Aptamer-based modulation of blood coagulation

Hamostaseologie

Volumn 31, Issue 4, 2011, Pages 258-263

  Mayer, G ^a   Rohrbach, F ^a   Potzsch B ^b   Muller J ^b  

^a UNIVERSITY OF BONN   (Germany)

^b UNIVERSITY HOSPITAL BONN   (Germany)

Author keywords

Aptamer; Coagulation; Photo control; SELEX

Indexed keywords

ANTICOAGULANT AGENT; ANTIDOTE; APTAMER; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING INHIBITOR; DESMOPRESSIN; DROTRECOGIN; EGAPTIVON PEGOL; FIBRINOGEN; HD1; HD1 22; HEPARIN; HEPARIN COFACTOR II; LOCKED NUCLEIC ACID; NU172; PEGNIVACOGIN; THROMBIN; TOG25; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

ACUTE CORONARY SYNDROME; ALLERGIC REACTION; ANTICOAGULANT THERAPY; BINDING AFFINITY; BLEEDING; BLOOD CLOTTING; CRYSTAL STRUCTURE; DNA BINDING; DRUG SAFETY; HEMOSTASIS; HUMAN; HYPERSENSITIVITY; IN VIVO STUDY; PERCUTANEOUS CORONARY INTERVENTION; PROTEIN FUNCTION; REVIEW; SEPSIS; THERMOSTABILITY; THROMBOCYTE AGGREGATION; THROMBOTIC THROMBOCYTOPENIC PURPURA; UNSPECIFIED SIDE EFFECT;

ANIMALS; ANTICOAGULANTS; APTAMERS, NUCLEOTIDE; BLOOD COAGULATION; BLOOD COAGULATION FACTORS; DRUG DESIGN; HUMANS; THROMBOSIS;

EID: 83755225854     PISSN: 07209355     EISSN: None     Source Type: Journal    
DOI: 10.5482/ha-1156     Document Type: Review

References (39)

