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Volumn 111, Issue 4, 2014, Pages 590-597

Synergies of phosphatidylserine and protein disulfide isomerase in tissue factor activation

Author keywords

Phosphatidylserine; Protein disulfide isomerase; Thioldisulfide exchange; Thrombosis; Tissue factor

Indexed keywords

ADENOSINE TRIPHOSPHATE; DISULFIDE; PHOSPHATIDYLSERINE; PROTEIN DISULFIDE ISOMERASE; PURINERGIC P2X7 RECEPTOR; THIOL; THROMBIN; THROMBOPLASTIN; CARBOXYLYASE; LYMPHOCYTE ANTIBODY; PHOSPHATIDYLSERINE DECARBOXYLASE;

EID: 84897497741     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH13-09-0802     Document Type: Article
Times cited : (83)

References (97)
  • 1
    • 22944462705 scopus 로고    scopus 로고
    • Defective thrombus formation in mice lacking coagulation factor XII
    • Renné T, Pozgajová M, Grüner S, et al. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med 2005; 202: 271-281.
    • (2005) J Exp Med , vol.202 , pp. 271-281
    • Renné, T.1    Pozgajová, M.2    Grüner, S.3
  • 2
    • 33644511050 scopus 로고    scopus 로고
    • Tissue factor in hemostasis and thrombosis
    • Tilley R, Mackman N. Tissue factor in hemostasis and thrombosis. Semin Thromb Hemost 2006; 32: 5-10.
    • (2006) Semin Thromb Hemost , vol.32 , pp. 5-10
    • Tilley, R.1    McKman, N.2
  • 3
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis
    • Drake TA, Morrissey JH, Edgington TS. Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am J Pathol 1989; 134: 1087-1097.
    • (1989) Am J Pathol , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrissey, J.H.2    Edgington, T.S.3
  • 4
    • 84870561561 scopus 로고    scopus 로고
    • Role of tissue factor in atherothrombosis
    • Owens AP 3rd, Mackman N. Role of tissue factor in atherothrombosis. Curr Atheroscler Rep 2012; 14: 394-401.
    • (2012) Curr Atheroscler Rep , vol.14 , pp. 394-401
    • Owens III, A.P.1    McKman, N.2
  • 5
    • 48449101517 scopus 로고    scopus 로고
    • Circulating tissue factor-exposing microparticles
    • Lechner D, Weltermann A. Circulating tissue factor-exposing microparticles. Thromb Res 2008; 122 (Suppl 1): S47-S54.
    • (2008) Thromb Res , vol.122 , Issue.SUPPL. 1
    • Lechner, D.1    Weltermann, A.2
  • 6
    • 77954396958 scopus 로고    scopus 로고
    • Disseminated intravascular coagulation in trauma injuries
    • Lippi G, Cervellin G. Disseminated intravascular coagulation in trauma injuries. Semin Thromb Hemost 2010; 36: 378-387.
    • (2010) Semin Thromb Hemost , vol.36 , pp. 378-387
    • Lippi, G.1    Cervellin, G.2
  • 7
    • 84863085792 scopus 로고    scopus 로고
    • Infection and inflammation as risk factors for thrombosis and atherosclerosis
    • Levi M, van der Poll T, Schultz M. Infection and inflammation as risk factors for thrombosis and atherosclerosis. Semin Thromb Hemost 2012; 38: 506-514.
    • (2012) Semin Thromb Hemost , vol.38 , pp. 506-514
    • Levi, M.1    van der Poll, T.2    Schultz, M.3
  • 8
    • 84863463096 scopus 로고    scopus 로고
    • Crosstalk between cancer and haemostasis. Implications for cancer biology and cancer-associated thrombosis with focus on tissue factor
    • Langer F, Bokemeyer C. Crosstalk between cancer and haemostasis. Implications for cancer biology and cancer-associated thrombosis with focus on tissue factor. Hamostaseologie 2012; 32: 95-104.
    • (2012) Hamostaseologie , vol.32 , pp. 95-104
    • Langer, F.1    Bokemeyer, C.2
  • 9
    • 70449596043 scopus 로고    scopus 로고
    • The role of monocytes in thrombotic disorders. Insights from tissue factor, monocyte-platelet aggregates and novel mechanisms
    • Shantsila E, Lip GY. The role of monocytes in thrombotic disorders. Insights from tissue factor, monocyte-platelet aggregates and novel mechanisms. Thromb Haemost 2009; 102: 916-924.
    • (2009) Thromb Haemost , vol.102 , pp. 916-924
    • Shantsila, E.1    Lip, G.Y.2
  • 10
    • 77956291941 scopus 로고    scopus 로고
    • Hematopoietic and nonhematopoietic cell tissue factor activates the coagulation cascade in endotoxemic mice
    • Pawlinski R, Wang JG, Owens AP 3rd, et al. Hematopoietic and nonhematopoietic cell tissue factor activates the coagulation cascade in endotoxemic mice. Blood 2010; 116: 806-814.
    • (2010) Blood , vol.116 , pp. 806-814
    • Pawlinski, R.1    Wang, J.G.2    Owens III, A.P.3
  • 11
    • 34249821918 scopus 로고    scopus 로고
    • Stimulation of P2 (P2X7) receptors in human dendritic cells induces the release of tissue factor-bearing microparticles
    • Baroni M, Pizzirani C, Pinotti M, et al. Stimulation of P2 (P2X7) receptors in human dendritic cells induces the release of tissue factor-bearing microparticles. FASEB J 2007; 21: 1926-1933.
