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Thromb Haemost 1998; 79(03): 609-613
DOI: 10.1055/s-0037-1614954
Review Articles
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Alboaggregins A and B. Structure and Interaction with Human Platelets

Anna M. Kowalska   *
1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
,
Li Tan
1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
,
John C. Holt
2   Rhone Poulenc Rorer Research Laboratories, King of Prussia, PA, USA
,
Manling Peng
1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
,
Jerzy Karczewski
3   Merck Research Laboratories, West Point, PA, USA
,
Juan J. Calvete
4   Institut für Reproduktionsmedizin, Tierärztliche Hochschule, Hannover, Germany
,
Stefan Niewiarowski
1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
› Author Affiliations
Further Information

Publication History

Received 16 June 1997

Accepted after revision 05 November 1997

Publication Date:
07 December 2017 (online)

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Summary

Viper venoms contain a variety of platelet binding proteins including those which bind to platelet GPIb/GPIX. Most of these proteins inhibit von Willebrand factor mediated platelet agglutination. Here we report the primary structures of unique members of this family, alboaggregins A and B, isolated from Trimeresurus albolabris, which have the ability to stimulate platelet agglutination and aggregation. Four chains of alboaggregin A and two chains of alboaggregin B share a high degree of homology and all cysteines in both alboaggregins are conserved. Both alboaggregins caused similar agglutination of fixed platelets. Alboaggregin A induced platelet aggregation and release reaction with EC50 = 10 and 30 nM, respectively, which is 20-fold lower than those for alboaggregin B. These observations suggest that the dimeric structure of alboaggregin B is sufficient to mediate its binding to GPIb and induce agglutination of platelets whereas aggregation and release reaction are significantly enhanced by tetrameric structure of alboaggregin A.

* Present address: M. A. Kowalska, Department of Hematology, Children’s Hospital of Philadelphia, Philadelphia, PA, USA


 

