메뉴 건너뛰기




Volumn 9, Issue 11, 2011, Pages 2278-2290

Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding

Author keywords

Blood cells; Coagulation; Platelets; Redox control; Thrombin; Thrombosis

Indexed keywords

BACITRACIN; BLOOD CLOTTING FACTOR; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE);

EID: 80055109602     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2011.04509.x     Document Type: Article
Times cited : (62)

References (46)
  • 2
    • 34547630092 scopus 로고    scopus 로고
    • Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis
    • Mackman N, Tilley RE, Key NS. Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis. Arterioscler Thromb Vasc Biol 2007; 27: 1687-93.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1687-1693
    • Mackman, N.1    Tilley, R.E.2    Key, N.S.3
  • 3
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • Brummel KE, Paradis SG, Butenas S, Mann KG. Thrombin functions during tissue factor-induced blood coagulation. Blood 2002; 100: 148-52.
    • (2002) Blood , vol.100 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3    Mann, K.G.4
  • 4
    • 0034307532 scopus 로고    scopus 로고
    • The GPIb thrombin-binding site is essential for thrombin-induced platelet procoagulant activity
    • Dörmann D, Clemetson KJ, Kehrel BE. The GPIb thrombin-binding site is essential for thrombin-induced platelet procoagulant activity. Blood 2000; 96: 2469-78.
    • (2000) Blood , vol.96 , pp. 2469-2478
    • Dörmann, D.1    Clemetson, K.J.2    Kehrel, B.E.3
  • 5
    • 33646475277 scopus 로고    scopus 로고
    • A cell-based model of thrombin generation
    • Roberts HR, Hoffman M, Monroe DM. A cell-based model of thrombin generation. Semin Thromb Hemost 2006; 32 (Suppl. 1): 32-8.
    • (2006) Semin Thromb Hemost , vol.32 , Issue.SUPPL.. 1 , pp. 32-38
    • Roberts, H.R.1    Hoffman, M.2    Monroe, D.M.3
  • 6
    • 4444252017 scopus 로고    scopus 로고
    • Platelet coagulation-protein interactions
    • Walsh PN. Platelet coagulation-protein interactions. Semin Thromb Hemost 2004; 30: 461-71.
    • (2004) Semin Thromb Hemost , vol.30 , pp. 461-471
    • Walsh, P.N.1
  • 7
    • 0029939917 scopus 로고    scopus 로고
    • Variability in platelet procoagulant activity in healthy volunteers
    • Sumner WT, Monroe DM, Hoffman M. Variability in platelet procoagulant activity in healthy volunteers. Thromb Res 1996; 81: 533-43.
    • (1996) Thromb Res , vol.81 , pp. 533-543
    • Sumner, W.T.1    Monroe, D.M.2    Hoffman, M.3
  • 8
    • 2942637935 scopus 로고    scopus 로고
    • Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids
    • Zwaal RF, Comfurius P, Bevers EM. Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids. Biochim Biophys Acta 2004; 1636: 119-28.
    • (2004) Biochim Biophys Acta , vol.1636 , pp. 119-128
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 9
    • 0030832008 scopus 로고    scopus 로고
    • The physical exchange of factor VIII (FVIII) between von Willebrand factor and activated platelets and the effect of the FVIII B-domain on platelet binding
    • Li X, Gabriel DA. The physical exchange of factor VIII (FVIII) between von Willebrand factor and activated platelets and the effect of the FVIII B-domain on platelet binding. Biochemistry 1997; 36: 10760-7.
    • (1997) Biochemistry , vol.36 , pp. 10760-10767
    • Li, X.1    Gabriel, D.A.2
  • 11
    • 0346850827 scopus 로고    scopus 로고
    • Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively
