Streptokinase and Urokinase Activation of Human, Chimpanzee and Baboon Plasminogen

Summary

Human, chimpanzee and baboon plasminogens, in that order, were found to be decreasingly susceptible to streptokinase (SK) activation. The relative activation of the three primate plasminogens remained the same when species specific fibrin or casein was used as substrate and when the following conditions were varied: 1. SK concentration; 2. plasminogen concentration; and 3. length of incubation of the SK-plasminogen-substrate reaction mixture. Under the same conditions, the three primate plasminogens were readily activated by human urokinase (UK) and no consistent order of activation by UK was observed. Our findings suggest that the site on plasminogen which interacts with SK has undergone changes during evolution whereas the site at which UK activates each of the three plasminogens has changed little. It remains obscure whether the susceptibility of primate plasminogen to SK activation is a specifically selected genetic trait or is simply a laboratory indication of structural changes in the plasminogen molecule that have occurred for other reasons.

^* Present address : Department of Medicine, Duke University Medical Center, Durham, North Carolina 27706.

^** Recipient of a Career Development Award, National H eart Institute, National I nstitutes of Health.

• References

• 1 Ablondi F. B, Hagan J. J. Comparison of certain properties of human plasminogen and “proactivator”. Proc. Soc. exp. Biol. (N. Y) 95: 195 1957;
• 2 Ablondi F. B, Hagan J. J. Studies on specificity of streptokinase. Proc. Soc. exp. Biol. (N. Y) 99: 769 1958;
• 3 Alkjaersig N, Fletcher A. P, Sherry S. The activation of human plasminogen. II. A kinetic study of activation with trypsin, urokinase and streptokinase. J. biol. Chem 233: 86 1958;
• 4 Buettner-Janusch J. (editor) Evolutionary and Genetic Biology of Primates. 36 Academic Press; New York: 1963
• 5 Celander D. R, Guest M. M. The biochemistry and physiology of urokinase. Amer. J. Cardiol 06: 409 1960;
• 6 Chandrasekhar N, Laki K. Evolution and the fibrinogen-thrombin interaction. In: Fibrinogen KLaki. (editor) 117 Marcel Dekker, Inc; New York: 1968
• 7 Cliffton E. E, Gannamela D. A. Variations in proteolytic activity of serum of animals including man. Proc. Soc. exp. Biol. (N. Y) 77: 305 1951;
• 8 Cliffton E. E, Downie G. R. Variations in proteolytic activity of serum of animals including man. Proc. Soc. exp. Biol. (N. Y) 73: 559 1950;
• 9 Cliffton E. E, Mootse G. Species variation in fibrinolytic activity. Thrombos. Diathes. hae-morrh. (Stuttg) 18: 291 1967;
• 10 Dayhoff M. O. Computer analysis of protein evolution. Sei. Amer 221: 87 1969;
• 11 DeRenzo E. C, Barg Jr. W, Boggiano C, Englert M. E, Davies M. C. Interaction of streptokinase and plasminogen. Biochem. biophys. Res. Commun 12: 105 1963;
• 12 DeRenzo E. C, Boggiano E, Barg Jr. W. F, Buck F. F. Interaction of streptokinase and human plasminogen. IV. Further gel electrophoretic studies on the combination of streptokinase with human plasminogen or human plasmin. J. biol. Chem 242: 2428 1967;
• 13 Dochez A. R, Shirley G. S, Mills K. C. Studies in the common cold. IV. Experimental transmission of the common cold to anthropoid apes and human beings by means of a filtrable agent. J. exp. Med 52: 701 1930;
• 14 Geiger W. B. Involvement of a complement-like factor in the activation of blood protease. J. Immunol 69: 597 1965;
• 15 Guest M. M, Daly B. M, Ware A. G, Seegers W. H. A study of the antifibrinolysin activity in the plasma of various animal species. J. clin. Invest 27: 785 1948;
• 16 Hadfield G, Magee V, Perry G. B. The lysis of fibrin by streptococci: Its application to the problems of rheumatic fever in children. Lancet I: 834 1934;
• 17 Hampton J. W, Matthews G. Similarities between baboon and human blood clotting. J. appl. Physiol 21: 1713 1966;
• 18 Hampton J. W, McKee P. A. The phylogeny of baboon fibrin-fibrinolysin. Acta Zoo. Path. Antverp 48: 59 1969;
• 19 Hawkey C. M. Fibrinolysis in animals. In: The Haemostatic Mechanism in Man and Other Animals. Symposia of the Zoological Society of London, No. 27. McFarlane R. G. (editor) 133 Academic Press Inc; New York and London: 1970
• 20 Hill R. L, Buettner-Janusch J. Evolution of hemoglobin. Fed. Proc 23: 1236 1964;
