870 1964;
18 Eylar E. H, Madoff M. A, Brody O. V, Oncley J. L. The contribution of sialic acid to the surface charge of the erythrocyte. J. biol. Chem 237: 1992 1962;