    • Yun TH, Baglia FA, Myles T, Navaneetham D, Lopez JA, Walsh PN, Leung LL. Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively. J Biol Chem 2003; 278: 48112-9.
    • (2003) J Biol Chem , vol.278 , pp. 48112-48119
    • Yun, T.H.1    Baglia, F.A.2    Myles, T.3    Navaneetham, D.4    Lopez, J.A.5    Walsh, P.N.6    Leung, L.L.7
  • 12
    • 54049130877 scopus 로고    scopus 로고
    • The glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface
    • Weeterings C, de Groot PG, Adelmeijer J, Lisman T. The glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface. Blood 2008; 112: 3227-33.
    • (2008) Blood , vol.112 , pp. 3227-3233
    • Weeterings, C.1    de Groot, P.G.2    Adelmeijer, J.3    Lisman, T.4
  • 14
    • 0030870212 scopus 로고    scopus 로고
    • Networking in the hemostatic system. Integrin alphaiibbeta3 binds prothrombin and influences its activation
    • Byzova TV, Plow EF. Networking in the hemostatic system. Integrin alphaiibbeta3 binds prothrombin and influences its activation. J Biol Chem 1997; 272: 27183-8.
    • (1997) J Biol Chem , vol.272 , pp. 27183-27188
    • Byzova, T.V.1    Plow, E.F.2
  • 15
    • 0030949504 scopus 로고    scopus 로고
    • Effector cell protease receptor-1, a platelet activation-dependent membrane protein, regulates prothrombinase-catalyzed thrombin generation
    • Bouchard BA, Catcher CS, Thrash BR, Adida C, Tracy PB. Effector cell protease receptor-1, a platelet activation-dependent membrane protein, regulates prothrombinase-catalyzed thrombin generation. J Biol Chem 1997; 272: 9244-51.
    • (1997) J Biol Chem , vol.272 , pp. 9244-9251
    • Bouchard, B.A.1    Catcher, C.S.2    Thrash, B.R.3    Adida, C.4    Tracy, P.B.5
  • 17
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J, Furie BC, Coughlin SR, Furie B. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J Clin Invest 2008; 118: 1123-31.
    • (2008) J Clin Invest , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 18
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu BP, Weissman JS. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 2004; 164: 341-6.
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 19
    • 0029025521 scopus 로고
    • Characterization of protein disulphide isomerase released from activated platelets
    • Chen K, Detwiler TC, Essex DW. Characterization of protein disulphide isomerase released from activated platelets. Br J Haematol 1995; 90: 425-31.
    • (1995) Br J Haematol , vol.90 , pp. 425-431
    • Chen, K.1    Detwiler, T.C.2    Essex, D.W.3
  • 20
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, Swiatkowska M. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 1995; 86: 2168-73.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 21
    • 67849095440 scopus 로고    scopus 로고
    • Contribution of allosteric disulfide bonds to regulation of hemostasis
    • Hogg PJ. Contribution of allosteric disulfide bonds to regulation of hemostasis. J Thromb Haemost 2009; 7 (Suppl 1): 13-6.
    • (2009) J Thromb Haemost , vol.7 , Issue.SUPPL. 1 , pp. 13-16
    • Hogg, P.J.1
  • 23
    • 75149147568 scopus 로고    scopus 로고
    • Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation
    • Holbrook LM, Watkins NA, Simmonds AD, Jones CI, Ouwehand WH, Gibbins JM. Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation. Br J Haematol 2010; 148: 627-37.
    • (2010) Br J Haematol , vol.148 , pp. 627-637
    • Holbrook, L.M.1    Watkins, N.A.2    Simmonds, A.D.3    Jones, C.I.4    Ouwehand, W.H.5    Gibbins, J.M.6
  • 26