    • (2007) FASEB J , vol.21 , pp. 1926-1933
    • Baroni, M.1    Pizzirani, C.2    Pinotti, M.3
  • 12
    • 55549102694 scopus 로고    scopus 로고
    • Monocyte-derived microparticles and exosomes induce procoagulant and apoptotic effects on endothelial cells
    • Aharon A, Tamari T, Brenner B. Monocyte-derived microparticles and exosomes induce procoagulant and apoptotic effects on endothelial cells. Thromb Haemost 2008; 100: 878-885.
    • (2008) Thromb Haemost , vol.100 , pp. 878-885
    • Aharon, A.1    Tamari, T.2    Brenner, B.3
  • 13
    • 79960019927 scopus 로고    scopus 로고
    • P2X7 receptor signaling contributes to tissue factor-dependent thrombosis in mice
    • Furlan-Freguia C, Marchese P, Gruber A, et al. P2X7 receptor signaling contributes to tissue factor-dependent thrombosis in mice. J Clin Invest 2011; 121: 2932-2944.
    • (2011) J Clin Invest , vol.121 , pp. 2932-2944
    • Furlan-Freguia, C.1    Marchese, P.2    Gruber, A.3
  • 14
    • 84861097186 scopus 로고    scopus 로고
    • Evidence for direct transfer of tissue factor from monocytes to platelets in whole blood
    • Sovershaev MA, Egorina EM, Osterud B, et al. Evidence for direct transfer of tissue factor from monocytes to platelets in whole blood. Blood Coagul Fibrinolysis 2012; 23: 345-350.
    • (2012) Blood Coagul Fibrinolysis , vol.23 , pp. 345-350
    • Sovershaev, M.A.1    Egorina, E.M.2    Osterud, B.3
  • 15
    • 23944509766 scopus 로고    scopus 로고
    • Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation
    • Del Conde I, Shrimpton CN, Thiagarajan P, et al. Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation. Blood 2005; 106: 1604-1611.
    • (2005) Blood , vol.106 , pp. 1604-1611
    • Del Conde, I.1    Shrimpton, C.N.2    Thiagarajan, P.3
  • 16
    • 66349098390 scopus 로고    scopus 로고
    • Inferior vena cava ligation rapidly induces tissue factor expression and venous thrombosis in rats
    • Zhou J, May L, Liao P, et al. Inferior vena cava ligation rapidly induces tissue factor expression and venous thrombosis in rats. Arterioscler Thromb Vasc Biol 2009; 29: 863-869.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 863-869
    • Zhou, J.1    May, L.2    Liao, P.3
  • 17
    • 84866144650 scopus 로고    scopus 로고
    • Tissue factor-positive neutrophils bind to injured endothelial wall and initiate thrombus formation
    • Darbousset R, Thomas GM, Mezouar S, et al. Tissue factor-positive neutrophils bind to injured endothelial wall and initiate thrombus formation. Blood 2012; 120: 2133-2143.
    • (2012) Blood , vol.120 , pp. 2133-2143
    • Darbousset, R.1    Thomas, G.M.2    Mezouar, S.3
  • 18
    • 84861750668 scopus 로고    scopus 로고
    • Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo
    • von Brühl ML, Stark K, Steinhart A, et al. Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo. J Exp Med 2012; 209: 819-835.
    • (2012) J Exp Med , vol.209 , pp. 819-835
    • von Brühl, M.L.1    Stark, K.2    Steinhart, A.3
  • 19
    • 84880616430 scopus 로고    scopus 로고
    • Crossroads of coagulation and innate immunity: The case of deep vein thrombosis
    • Schulz C, Engelmann B, Massberg S. Crossroads of coagulation and innate immunity: the case of deep vein thrombosis. J Thromb Haemost 2013; 11 (Suppl 1): 233-241.
    • (2013) J Thromb Haemost , vol.11 , Issue.SUPPL. 1 , pp. 233-241
    • Schulz, C.1    Engelmann, B.2    Massberg, S.3
  • 20
    • 0027530837 scopus 로고
    • The expression of tissue factor antigen and activity on the surface of leukemic cells
    • Tanaka M, Yamanishi H. The expression of tissue factor antigen and activity on the surface of leukemic cells. Leuk Res 1993; 17: 103-111.
    • (1993) Leuk Res , vol.17 , pp. 103-111
    • Tanaka, M.1    Yamanishi, H.2
  • 21
    • 0024382713 scopus 로고
    • Functional tissue factor is entirely cell surface expressed on lipopolysaccharide-stimulated human blood monocytes and a constitutively tissue factor-producing neoplastic cell line
    • Drake TA, Ruf W, Morrissey JH, et al. Functional tissue factor is entirely cell surface expressed on lipopolysaccharide-stimulated human blood monocytes and a constitutively tissue factor-producing neoplastic cell line. J Cell Biol 1989; 109: 389-395.
    • (1989) J Cell Biol , vol.109 , pp. 389-395
    • Drake, T.A.1    Ruf, W.2    Morrissey, J.H.3
  • 22
    • 9144266359 scopus 로고    scopus 로고
    • An in vitro study on the mechanisms of coagulation activation in acute myelogenous leukemia (AML): Role of tissue factor regulation by cytotoxic drugs and GM-CSF
    • Langer F, Amirkhosravi A, Loges S, et al. An in vitro study on the mechanisms of coagulation activation in acute myelogenous leukemia (AML): role of tissue factor regulation by cytotoxic drugs and GM-CSF. Thromb Haemost 2004; 92: 1136-1146.
