10 Aptamers for Thrombotic Diseases
317
102. Muller F, Gailani D, Renne T (2011) Factor XI and XII as antithrombotic targets. Curr Opin
Hematol 18(5):349–355
103. Gailani D, Bane CE, Gruber A (2015) Factor XI and contact activation as targets for
antithrombotic therapy. J Thromb Haemost 13(8):1383–1395
104. Weitz JI (2016) Factor XI and factor XII as targets for new anticoagulants. Thromb Res
141(Suppl 2):S40-45
105. Colman RW, Schmaier AH (1997) Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90(10):3819–
3843
106. Schmaier AH (2008) Assembly, activation, and physiologic influence of the plasma
kallikrein/kinin system. Int Immunopharmacol 8(2):161–165
107. Shariat-Madar Z, Schmaier AH (2004) The plasma kallikrein/kinin and renin angiotensin
systems in blood pressure regulation in sepsis. J Endotoxin Res 10(1):3–13
108. Bjorkqvist J, Jamsa A, Renne T (2013) Plasma kallikrein: the bradykinin-producing enzyme.
Thromb Haemost 110(3):399–407
109. DiScipio RG (1982) The activation of the alternative pathway C3 convertase by human plasma
kallikrein. Immunology 45(3):587–595
110. Steen BKA, Layzer J, Sullenger BA (2017) A kallikrein-targeting RNA aptamer inhibits
the intrinsic pathway of coagulation and reduces bradykinin release. J Thromb Haemost
15(9):1807–1817
111. Schmaier AH (2016) The contact activation and kallikrein/kinin systems: pathophysiologic
and physiologic activities. J Thromb Haemost 14(1):28–39
112. Bjorkqvist J, Sala-Cunill A, Renne T (2013) Hereditary angioedema: a bradykinin-mediated
swelling disorder. Thromb Haemost 109(3):368–374
113. Linkins LA, Choi PT, Douketis JD (2003) Clinical impact of bleeding in patients taking
oral anticoagulant therapy for venous thromboembolism: a meta-analysis. Ann Intern Med
139(11):893–900
114. Butcher EC (1991) Leukocyte-endothelial cell recognition: three (or more) steps to specificity
and diversity. Cell 67(6):1033–1036
115. Lasky LA (1992) Selectins: interpreters of cell-specific carbohydrate information during
inflammation. Science 258(5084):964–969
116. Foxall C, Watson SR, Dowbenko D, Fennie C, Lasky LA, Kiso M, Hasegawa A, Asa D,
Brandley BK (1992) The three members of the selectin receptor family recognize a common
carbohydrate epitope, the sialyl Lewis(x) oligosaccharide. J Cell Biol 117(4):895–902
117. Jenison RD, Jennings SD, Walker DW, Bargatze RF, Parma D (1998) Oligonucleotide
inhibitors of P-selectin-dependent neutrophil-platelet adhesion. Antisense Nucleic Acid Drug
Dev 8(4):265–279
118. Nimjee SM, Lohrmann JD, Wang H, Snyder DJ, Cummings TJ, Becker RC, Oney S, Sullenger
BA (2012) Rapidly regulating platelet activity in vivo with an antidote controlled platelet
inhibitor. Mol Ther 20(2):391–397
119. Hekman CM, Loskutoff DJ (1987) Fibrinolytic pathways and the endothelium. Semin Thromb
Hemost 13(4):514–527
120. Conway DS, Pearce LA, Chin BS, Hart RG, Lip GY (2003) Prognostic value of plasma
von Willebrand factor and soluble P-selectin as indices of endothelial damage and platelet
activation in 994 patients with nonvalvular atrial fibrillation. Circulation 107(25):3141–3145
121. Wu D, Vanhoorelbeke K, Cauwenberghs N, Meiring M, Depraetere H, Kotze HF, Deckmyn H
(2002) Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF
monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in
baboons. Blood 99(10):3623–3628
122. Cadroy Y, Hanson SR, Kelly AB, Marzec UM, Evatt BL, Kunicki TJ, Montgomery RR, Harker
LA (1994) Relative antithrombotic effects of monoclonal antibodies targeting different platelet
glycoprotein-adhesive molecule interactions in nonhuman primates. Blood 83(11):3218–3224
123. Huang RH, Fremont DH, Diener JL, Schaub RG, Sadler JE (2009) A structural explanation
for the antithrombotic activity of ARC1172, a DNA aptamer that binds von Willebrand factor
