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DOI: 10.1055/s-0037-1613067
Alboluxin, a Snake C-type Lectin from Trimeresurus albolabris Venom is a Potent Platelet Agonist acting via GPIb and GPVI
Publication History
Received
10 September 2001
Accepted after resubmission
28 December 2001
Publication Date:
08 December 2017 (online)
Summary
Alboluxin, a potent platelet activator, was purified from Trimeresurus albolabris venom with a mass of 120 kDa non-reduced and, after reduction, subunits of 17 and 24 kDa. Alboluxin induced a tyrosine phosphorylation profile in platelets that resembles those produced by collagen and convulxin, involving the time dependent tyrosine phosphorylation of Fc receptor γ chain (Fcγ), phospholipase Cγ2 (PLCγ2), LAT and p72SYK. Antibodies against both GPIb and GPVI inhibited platelet aggregation induced by alboluxin, whereas antibodies against α2β1 had no effect. Inhibition of αIIbβ3 reduced the aggregation response to alboluxin, as well as tyrosine phosphorylation of platelet proteins, showing that activation of αIIbβ3 and binding of fibrinogen are involved in alboluxin-induced platelet aggregation and it is not simply agglutination. N-terminal sequence data from the β-subunit of alboluxin indicates that it belongs to the snake C-type lectin family. The C-type lectin subunits are larger than usual possibly due to post-translational modifications such as glycosylation. Alboluxin is a hexameric (αβ)3 snake C-type lectin which activates platelets via both GPIb and GPVI.
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References
- 1 Clemetson KJ. Platelet collagen receptors: A new target for inhibition?. Haemostasis 1999; 29: 16-26.
- 2 Clemetson KJ. Primary haemostasis: Sticky fingers cement the relationship. Current Biology 1999; 09: 110-2.
- 3 Du X, Plow EF, Frelinger III AL, O’Toole TE, Loftus JC, Ginsberg MH. Ligands “activate” integrin αIIbβ3 (platelet GPIIb-IIIa). Cell 1991; 65: 409-16.
- 4 Moroi M, Onitsuka I, Imaizumi T, Jung SM. Involvement of activated integrin α2β1 in the firm adhesion of platelets onto a surface of immobilized collagen under flow conditions. Thromb Haemost 2000; 83: 769-76.
- 5 Clemetson JM, Polgar J, Magnenat E, Wells TN, Clemetson KJ. The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcαR and the natural killer receptors. J Biol Chem 1999; 274: 29019-24.
- 6 Clemetson KJ, Polgar J, Clemetson JM. Snake venom C-type lectins as tools in platelet research. Platelets 1998; 09: 165-9.
- 7 Andrews RK, Berndt MC. Snake venom modulators of platelet adhesion receptors and their ligands. Toxicon 2000; 38: 775-91.
- 8 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.
- 9 Peng M, Lu W, Kirby PE. Alboaggregin-B: A new platelet agonist that binds to platelet membrane glycoprotein Ib. Biochemistry 1991; 30: 11529-36.
- 10 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.
- 11 Dormann D, Clemetson JM, Navdaev A, Kehrel BE, Clemetson KJ. Alboaggregin A activates platelets by a mechanism involving glycoprotein VI as well as glycoprotein Ib. Blood 2001; 97: 929-36.
- 12 Wicki AN, Clemetson JM, Steiner B, Schnippering W, Clemetson KJ. Isolation and characterization of glycoprotein Ib. Methods Enzymol 1992; 215: 276-88.
- 13 Polar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, Timothy NCW, Clemetson KJ. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J Biol Chem 1997; 272: 13576-83.
- 14 Peng M, Lu W, Beviglia L, Niewiarowski S, Kirby EP. Echicetin: a snake venom protein that inhibits binding of von Willebrand factor and alboaggregins to platelet glycoprotein Ib. Blood 1993; 81: 2321-8.
- 15 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 1970; 227: 680-5.
- 16 Morrissey JH. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 1981; 117: 307-10.
- 17 Watson SP, Gibbins J. Collagen receptor signaling in platelets: extending the role of the ITAM. Immunology Today 1998; 19: 260-3.
- 18 Peng M, Lu W, Kirby EP. Characterization of three alboaggregins purified from Trimeresurus albolabris venom. Thromb Haemost 1992; 67: 702-7.
- 19 Usami Y, Fujimura Y, Suzuki M, Ozeki Y, Nishio K, Fukui H, Titani K. Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca . Proc Natl Acad Sci USA 1993; 90: 928-32.
- 20 Leduc M, Bon C. Cloning of subunits of convulxin, a collagen-like plateletaggregating protein from Crotalus durissus terrificus venom. Biochem J 1998; 333: 389-93.
- 21 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 Commun 1996; 219: 727-33.