    • (2004) Thromb Haemost , vol.92 , pp. 1136-1146
    • Langer, F.1    Amirkhosravi, A.2    Loges, S.3
  • 23
    • 0027161502 scopus 로고
    • Disseminated intravascular coagulation in a patient with acute myeloid leukemia. Ultrastructural evidence of hypercoagulation in bone marrow
    • Takemori N, Hirai K, Onodera R, et al. Disseminated intravascular coagulation in a patient with acute myeloid leukemia. Ultrastructural evidence of hypercoagulation in bone marrow. Am J Clin Pathol 1993; 99: 695-701.
    • (1993) Am J Clin Pathol , vol.99 , pp. 695-701
    • Takemori, N.1    Hirai, K.2    Onodera, R.3
  • 24
    • 0031005422 scopus 로고    scopus 로고
    • Mechanism of tissue factor activation on HL-60 cells
    • Bach RR, Moldow CF. Mechanism of tissue factor activation on HL-60 cells. Blood 1997; 89: 3270-3276.
    • (1997) Blood , vol.89 , pp. 3270-3276
    • Bach, R.R.1    Moldow, C.F.2
  • 25
    • 0019957155 scopus 로고
    • Binding of human factor VII and VIIa to monocytes
    • Broze GJ Jr. Binding of human factor VII and VIIa to monocytes. J Clin Invest 1982; 70: 526-535.
    • (1982) J Clin Invest , vol.70 , pp. 526-535
    • Broze Jr., G.J.1
  • 26
    • 0023258597 scopus 로고
    • Cooperative interaction between factor VII and cell surface-expressed tissue factor
    • Fair DS, MacDonald MJ. Cooperative interaction between factor VII and cell surface-expressed tissue factor. J Biol Chem 1987; 262: 11692-11698.
    • (1987) J Biol Chem , vol.262 , pp. 11692-11698
    • Fair, D.S.1    McDonald, M.J.2
  • 27
    • 0024345543 scopus 로고
    • Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation
    • Sakai T, Lund-Hansen T, Paborsky L, et al. Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation. J Biol Chem 1989; 264: 9980-9988.
    • (1989) J Biol Chem , vol.264 , pp. 9980-9988
    • Sakai, T.1    Lund-Hansen, T.2    Paborsky, L.3
  • 28
    • 0026650453 scopus 로고
    • Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces
    • Le DT, Rapaport SI, Rao LV. Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces. J Biol Chem 1992; 267: 15447-15454.
    • (1992) J Biol Chem , vol.267 , pp. 15447-15454
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.3
  • 29
    • 0030991982 scopus 로고    scopus 로고
    • Incorporation of an active site inhibitor in factor VIIa alters the affinity for tissue factor
    • Sorensen BB, Persson E, Freskgârd PO, et al. Incorporation of an active site inhibitor in factor VIIa alters the affinity for tissue factor. J Biol Chem 1997; 272: 11863-11868.
    • (1997) J Biol Chem , vol.272 , pp. 11863-11868
    • Sorensen, B.B.1    Persson, E.2    Freskgârd, P.O.3
  • 30
    • 0034640499 scopus 로고    scopus 로고
    • Factor VIIa and thrombin induce the expression of Cyr61 and connective tissue growth factor, extracellular matrix signaling proteins that could act as possible downstream mediators in factor VIIa x tissue factor-induced signal transduction
    • Pendurthi UR, Allen KE, Ezban M, et al. Factor VIIa and thrombin induce the expression of Cyr61 and connective tissue growth factor, extracellular matrix signaling proteins that could act as possible downstream mediators in factor VIIa x tissue factor-induced signal transduction. J Biol Chem 2000; 275: 14632-14641.
    • (2000) J Biol Chem , vol.275 , pp. 14632-14641
    • Pendurthi, U.R.1    Allen, K.E.2    Ezban, M.3
  • 31
    • 84868156108 scopus 로고    scopus 로고
    • Regulation of tissue factor coagulant activity on cell surfaces
    • Rao LV, Pendurthi UR. Regulation of tissue factor coagulant activity on cell surfaces. J Thromb Haemost 2012; 10: 2242-2253.
    • (2012) J Thromb Haemost , vol.10 , pp. 2242-2253
    • Rao, L.V.1    Pendurthi, U.R.2
  • 32
    • 84886730888 scopus 로고    scopus 로고
    • Encryption and decryption of tissue factor
    • Chen VM, Hogg PJ. Encryption and decryption of tissue factor. J Thromb Haemost 2013; 11 (Suppl 1): 277-284.
    • (2013) J Thromb Haemost , vol.11 , Issue.SUPPL. 1 , pp. 277-284
    • Chen, V.M.1    Hogg, P.J.2
  • 33
    • 84880399802 scopus 로고    scopus 로고
    • Analysis of tissue factor expression in various cell model systems: Cryptic vs. active
    • Kothari H, Pendurthi UR, Rao LV. Analysis of tissue factor expression in various cell model systems: cryptic vs. active. J Thromb Haemost 2013; 11: 1353-1363.