1. Bock LC et al. Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature 1992; 355: 564-566.
2. Padmanabhang K et al. The structure of a thrombin inhibited by a 15-mer single-standed DNA aptamer. J Biol Chem 1993; 268: 17651-17654.
3. Lane DA, Philippou H, Huntington JA. Directing thrombin. Blood 2005; 106: 2605-2612.
4. Kretz CA et al. HD1, a thrombin-directed aptamer, binds exosite 1 on prothrombin with high affinity and inhibits its activation by prothrombinase. J Biol Chem 2006; 281: 37477-37485.
5. Tasset DM, Kubik MK, Steiner W. Oligonucleotide inhibitors of human thrombin that bind distinct epitopes. J Mol Biol 1997; 272: 688-698.
6. Zingali RB et al. Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom. Biochemistry 1993; 32: 10794-10802.
7. Arocas V et al. Bothrojaracin: a potent two-site-directed thrombin inhibitor. Biochemistry 1996; 35: 9083-9089.
8. Müller J et al. Multidomain targeting generates a high-affinity thrombin-inhibiting bivalent aptamer. Chembiochem 2007; 8: 2223-2226.
9. Müller J et al. Anticoagulant characteristics of HD1-22, a bivalent aptamer that specifically inhibits thrombin and prothrombinase. J J Thromb Haemost 2008; 6: 2105-2112.
10. Hasegawa H et al. Improvement of aptamer affinity by dimerization. Sensors 2008; 8: 1090-1098.
11. Kim Y, Cao Z, Tan W. Molecular assembly for highperformance bivalent nucleic acid inhibitor. Proc Natl Acad Sci USA 2008; 105: 5664-5669.
12. Müller J et al. Profiling of in vivo thrombin activity via supramolecular complexes. Ang Chem 2011; 50: 6075-6078.
13. Becker RC et al. Nucleic acid aptamers as antithrombotic agents. Thromb Haemost 2010; 103: 586-595.
14. White R et al. Generation of species cross-reactive aptamers using "toggle" SELEX. Mol Ther 2001; 4: 567-573.
15. Long SB et al. Crystal structure of an RNA aptamer bound to thrombin. RNA 2008; 14: 2504-2512.
16. Kaur H et al. Thermodynamic, counterion, and hydration effects for the incorporation of locked nucleic acid nucleotides into DNA duplexes. Biochemistry 2006; 45: 7347-7355.
17. Virno A et al. A novel thrombin binding aptamer containing a G-LNA residue. Bioorga Med Chem 2007; 15: 5710-5718.
18. Müller J et al. An exosite-specific ssDNA aptamer inhibits the anticoagulant functions of activated protein C and enhances inhibition by protein C inhibitor. Chem Biol 2009; 16: 442-451.
19. Oney S et al. Antidote-controlled platelet inhibition targeting von Willebrand factor with aptamers. Oligonucleotides 2007; 17: 265-274.
20. Oney S et al. Development of universal antidotes to control aptamer activity. Nat Med 2009; 15: 1224-1228.
21. Heckel A, Mayer G. Light regulation of aptamer activity. J Am Chem Soc 2005; 127: 822-823.
22. Mayer G et al. Light-induced formation of G-quadruplex DNA secondary structures. Chembiochem 2005; 6: 1966-1970.
23. Buff MC et al. Dependence of aptamer activity on opposed terminal extensions. Nucleic Acids Res 2010; 38: 2111-2118.
24. Mayer G et al. Differential regulation of protein subdomain activity with caged bivalent ligands. Chembiochem 2009; 10: 654-657.
25. Mayer G et al. From selection to caged aptamers: identification of light-dependent ssDNA aptamers targeting cytohesin. Bioorg Med Chem Lett 2009; 19: 6561-6564.
26. Povsic TJ et al. Translating nucleic acid aptamers to antithrombotic drugs in cardiovascular medicine. J Cardiovasc Transl Res 2010; 3: 704-716.
27. Rusconi CP et al. RNA aptamers as reversible antagonists of coagulation factor IXa. Nature 2002; 419: 90-94.
28. Dyke CK et al. First-in-human experience of an antidote-controlled anticoagulant using RNA aptamer technology. Circulation 2006; 114: 2490-2497.
29. Chan MY, Andreotti F, Becker RC. Hypercoagulable states in cardiovascular disease. Circulation 2008; 118: 2286-2297.
30. Cohen MG et al. First clinical application of an actively reversible direct factor IXa inhibitor as an anticoagulation strategy in patients undergoing percutaneous coronary intervention. Circulation 2010; 122: 614-622.
31. Chan MY et al. A randomized, repeat-dose, pharmacodynamic and safety study of an antidote-controlled factor IXa inhibitor. J Thromb Haemost 2008; 6: 789-796.
32. Chan MY et al. Phase 1b randomized study of antidote-controlled modulation of factor IXa activity in patients with stable coronary artery disease. Circulation 2008; 117: 2865-2874.
33. Hughes S. RADAR: First significant clinical use of novel reversible anticoagulation system. http://www.theheart.org/article/1208729.do 2011
34. Povsic TJ et al. A randomized, partially blinded, multicenter, active-controlled, dose-ranging study assessing the safety, efficacy, and pharmacodynamics of the REG1 anticoagulation system in patients with acute coronary syndromes. Am Heart J 2011; 161: 261-268 e1-2.
35. Gilbert JC et al. First-in-human evaluation of anti von Willebrand factor therapeutic aptamer ARC1779 in healthy volunteers. Circulation 2007; 116: 2678-2686.
36. Jilma B et al. A randomised pilot trial of the antivon Willebrand factor aptamer ARC1779 in patients with type 2b von Willebrand disease. Thromb Haemost 2010; 104: 563-570.
37. Mayr FB et al. The aptamer ARC1779 blocks von Willebrand factor-dependent platelet function in patients with thrombotic thrombocytopenic purpura ex vivo. Transfusion 2010; 50: 1079-1087.
38. Jilma-Stohlawetz P et al. Inhibition of von Willebrand factor by ARC1779 in patients with acute thrombotic thrombocytopenic purpura. Thromb Haemost 2011; 105: 545-552.
39. Gomez-Outes A et al. New parenteral anticoagulants in development. Ther Adv Cardiovasc Dis 2011; 5: 33-59.