  • References

  • 1 Ikeda Y, Handa M, Kamata T, Kawano K, Kawai Y, Watanabe K, Kawakami K, Sagai K, Fukuyama M, Itagaki I, Yoshioka A, Rugieri ZM. Trans-membrane calcium influx assiociated with von Willebrand Factor binding to GPIb in the initiation of shear-induced platelet aggregation. Thromb Haemost 1993; 69: 469-502.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 2 Kroll MH, Harris TS, Moake JL, Handin RI, Schafer AI. Von Willebrand factor binding to platelet GPIb initiates signals for platelet activation. J Clin Invest 1991; 88: 1568-73.
    CrossrefPubMedGoogle Scholar
  • 3 Ruggeri ZM. Cell adhesion in vascular biology – von Willebrand Factor. J Clin Invest 1997; 99: 559-64.
    CrossrefPubMedGoogle Scholar
  • 4 Fujimura Y, Kawasaki T, Titani K. Snake venom proteins modulating the interaction between von Willebrand Factor and platelet glycoprotein Ib. Thromb Haemost 1996; 76: 633-9.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 5 Peng M, Lu W, Beviglia L, Niewiarowski S, Kirby EP. Echicetin: A snake venom protein that inhibits binding of von Willebrand factor and alboaggre-gins to platelet glycoprotein Ib. Blood 1993; 81: 2321-8.
    PubMedGoogle Scholar
  • 6 Chen YL, Tsai IH. Functional and sequence characterization of agkicetin, a new glycoprotein Ib antagonist isolated from Agkistrodon acutus venom. Biochem Biophys Res Comm 1995; 210: 472-7.
    CrossrefPubMedGoogle Scholar
  • 7 Taniuchi Y, Kawasaki T, Fujimura Y, Suzuki M, Titani K, Sakai Y, Kaku S, Hisamichi N, Satoh N, Takenaka T, Handa M, Sawai Y. Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. Biochim Biophys Acta 1995; 1244: 331-8.
    CrossrefPubMedGoogle Scholar
  • 8 Kawasaki T, Taniuchi Y, Hisamichi N, Fujimura Y, Suzuki M, Titani K, Sakai Y, Kaku S, Satoh N, Takenaka T, Handa M, Sawai Y. Tokaracetin, a new platelet antagonist that binds to platelet glycoprotein Ib and inhibits von Willebrand factor-dependent shear-induced platelet aggregation. Biochem J 1995; 308: 947-53.
    CrossrefPubMedGoogle Scholar
  • 9 Kawasaki T, Fujimura Y, Usami Y, Suzuki M, Miura S, Sakurai Y, Makita K, Taniuchi Y, Hirano K, Titani K. Complete amino acid sequence and identification of the platelet glycoprotein Ib-binding site of jararaca GPIb-BP, a snake venom protein isolated from B. jararaca . J Biol Chem 1996; 271: 10635-9.
    CrossrefPubMedGoogle Scholar
  • 10 Peng M, Emig FA, Mao A, Lu W, Kirby EP, Niewiarowski S, Kowalska MA. Interaction of echicetin with a high affinity thrombin binding site on platelet glycoprotein GPIb. Thromb Haemost 1995; 74: 954-7.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 11 Peng M, Lu W, Kirby EP. Alboaggregin-B: A new platelet agonist that binds to platelet membrane glycoprotein Ib. Biochemistry 1991; 30: 11529-362.
    CrossrefPubMedGoogle Scholar
  • 12 Peng M, Lu W, Kirby EP. Characterization of three alboaggregins purified from Trimeresurus albolabris venom. Thromb Haemost 1992; 67: 702-7.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 13 Usami Y, Suzuki M, Yoshida E, Sakurai Y, Hirano K, Kawasaki T, Fujimura Y, Titani K. Primary structure of alboaggregin-B purified from the venom of Trimeresurus albolabris . Biochem Biophys Res Comm 1996; 219: 727-33.
    CrossrefPubMedGoogle Scholar
  • 14 Andrews RK, Kroll MH, Ward CM, Rose JW, Scarborough RM, Smith AI, Lopez JA, Berndt MC. Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet activation. Biochemistry 1996; 35: 12629-39.
    CrossrefPubMedGoogle Scholar
  • 15 Kroll MH, Andrews RK, Lopez JA. A 50-kDa alboaggregin from Trimeresurus albolabris viper venom initiates signals for platelet activation by binding to the glycoprotein Ib/IX/V complex. Blood 1995; 86: 618a.
    PubMedGoogle Scholar
  • 16 Peng M, Lu W, Beviglia L, Niewiarowski S, Kirby EP. Echicetin: A snake venom protein that inhibits binding of von Willebrand factor and alboaggre-gins to platelet glycoprotein Ib. Blood 1993; 81: 2321-8.
    PubMedGoogle Scholar
  • 17 Peng M, Holt JC, Niewiarowski S. Isolation, characterization and amino acid sequence of echicetin β subunit, a specific inhibitor of von Willebrand factor and thrombin interaction with glycoprotein Ib. Biochem Biophys Res Comm 1994; 205: 68-72.
    CrossrefPubMedGoogle Scholar
  • 18 Mustard JF, Perry DW, Ardlie NG, Packham MA. Preparation of suspension of washed platelets from humans. Br J Haematol 1972; 22: 193-204.
    CrossrefPubMedGoogle Scholar
  • 19 Kirby EP. The agglutination of human platelets by bovine factor VIII:R. J Lab Clin Med 1982; 100: 963-76.
    PubMedGoogle Scholar
  • 20 Kowalska MA, Badellino K. Beta-amyloid protein induces platelet aggregation and supports platelet adhesion. Biochem Biophys Res Comm 1994; 205: 1829-35.
    CrossrefPubMedGoogle Scholar
  • 21 Dennis MS, Henzel WJ, Pitti RM, Lipari MT, Napier MA, Deisher TA, Bunting S, Lazarus RA. Platelet glycoprotein IIb/IIIa protein antagonists from snake venom: Evidence for a family of platelet aggregation inhibitors. Proc Soc Natl Acad Sci (USA) 1990; 87: 24741-51.
    PubMedGoogle Scholar
  • 22 Polgar J, Magnenat EM, Peitsch MC, Wells TN, Sagi MS, Clementson KJ. Amino acid sequence of the alpha subunit and computer modelling of the alpha and beta subunits of echicetin from the venom of Echis carinatus (saw-scaled viper). Biochem J 1997; 323: 533-7.
    CrossrefPubMedGoogle Scholar
  • 23 Mizuno H, Fujimoto Z, Koizumi M, Kana H, Atoda H, Morita T. Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains (letter). Nature Structural Biology 1997; 4: 438-41.
    CrossrefPubMedGoogle Scholar