    • (2013) J Thromb Haemost , vol.11 , pp. 1353-1363
    • Kothari, H.1    Pendurthi, U.R.2    Rao, L.V.3
  • 34
    • 33748992850 scopus 로고    scopus 로고
    • Disulfide isomerisation switches tissue factor from coagulation to cell signaling
    • Ahamed J, Versteeg HH, Kerver M, et al. Disulfide isomerisation switches tissue factor from coagulation to cell signaling. Proc Natl Acad Sci USA 2006; 103: 13932-13937.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13932-13937
    • Ahamed, J.1    Versteeg, H.H.2    Kerver, M.3
  • 35
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium
    • Bach R, Rifkin DB. Expression of tissue factor procoagulant activity: regulation by cytosolic calcium. Proc Natl Acad Sci USA 1990; 87: 6995-6999.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6995-6999
    • Bach, R.1    Rifkin, D.B.2
  • 37
    • 0008103207 scopus 로고    scopus 로고
    • Tissue factor de-encryption: Ionophore treatment induces changes in tissue factor activity by phosphatidylserinedependent and-independent mechanisms
    • Wolberg AS, Monroe DM, Roberts HR, et al. Tissue factor de-encryption: ionophore treatment induces changes in tissue factor activity by phosphatidylserinedependent and-independent mechanisms. Blood Coagul Fibrinolysis 1999; 10: 201-210.
    • (1999) Blood Coagul Fibrinolysis , vol.10 , pp. 201-210
    • Wolberg, A.S.1    Monroe, D.M.2    Roberts, H.R.3
  • 38
    • 0028884030 scopus 로고
    • Phosphatidylethanolamine augments factor VIIa-tissue factor activity: Enhancement of sensitivity to phosphatidylserine
    • Neuenschwander PF, Bianco-Fisher E, Rezaie AR, et al. Phosphatidylethanolamine augments factor VIIa-tissue factor activity: enhancement of sensitivity to phosphatidylserine. Biochemistry 1995; 34: 13988-13993.
    • (1995) Biochemistry , vol.34 , pp. 13988-13993
    • Neuenschwander, P.F.1    Bianco-Fisher, E.2    Rezaie, A.R.3
  • 39
    • 79959548059 scopus 로고    scopus 로고
    • Molecular determinants of phospholipid synergy in blood clotting
    • Tavoosi N, Davis-Harrison RL, Pogorelov TV, et al. Molecular determinants of phospholipid synergy in blood clotting. J Biol Chem 2011; 286: 23247-23253.
    • (2011) J Biol Chem , vol.286 , pp. 23247-23253
    • Tavoosi, N.1    Davis-Harrison, R.L.2    Pogorelov, T.V.3
  • 40
    • 29244486444 scopus 로고    scopus 로고
    • Discrepancy between tissue factor activity and tissue factor expression in endotoxin-induced monocytes is associated with apoptosis and necrosis
    • Henriksson CE, Klingenberg O, Ovstebø R, et al. Discrepancy between tissue factor activity and tissue factor expression in endotoxin-induced monocytes is associated with apoptosis and necrosis. Thromb Haemost 2005; 94: 1236-1244.
    • (2005) Thromb Haemost , vol.94 , pp. 1236-1244
    • Henriksson, C.E.1    Klingenberg, O.2    Ovstebø, R.3
  • 41
    • 0025330312 scopus 로고
    • Consecutive enzyme cascades: Complement activation at the cell surface triggers increased tissue factor activity
    • Carson SD, Johnson DR. Consecutive enzyme cascades: complement activation at the cell surface triggers increased tissue factor activity. Blood 1990; 76: 361-367.
    • (1990) Blood , vol.76 , pp. 361-367
    • Carson, S.D.1    Johnson, D.R.2
  • 42
    • 84855879112 scopus 로고    scopus 로고
    • Anthracycline treatment of the human monocytic leukemia cell line THP-1 increases phosphatidylserine exposure and tissue factor activity
    • Boles JC, Williams JC, Hollingsworth RM, et al. Anthracycline treatment of the human monocytic leukemia cell line THP-1 increases phosphatidylserine exposure and tissue factor activity. Thromb Res 2012; 129: 197-203.
    • (2012) Thromb Res , vol.129 , pp. 197-203
    • Boles, J.C.1    Williams, J.C.2    Hollingsworth, R.M.3
  • 43
    • 33748089036 scopus 로고    scopus 로고
    • Lactadherin binding and phosphatidylserine expression on cell surface-comparison with annexin A5
    • Dasgupta SK, Guchhait P, Thiagarajan P. Lactadherin binding and phosphatidylserine expression on cell surface-comparison with annexin A5. Transl Res 2006; 148: 19-25.
    • (2006) Transl Res , vol.148 , pp. 19-25
    • Dasgupta, S.K.1    Guchhait, P.2    Thiagarajan, P.3
  • 44
    • 33845929582 scopus 로고    scopus 로고
    • Lactadherin detects early phosphatidylserine exposure on immortalized leukemia cells undergoing programmed cell death
    • Shi J, Shi Y, Waehrens LN, et al. Lactadherin detects early phosphatidylserine exposure on immortalized leukemia cells undergoing programmed cell death. Cytometry A 2006; 69: 1193-1201.