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange
    • Lahav J, Jurk K, Hess O, Barnes MJ, Farndale RW, Luboshitz J, Kehrel BE. Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange. Blood 2002; 100: 2472-8.
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1    Jurk, K.2    Hess, O.3    Barnes, M.J.4    Farndale, R.W.5    Luboshitz, J.6    Kehrel, B.E.7
  • 27
    • 0032985071 scopus 로고    scopus 로고
    • Protein disulphide isomerase mediates platelet aggregation and secretion
    • Essex DW, Li M. Protein disulphide isomerase mediates platelet aggregation and secretion. Br J Haematol 1999; 104: 448-54.
    • (1999) Br J Haematol , vol.104 , pp. 448-454
    • Essex, D.W.1    Li, M.2
  • 29
    • 1242306912 scopus 로고    scopus 로고
    • Platelets in patients with acute ischemic stroke are exhausted and refractory to thrombin, due to cleavage of the seven-transmembrane thrombin receptor (PAR-1)
    • Jurk K, Jahn UR, Van Aken H, Schriek C, Droste DW, Ritter MA, Bernd RE, Kehrel BE. Platelets in patients with acute ischemic stroke are exhausted and refractory to thrombin, due to cleavage of the seven-transmembrane thrombin receptor (PAR-1). Thromb Haemost 2004; 91: 334-44.
    • (2004) Thromb Haemost , vol.91 , pp. 334-344
    • Jurk, K.1    Jahn, U.R.2    Van Aken, H.3    Schriek, C.4    Droste, D.W.5    Ritter, M.A.6    Bernd, R.E.7    Kehrel, B.E.8
  • 32
    • 0029998797 scopus 로고    scopus 로고
    • Optimally functional fluorescein isothiocyanate-labelled fibrinogen for quantitative studies of binding to activated platelets and platelet aggregation
    • Xia Z, Wong T, Liu Q, Kasirer-Friede A, Brown E, Frojmovic MM. Optimally functional fluorescein isothiocyanate-labelled fibrinogen for quantitative studies of binding to activated platelets and platelet aggregation. Br J Haematol 1996; 93: 204-14.
    • (1996) Br J Haematol , vol.93 , pp. 204-214
    • Xia, Z.1    Wong, T.2    Liu, Q.3    Kasirer-Friede, A.4    Brown, E.5    Frojmovic, M.M.6
  • 33
    • 34249903638 scopus 로고    scopus 로고
    • Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay
    • Raturi A, Mutus B. Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay. Free Radic Biol Med 2007; 43: 62-70.
    • (2007) Free Radic Biol Med , vol.43 , pp. 62-70
    • Raturi, A.1    Mutus, B.2
  • 34
    • 33644848864 scopus 로고    scopus 로고
    • Bacitracin reveals a role for multiple thiol isomerases in platelet function
    • Robinson A, O'Neill S, Kiernan A, O'Donoghue N, Moran N. Bacitracin reveals a role for multiple thiol isomerases in platelet function. Br J Haematol 2006; 132: 339-48.
    • (2006) Br J Haematol , vol.132 , pp. 339-348
    • Robinson, A.1    O'Neill, S.2    Kiernan, A.3    O'Donoghue, N.4    Moran, N.5
  • 35
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan PA, Gibbins JM. Extracellular disulfide exchange and the regulation of cellular function. Antioxid Redox Signal 2006; 8: 312-24.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 36
    • 0034737776 scopus 로고    scopus 로고
    • Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane
    • Burgess JK, Hotchkiss KA, Suter C, Dudman NP, Szollosi J, Chesterman CN, Chong BH, Hogg PJ. Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane. J Biol Chem 2000; 275: 9758-66.
    • (2000) J Biol Chem , vol.275 , pp. 9758-9766
    • Burgess, J.K.1    Hotchkiss, K.A.2    Suter, C.3    Dudman, N.P.4    Szollosi, J.5    Chesterman, C.N.6    Chong, B.H.7    Hogg, P.J.8
  • 37
    • 0034711264 scopus 로고    scopus 로고