• 21 Kline D. L, Fishman J. B. Proactivator function of human plasmin as shown by lysine esterase assay. J. Biol. Chem 236: 2807 1961;
• 22 Kline D. L, Ts’ao G. H. Activation of human plasminogen by streptolinase in absence of plasmin -SK activator. Amer. J. Physiol 220: 440 1971;
• 23 Kowalski E, Kopec M, Niewiarowski S. An evaluation of the euglobulin method for the determination of fibrinolysis. J. clin. Path 12: 215 1959;
• 24 Ling G, Summaria L, Robbins K. G. Isolation and characterization of bovine plasminogen activator from a human plasminogen-streptokinase mixture. J. biol. Chem 242: 1419 1967;
• 25 Matthews G, McKee P, Kramer J, Hampton J. W. Functional and analytical characteristics of baboon plasminogen. Proc. Second Int. Cong. Primat 03: 113 1968;
• 26 Mohler S, Celander D. R, Guest M. M. Distribution of urokinase among the common mammals. Amer. J. Physiol 192: 186 1958;
• 27 Mullertz S. Formation and properties of the activator of plasminogen and of human and bovine plasmin. Biochem. J 61: 424 1955;
• 28 Müllertz S, Lassen M. An activator system in blood indispensable for formation of plasmin by streptokinase. Proc. Soc. exp. Biol. (N. Y) 82: 264 1953;
• 29 Muramatu M, Hayakumo Y, Onishi T, Sato T, Fujii S. Comparison of human plasmins formed by trace and large amounts of streptokinase. Jap. J. Biochem 65: 329 1969;
• 30 Niewiarowski S, Latallo Z. Comparative studies of the fibrinolytic system of sera of various vertebrates. Thrombos. Diathes. haemorrh. (Stuttg) 03: 404 1959;
• 31 Phillips L. L, Skrodelis V. The fibrinolytic enzyme system in normal, hemorrhagic and disease states. J. clin. Invest 37: 965 1958;
• 32 Pinkerton M. E, Boncyk L. H, Gline J. A. Microbiological parameters of the baboon (Papio sp) : Bacteriology. In: The Baboon in Medical Research. Vagtborg H. (editor) 717 University Press; Austin: 1967
• 33 Rantz L. A, Randall E. A modification of the technic for determination of the antistreptolysin titer. Proc. Soc. exp. Biol. (N. Y) 59: 22 1945;
• 34 Ratnoff O. D. Studies on a proteolytic enzyme in human plasma. II. Some factors influencing the enzymes activated by chloroform and streptococcal fibrinolysin. J. exp. Med 87: 211 1948;
• 35 Ruch T. G. Diseases of Laboratory Primates. 269 Saunders Co; Philadelphia, W.B: 1959
• 36 Saslaw S, Carlisle H. N. Streptococcal infection in normal and spelenctomized monkeys Proc. Soc. exp. Biol. (N. Y) 117: 420 1964;
• 37 Schwab J. B. S, Saslaw O. C, Woolpert G, Merino C. A. Doan Reactions of monkeys to experimental respiratory infections. II. Response to streptococcus hemolyticus group C. Proc. Soc. exp. Biol. (N. Y) 48: 560 1941;
• 38 Seegal B. G, Heller G, Jablonowitz J. Incidence of hemolytic streptococci and pneumococci in the pharyngeal flora or normal rhesus monkeys. Proc. Soc. exp. Biol. (N. Y) 34: 812 1936;
• 39 Sherry S. The fibrinolytic activity of streptokinase activated human plasmin. J. clin. Invest 33: 1054 1954;
• 40 Summaria L, Groskopf W. R, Robbins K. C. Urea dissociation of the isolated equimolar human plasmin -streptokinase complex (bovine plasminogen activator). Fed. Proc 28: 322 1964;
• 41 Summaria L, Hsich B, Groskopf W. R, Robbins K. G. Direct activation of human plasminogen by streptokinase. Proc. Soc. exp. Biol. (N. Y) 130: 737 1969;
• 42 Takada A, Takada Y, Ambrus J. L. Streptokinase -activatable proactivator of human and bovine plasminogen. J. biol. Chem 245: 6389 1970;
• 43 Takada Y. A, Takada J. L. Ambrus Comparative study of proactivators of the fibrinolysin system in three mammalian species. Thrombos. Diathes. haemorrh. (Stuttg) 21: 594 1969;
• 44 Tocantins L. M. (editor) The Coagulation of Blood: Methods of Study. 154 Grune and Stratton; New York: 1955
• 45 Ts’ao G. H, Kline D. L. Plasminogen activator formed by reaction of streptokinase with human plasminogen. J. appl. Physiol 26: 634 1969;
• 46 Vanace P. W. Experimental streptococcal infection in the rhesus monkey. Ann. N.Y. Acad. Sei 85: 910 1960;
• 47 Wallen P. B. Studies on the purification of human plasminogen: 1. The preparation of a partially purified human plasminogen with a low spontaneous proteolytic activity. Arkiv Kemi 19: 451 1962;
• 48 Wulf R. F, Mertz E. T. Studies on plasminogen. VIII. Species specificity of streptokinase. Canad. J. Biochem 47: 927 1969;