    • (2006) Cytometry A , vol.69 , pp. 1193-1201
    • Shi, J.1    Shi, Y.2    Waehrens, L.N.3
  • 45
    • 0034616668 scopus 로고    scopus 로고
    • Deencryption of cellular tissue factor is independent of its cytoplasmic domain
    • Wolberg AS, Kon RH, Monroe DM, et al. Deencryption of cellular tissue factor is independent of its cytoplasmic domain. Biochem Biophys Res Commun 2000; 272: 332-336.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 332-336
    • Wolberg, A.S.1    Kon, R.H.2    Monroe, D.M.3
  • 46
    • 33749366436 scopus 로고    scopus 로고
    • Evidence for activation of tissue factor by an allosteric disulfide bond
    • Chen VM, Ahamed J, Versteeg HH, et al. Evidence for activation of tissue factor by an allosteric disulfide bond. Biochemistry 2006; 45: 12020-12028.
    • (2006) Biochemistry , vol.45 , pp. 12020-12028
    • Chen, V.M.1    Ahamed, J.2    Versteeg, H.H.3
  • 47
    • 0028643608 scopus 로고
    • Studies of the mechanism for enhanced cell surface factor VIIa/tissue factor activation of factor X on fibroblast monolayers after their exposure to N-ethylmaleimide
    • Le DT, Rapaport SI, Rao LV. Studies of the mechanism for enhanced cell surface factor VIIa/tissue factor activation of factor X on fibroblast monolayers after their exposure to N-ethylmaleimide. Thromb Haemost 1994; 72: 848-855.
    • (1994) Thromb Haemost , vol.72 , pp. 848-855
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.3
  • 48
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf W, Schullek JR, Stone MJ, et al. Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry 1994; 33: 1565-1572.
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3
  • 49
    • 77951884050 scopus 로고    scopus 로고
    • Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance
    • Sen P, Neuenschwander PF, Pendurthi UR, et al. Analysis of factor VIIa binding to relipidated tissue factor by surface plasmon resonance. Blood Coagul Fibrinolysis 2010; 21: 376-379.
    • (2010) Blood Coagul Fibrinolysis , vol.21 , pp. 376-379
    • Sen, P.1    Neuenschwander, P.F.2    Pendurthi, U.R.3
  • 50
    • 77953786929 scopus 로고    scopus 로고
    • Dynamical view of membrane binding and complex formation of human factor VIIa and tissue factor
    • Ohkubo YZ, Morrissey JH, Tajkhorshid E. Dynamical view of membrane binding and complex formation of human factor VIIa and tissue factor. J Thromb Haemost 2010; 8: 1044-1053.
    • (2010) J Thromb Haemost , vol.8 , pp. 1044-1053
    • Ohkubo, Y.Z.1    Morrissey, J.H.2    Tajkhorshid, E.3
  • 51
    • 0026733665 scopus 로고
    • Cofactor residues lysine 165 and 166 are critical for protein substrate recognition by the tissue factor-factor VIIa protease complex
    • Ruf W, Miles DJ, Rehemtulla A, et al. Cofactor residues lysine 165 and 166 are critical for protein substrate recognition by the tissue factor-factor VIIa protease complex. J Biol Chem 1992; 267: 6375-6381.
    • (1992) J Biol Chem , vol.267 , pp. 6375-6381
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3
  • 52
    • 0026540132 scopus 로고
    • Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII
    • Ruf W, Miles DJ, Rehemtulla A, et al. Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and factor VII. J Biol Chem 1992; 267: 22206-22210.
    • (1992) J Biol Chem , vol.267 , pp. 22206-22210
    • Ruf, W.1    Miles, D.J.2    Rehemtulla, A.3
  • 53
    • 33750985704 scopus 로고    scopus 로고
    • Allosteric disulfide bonds in thrombosis and thrombolysis
    • Chen VM, Hogg PJ. Allosteric disulfide bonds in thrombosis and thrombolysis. J Thromb Haemost 2006; 4: 2533-2541.
    • (2006) J Thromb Haemost , vol.4 , pp. 2533-2541
    • Chen, V.M.1    Hogg, P.J.2
  • 54
    • 79960282808 scopus 로고    scopus 로고
    • Redox properties of the tissue factor Cys186-Cys209 disulfide bond
    • Liang HP, Brophy TM, Hogg PJ. Redox properties of the tissue factor Cys186-Cys209 disulfide bond. Biochem J 2011; 437: 455-460.
    • (2011) Biochem J , vol.437 , pp. 455-460
    • Liang, H.P.1    Brophy, T.M.2    Hogg, P.J.3
  • 55
    • 40549121595 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation
    • Reinhardt C, von Brühl ML, Manukyan D, et al. Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J Clin Invest 2008; 118: 1110-1122.
    • (2008) J Clin Invest , vol.118 , pp. 1110-1122
    • Reinhardt, C.1    von Brühl, M.L.2    Manukyan, D.3
  • 56
    • 77955907854 scopus 로고    scopus 로고
    • Tissue factor mutated at the allosteric Cys186-Cys209 disulfide bond is severely impaired in decrypted procoagulant activity
    • Ruf W, Versteeg HH. Tissue factor mutated at the allosteric Cys186-Cys209 disulfide bond is severely impaired in decrypted procoagulant activity. Blood 2010; 116: 500-501.
    • (2010) Blood , vol.116 , pp. 500-501
    • Ruf, W.1    Versteeg, H.H.2
  • 57
    • 80053216002 scopus 로고    scopus 로고
    • Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue factor
    • van den Hengel LG, Kocatürk B, Reitsma PH, et al. Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue factor. Blood 2011; 118: 3446-3448.