    • The platelet integrin alpha IIbbeta 3 has an endogenous thiol isomerase activity
    • O'Neill S, Robinson A, Deering A, Ryan M, Fitzgerald DJ, Moran N. The platelet integrin alpha IIbbeta 3 has an endogenous thiol isomerase activity. J Biol Chem 2000; 275: 36984-90.
    • (2000) J Biol Chem , vol.275 , pp. 36984-36990
    • O'Neill, S.1    Robinson, A.2    Deering, A.3    Ryan, M.4    Fitzgerald, D.J.5    Moran, N.6
  • 38
    • 0029085314 scopus 로고
    • Thrombin generation in plasma: its assessment via the endogenous thrombin potential
    • Hemker HC, Beguin S. Thrombin generation in plasma: its assessment via the endogenous thrombin potential. Thromb Haemost 1995; 74: 134-8.
    • (1995) Thromb Haemost , vol.74 , pp. 134-138
    • Hemker, H.C.1    Beguin, S.2
  • 39
    • 17744362278 scopus 로고    scopus 로고
    • Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activity
    • Maun HR, Eigenbrot C, Raab H, Arnott D, Phu L, Bullens S, Lazarus RA. Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activity. Protein Sci 2005; 14: 1171-80.
    • (2005) Protein Sci , vol.14 , pp. 1171-1180
    • Maun, H.R.1    Eigenbrot, C.2    Raab, H.3    Arnott, D.4    Phu, L.5    Bullens, S.6    Lazarus, R.A.7
  • 40
  • 41
    • 0030798989 scopus 로고    scopus 로고
    • Conformation of factor VIIa stabilized by a labile disulfide bond (Cys-310-Cys-329) in the protease domain is essential for interaction with tissue factor
    • Higashi S, Matsumoto N, Iwanaga S. Conformation of factor VIIa stabilized by a labile disulfide bond (Cys-310-Cys-329) in the protease domain is essential for interaction with tissue factor. J Biol Chem 1997; 272: 25724-30.
    • (1997) J Biol Chem , vol.272 , pp. 25724-25730
    • Higashi, S.1    Matsumoto, N.2    Iwanaga, S.3
  • 42
    • 34848874846 scopus 로고    scopus 로고
    • Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery
    • Bush-Pelc LA, Marino F, Chen Z, Pineda AO, Mathews FS, Di Cera E. Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery. J Biol Chem 2007; 282: 27165-70.
    • (2007) J Biol Chem , vol.282 , pp. 27165-27170
    • Bush-Pelc, L.A.1    Marino, F.2    Chen, Z.3    Pineda, A.O.4    Mathews, F.S.5    Di Cera, E.6
  • 43
    • 37249050299 scopus 로고    scopus 로고
    • A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets
    • Miller TN, Sinha D, Baird TR, Walsh PN. A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets. Biochemistry 2007; 46: 14450-60.
    • (2007) Biochemistry , vol.46 , pp. 14450-14460
    • Miller, T.N.1    Sinha, D.2    Baird, T.R.3    Walsh, P.N.4
  • 44
    • 0025247833 scopus 로고
    • Purification and characterization of factor VIII 372-Cys: a hypofunctional cofactor from a patient with moderately severe hemophilia A
    • O'Brien DP, Pattinson JK, Tuddenham EG. Purification and characterization of factor VIII 372-Cys: a hypofunctional cofactor from a patient with moderately severe hemophilia A. Blood 1990; 75: 1664-72.
    • (1990) Blood , vol.75 , pp. 1664-1672
    • O'Brien, D.P.1    Pattinson, J.K.2    Tuddenham, E.G.3
  • 45
    • 0033059442 scopus 로고    scopus 로고
    • Prothrombin carora: hypoprothrombinaemia caused by substitution of Tyr-44 by Cys
    • Sun WY, Ruiz-Saez A, Burkart MC, Bosch N, Degen SJ. Prothrombin carora: hypoprothrombinaemia caused by substitution of Tyr-44 by Cys. Br J Haematol 1999; 105: 670-2.
    • (1999) Br J Haematol , vol.105 , pp. 670-672
    • Sun, W.Y.1    Ruiz-Saez, A.2    Burkart, M.C.3    Bosch, N.4    Degen, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.