domain A1. Structure 17(11):1476–1484
317
102. Muller F, Gailani D, Renne T (2011) Factor XI and XII as antithrombotic targets. Curr Opin
Hematol 18(5):349–355
103. Gailani D, Bane CE, Gruber A (2015) Factor XI and contact activation as targets for
antithrombotic therapy. J Thromb Haemost 13(8):1383–1395
104. Weitz JI (2016) Factor XI and factor XII as targets for new anticoagulants. Thromb Res
141(Suppl 2):S40-45
105. Colman RW, Schmaier AH (1997) Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90(10):3819–
3843
106. Schmaier AH (2008) Assembly, activation, and physiologic influence of the plasma
kallikrein/kinin system. Int Immunopharmacol 8(2):161–165
107. Shariat-Madar Z, Schmaier AH (2004) The plasma kallikrein/kinin and renin angiotensin
systems in blood pressure regulation in sepsis. J Endotoxin Res 10(1):3–13
108. Bjorkqvist J, Jamsa A, Renne T (2013) Plasma kallikrein: the bradykinin-producing enzyme.
Thromb Haemost 110(3):399–407
109. DiScipio RG (1982) The activation of the alternative pathway C3 convertase by human plasma
kallikrein. Immunology 45(3):587–595
110. Steen BKA, Layzer J, Sullenger BA (2017) A kallikrein-targeting RNA aptamer inhibits
the intrinsic pathway of coagulation and reduces bradykinin release. J Thromb Haemost
15(9):1807–1817
111. Schmaier AH (2016) The contact activation and kallikrein/kinin systems: pathophysiologic
and physiologic activities. J Thromb Haemost 14(1):28–39
112. Bjorkqvist J, Sala-Cunill A, Renne T (2013) Hereditary angioedema: a bradykinin-mediated
swelling disorder. Thromb Haemost 109(3):368–374
113. Linkins LA, Choi PT, Douketis JD (2003) Clinical impact of bleeding in patients taking
oral anticoagulant therapy for venous thromboembolism: a meta-analysis. Ann Intern Med
139(11):893–900
114. Butcher EC (1991) Leukocyte-endothelial cell recognition: three (or more) steps to specificity
and diversity. Cell 67(6):1033–1036
115. Lasky LA (1992) Selectins: interpreters of cell-specific carbohydrate information during
inflammation. Science 258(5084):964–969
116. Foxall C, Watson SR, Dowbenko D, Fennie C, Lasky LA, Kiso M, Hasegawa A, Asa D,
Brandley BK (1992) The three members of the selectin receptor family recognize a common
carbohydrate epitope, the sialyl Lewis(x) oligosaccharide. J Cell Biol 117(4):895–902
117. Jenison RD, Jennings SD, Walker DW, Bargatze RF, Parma D (1998) Oligonucleotide
inhibitors of P-selectin-dependent neutrophil-platelet adhesion. Antisense Nucleic Acid Drug
Dev 8(4):265–279
118. Nimjee SM, Lohrmann JD, Wang H, Snyder DJ, Cummings TJ, Becker RC, Oney S, Sullenger
BA (2012) Rapidly regulating platelet activity in vivo with an antidote controlled platelet
inhibitor. Mol Ther 20(2):391–397
119. Hekman CM, Loskutoff DJ (1987) Fibrinolytic pathways and the endothelium. Semin Thromb
Hemost 13(4):514–527
120. Conway DS, Pearce LA, Chin BS, Hart RG, Lip GY (2003) Prognostic value of plasma
von Willebrand factor and soluble P-selectin as indices of endothelial damage and platelet
activation in 994 patients with nonvalvular atrial fibrillation. Circulation 107(25):3141–3145
121. Wu D, Vanhoorelbeke K, Cauwenberghs N, Meiring M, Depraetere H, Kotze HF, Deckmyn H
(2002) Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF
monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in
baboons. Blood 99(10):3623–3628
122. Cadroy Y, Hanson SR, Kelly AB, Marzec UM, Evatt BL, Kunicki TJ, Montgomery RR, Harker
LA (1994) Relative antithrombotic effects of monoclonal antibodies targeting different platelet
glycoprotein-adhesive molecule interactions in nonhuman primates. Blood 83(11):3218–3224
123. Huang RH, Fremont DH, Diener JL, Schaub RG, Sadler JE (2009) A structural explanation
for the antithrombotic activity of ARC1172, a DNA aptamer that binds von Willebrand factor
domain A1. Structure 17(11):1476–1484