    • (2011) Blood , vol.118 , pp. 3446-3448
    • van den Hengel, L.G.1    Kocatürk, B.2    Reitsma, P.H.3
  • 58
    • 84868112365 scopus 로고    scopus 로고
    • Murine tissue factor coagulant activity is critically dependent on the presence of an intact allosteric disulfide
    • van den Hengel LG, Osanto S, Reitsma PH, et al. Murine tissue factor coagulant activity is critically dependent on the presence of an intact allosteric disulfide. Haematologica 2013; 98: 153-158.
    • (2013) Haematologica , vol.98 , pp. 153-158
    • van den Hengel, L.G.1    Osanto, S.2    Reitsma, P.H.3
  • 59
    • 84875999635 scopus 로고    scopus 로고
    • Disulfide reduction abolishes tissue factor cofactor function
    • Krudysz-Amblo J, Jennings ME 2nd, Knight T, et al. Disulfide reduction abolishes tissue factor cofactor function. Biochim Biophys Acta 2013; 1830: 3489-3496.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 3489-3496
    • Krudysz-Amblo, J.1    Jennings II, M.E.2    Knight, T.3
  • 60
    • 77953625529 scopus 로고    scopus 로고
    • Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its de-encryption
    • Kothari H, Nayak RC, Rao LV, et al. Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its de-encryption. Blood 2010; 115: 4273-4283.
    • (2010) Blood , vol.115 , pp. 4273-4283
    • Kothari, H.1    Nayak, R.C.2    Rao, L.V.3
  • 61
    • 73849123856 scopus 로고    scopus 로고
    • What is wrong with the allosteric disulfide bond hypothesis?
    • Bach RR, Monroe D. What is wrong with the allosteric disulfide bond hypothesis? Arterioscler Thromb Vasc Biol 2009; 29: 1997-1998.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1997-1998
    • Bach, R.R.1    Monroe, D.2
  • 62
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner DW, D'Arcy A, Chène C, et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 1996; 380: 41-46.
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chène, C.3
  • 63
    • 33747702876 scopus 로고    scopus 로고
    • High resolution structures of p-aminobenzamidine-and benzamidine-VIIa/soluble tissue factor: Unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa
    • Bajaj SP, Schmidt AE, Agah S, et al. High resolution structures of p-aminobenzamidine-and benzamidine-VIIa/soluble tissue factor: unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa. J Biol Chem 2006; 281: 24873-24888.
    • (2006) J Biol Chem , vol.281 , pp. 24873-24888
    • Bajaj, S.P.1    Schmidt, A.E.2    Agah, S.3
  • 64
    • 0029062944 scopus 로고
    • Energetic contributions and topographical organisation of ligand binding residues of tissue factor
    • Ruf W, Kelly CR, Schullek JR, et al. Energetic contributions and topographical organisation of ligand binding residues of tissue factor. Biochemistry 1995; 34: 6310-6315.
    • (1995) Biochemistry , vol.34 , pp. 6310-6315
    • Ruf, W.1    Kelly, C.R.2    Schullek, J.R.3
  • 65
    • 0028019121 scopus 로고
    • Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis
    • Gibbs C, McCurdy S, Leung L, et al. Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis. Biochemistry 1994; 33: 14003-14010.
    • (1994) Biochemistry , vol.33 , pp. 14003-14010
    • Gibbs, C.1    McCurdy, S.2    Leung, L.3
  • 66
    • 0025925360 scopus 로고
    • Characterisation of factor VII association with tissue factor in solution. High and low affinity calcium binding sites in factor VII contribute to functionally distinct interactions
    • Ruf W, Kalnik MW, Lund-Hansen T, et al. Characterisation of factor VII association with tissue factor in solution. High and low affinity calcium binding sites in factor VII contribute to functionally distinct interactions. J Biol Chem 1991; 266: 15719-15725.
    • (1991) J Biol Chem , vol.266 , pp. 15719-15725
    • Ruf, W.1    Kalnik, M.W.2    Lund-Hansen, T.3
  • 67
    • 0032488808 scopus 로고    scopus 로고
    • The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF-5G9 complex
    • Huang M, Syed R, Stura EA, et al. The mechanism of an inhibitory antibody on TF-initiated blood coagulation revealed by the crystal structures of human tissue factor, Fab 5G9 and TF-5G9 complex. J Mol Biol 1998; 275: 873-894.
    • (1998) J Mol Biol , vol.275 , pp. 873-894
    • Huang, M.1    Syed, R.2    Stura, E.A.3
  • 68
    • 84877930702 scopus 로고    scopus 로고
    • Rapid activation of monocyte tissue factor by antithymocyte globulin is dependent on complement and protein disulfide isomerase
    • Langer F, Spath B, Fischer C, et al. Rapid activation of monocyte tissue factor by antithymocyte globulin is dependent on complement and protein disulfide isomerase. Blood 2013; 121: 2324-2335.
    • (2013) Blood , vol.121 , pp. 2324-2335
    • Langer, F.1    Spath, B.2    Fischer, C.3
  • 69
    • 37049001668 scopus 로고    scopus 로고
    • Tissue factor activation: Is disulfide bond switching a regulatory mechanism?
    • Pendurthi UR, Ghosh S, Mandal SK, et al. Tissue factor activation: is disulfide bond switching a regulatory mechanism? Blood 2007; 110: 3900-3908.
    • (2007) Blood , vol.110 , pp. 3900-3908
    • Pendurthi, U.R.1    Ghosh, S.2    Mandal, S.K.3
  • 70
    • 50949106954 scopus 로고    scopus 로고
    • Critical importance of the cell system when studying tissue factor de-encryption
    • Liang HP, Hogg PJ. Critical importance of the cell system when studying tissue factor de-encryption. Blood 2008; 112: 912-913.
    • (2008) Blood , vol.112 , pp. 912-913
    • Liang, H.P.1    Hogg, P.J.2
  • 71
    • 0037470064 scopus 로고    scopus 로고
    • Reduction-reoxidation cycles contribute to catalysis of disulfide isomerisation by protein-disulfide isomerase
    • Schwaller M, Wilkinson B, Gilbert HF. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerisation by protein-disulfide isomerase. J Biol Chem 2003; 278: 7154-7159.
    • (2003) J Biol Chem , vol.278 , pp. 7154-7159
    • Schwaller, M.1    Wilkinson, B.2    Gilbert, H.F.3
  • 72
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundström J, Holmgren A. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J Biol Chem 1990; 265: 9114-9120.
    • (1990) J Biol Chem , vol.265 , pp. 9114-9120
    • Lundström, J.1    Holmgren, A.2
  • 73
    • 0026704930 scopus 로고
    • Protein disulfide isomerase activity is released by activated platelets
    • Chen K, Lin Y, Detwiler TC. Protein disulfide isomerase activity is released by activated platelets. Blood 1992; 79: 2226-2228.
    • (1992) Blood , vol.79 , pp. 2226-2228
    • Chen, K.1    Lin, Y.2    Detwiler, T.C.3
  • 74
    • 0029144477 scopus 로고
    • Localisation of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, Swiatkowska M. Localisation of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 1995; 86: 2168-2173.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 75
    • 77956533379 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
    • Popescu NI, Lupu C, Lupu F. Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure. Blood 2010; 116: 993-1001.
    • (2010) Blood , vol.116 , pp. 993-1001
    • Popescu, N.I.1    Lupu, C.2    Lupu, F.3
  • 76
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • Jiang XM, Fitzgerald M, Grant CM, et al. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase. J Biol Chem 1999; 274: 2416-2423.
    • (1999) J Biol Chem , vol.274 , pp. 2416-2423
    • Jiang, X.M.1    Fitzgerald, M.2    Grant, C.M.3
  • 77
    • 0035859858 scopus 로고    scopus 로고
    • Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase
    • Ramachandran N, Root P, Jiang XM, et al. Mechanism of transfer of NO from extracellular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proc Natl Acad Sci USA 2001; 98: 9539-9544.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9539-9544
    • Ramachandran, N.1    Root, P.2    Jiang, X.M.3
  • 78
    • 15744403464 scopus 로고    scopus 로고
    • Characterisation of the S-denitrosation activity of protein disulfide isomerase
    • Sliskovic I, Raturi A, Mutus B. Characterisation of the S-denitrosation activity of protein disulfide isomerase. J Biol Chem 2005; 280: 8733-8741.
    • (2005) J Biol Chem , vol.280 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 79
    • 34548494139 scopus 로고    scopus 로고
    • Tissue factor coagulant function is enhanced by proteindisulfide isomerase independent of oxidoreductase activity
    • Versteeg HH, Ruf W. Tissue factor coagulant function is enhanced by proteindisulfide isomerase independent of oxidoreductase activity. J Biol Chem 2007; 282: 25416-25424.
    • (2007) J Biol Chem , vol.282 , pp. 25416-25424
    • Versteeg, H.H.1    Ruf, W.2
  • 80
    • 77958522684 scopus 로고    scopus 로고
    • Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity
    • Raturi A, Ruf W. Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity. J Thromb Haemost 2010; 8: 1863-1865.
    • (2010) J Thromb Haemost , vol.8 , pp. 1863-1865
    • Raturi, A.1    Ruf, W.2
  • 81
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J, Furie BC, Coughlin SR, et al. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J Clin Invest 2008; 118: 1123-1131.
    • (2008) J Clin Invest , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3
  • 82
    • 78649466923 scopus 로고    scopus 로고
    • Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo
    • Jasuja R, Furie B, Furie BC. Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo. Blood 2010; 116: 4665-4674.
    • (2010) Blood , vol.116 , pp. 4665-4674
    • Jasuja, R.1    Furie, B.2    Furie, B.C.3
  • 83
    • 84861808529 scopus 로고    scopus 로고
    • Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents
    • Jasuja R, Passam FH, Kennedy DR, et al. Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents. J Clin Invest 2012; 122: 2104-2113.
    • (2012) J Clin Invest , vol.122 , pp. 2104-2113
    • Jasuja, R.1    Passam, F.H.2    Kennedy, D.R.3
  • 84
    • 84864125078 scopus 로고    scopus 로고
    • Protein disulfide isomerase capture during thrombus formation in vivo depends on the presence of β3 integrins
    • Cho J, Kennedy DR, Lin L, et al. Protein disulfide isomerase capture during thrombus formation in vivo depends on the presence of β3 integrins. Blood 2012; 120: 647-655.
    • (2012) Blood , vol.120 , pp. 647-655
    • Cho, J.1    Kennedy, D.R.2    Lin, L.3
  • 85
    • 84880448971 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation
    • Hahm E, Li J, Kim K, et al. Extracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation. Blood 2013; 121: 3789-3800.
    • (2013) Blood , vol.121 , pp. 3789-3800
    • Hahm, E.1    Li, J.2    Kim, K.3
  • 86
    • 84886930949 scopus 로고    scopus 로고
    • Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice
    • Kim K, Hahm E, Li J, et al. Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice. Blood 2013; 122: 1052-1061.
    • (2013) Blood , vol.122 , pp. 1052-1061
    • Kim, K.1    Hahm, E.2    Li, J.3
  • 87
    • 80055109602 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding
    • Jurk K, Lahav J, VAN Aken H, et al. Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding. J Thromb Haemost 2011; 9: 2278-2290.
    • (2011) J Thromb Haemost , vol.9 , pp. 2278-2290
    • Jurk, K.1    Lahav, J.2    Van Aken, H.3
  • 88
    • 84863139700 scopus 로고    scopus 로고
    • The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis
    • Wu Y, Ahmad SS, Zhou J, et al. The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis. Blood 2012; 119: 1737-1746.
    • (2012) Blood , vol.119 , pp. 1737-1746
    • Wu, Y.1    Ahmad, S.S.2    Zhou, J.3
  • 89
    • 84860320635 scopus 로고    scopus 로고
    • Truncated and full-length thioredoxin-1 have opposing activating and inhibitory properties for human complement with relevance to endothelial surfaces
    • King BC, Nowakowska J, Karsten CM, et al. Truncated and full-length thioredoxin-1 have opposing activating and inhibitory properties for human complement with relevance to endothelial surfaces. J Immunol 2012; 188: 4103-4112.
    • (2012) J Immunol , vol.188 , pp. 4103-4112
    • King, B.C.1    Nowakowska, J.2    Karsten, C.M.3
  • 90
    • 4644312977 scopus 로고    scopus 로고
    • Cross-talk of integrin alpha3beta1 and tissue factor in cell migration
    • Dorfleutner A, Hintermann E, Tarui T, et al. Cross-talk of integrin alpha3beta1 and tissue factor in cell migration. Mol Biol Cell 2004; 15: 4416-4425.
    • (2004) Mol Biol Cell , vol.15 , pp. 4416-4425
    • Dorfleutner, A.1    Hintermann, E.2    Tarui, T.3
  • 91
    • 84873320784 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase control tissue factor activity by thiol redox-dependent mechanism
    • Wang P, Wu Y, Li X, et al. Thioredoxin and thioredoxin reductase control tissue factor activity by thiol redox-dependent mechanism. J Biol Chem 2013; 288: 3346-3358.
    • (2013) J Biol Chem , vol.288 , pp. 3346-3358
    • Wang, P.1    Wu, Y.2    Li, X.3
  • 92
    • 0346433810 scopus 로고    scopus 로고
    • Thrombosis in patients with paroxysmal nocturnal hemoglobinuria is associated with markedly elevated plasma levels of leukocyte-derived tissue factor
    • Liebman HA, Feinstein DI. Thrombosis in patients with paroxysmal nocturnal hemoglobinuria is associated with markedly elevated plasma levels of leukocyte-derived tissue factor. Thromb Res 2003; 111: 235-238.
    • (2003) Thromb Res , vol.111 , pp. 235-238
    • Liebman, H.A.1    Feinstein, D.I.2
  • 93
    • 84865254102 scopus 로고    scopus 로고
    • Eculizumab therapy results in rapid and sustained decreases in markers of thrombin generation and inflammation in patients with PNH independent of its effects on hemolysis and microparticle formation
    • Weitz IC, Razavi P, Rochanda L, et al. Eculizumab therapy results in rapid and sustained decreases in markers of thrombin generation and inflammation in patients with PNH independent of its effects on hemolysis and microparticle formation. Thromb Res 2012; 130: 361-368.
    • (2012) Thromb Res , vol.130 , pp. 361-368
    • Weitz, I.C.1    Razavi, P.2    Rochanda, L.3
  • 94
    • 0028203748 scopus 로고
    • Hemoglobin enhances the production of tissue factor by endothelial cells in response to bacterial endotoxin
    • Roth RI. Hemoglobin enhances the production of tissue factor by endothelial cells in response to bacterial endotoxin. Blood 1994; 83: 2860-2865.
    • (1994) Blood , vol.83 , pp. 2860-2865
    • Roth, R.I.1
  • 95
    • 56749170891 scopus 로고    scopus 로고
    • Heme induces endothelial tissue factor expression: Potential role in hemostatic activation in patients with hemolytic anemia
    • Setty BN, Betal SG, Zhang J, et al. Heme induces endothelial tissue factor expression: potential role in hemostatic activation in patients with hemolytic anemia. J Thromb Haemost 2008; 6: 2202-2209.
    • (2008) J Thromb Haemost , vol.6 , pp. 2202-2209
    • Setty, B.N.1    Betal, S.G.2    Zhang, J.3
  • 96
    • 84880923632 scopus 로고    scopus 로고
    • Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome
    • Frimat M, Tabarin F, Dimitrov JD, et al. Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome. Blood 2013; 122: 282-292.
    • (2013) Blood , vol.122 , pp. 282-292
    • Frimat, M.1    Tabarin, F.2    Dimitrov, J.D.3
  • 97
    • 84879075840 scopus 로고    scopus 로고
    • Interplay between coagulation and vascular inflammation in sickle cell disease
    • Sparkenbaugh E, Pawlinski R. Interplay between coagulation and vascular inflammation in sickle cell disease. Br J Haematol 2013; 162: 3-14.
    • (2013) Br J Haematol , vol.162 , pp. 3-14
    • Sparkenbaugh, E.1    Pawlinski, R.2


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