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Volumn 134, Issue 1, 2014, Pages 144-152

Protein S and factor v in regulation of coagulation on platelet microparticles by activated protein C

Author keywords

Activated protein C; Coagulation; Factor V; Factor VIII; Microparticles; Protein S

Indexed keywords

ACTIVATED PROTEIN C; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 5A; BLOOD CLOTTING FACTOR 8A; CALCIMYCIN; COLLAGEN; LACTADHERIN; PHOSPHATIDYLSERINE; PROTEIN S; THROMBIN; PROTEIN C;

EID: 84902535266     PISSN: 00493848     EISSN: 18792472     Source Type: Journal    
DOI: 10.1016/j.thromres.2014.04.031     Document Type: Article
Times cited : (30)

References (57)
  • 3
    • 0032953002 scopus 로고    scopus 로고
    • Platelet microparticles: A wide-angle perspective
    • L.L. Horstman, and Y.S. Ahn Platelet microparticles: a wide-angle perspective Crit Rev Oncol Hematol 30 1999 111 142
    • (1999) Crit Rev Oncol Hematol , vol.30 , pp. 111-142
    • Horstman, L.L.1    Ahn, Y.S.2
  • 4
    • 0024325249 scopus 로고
    • Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: An isolated defect in platelet procoagulant activity
    • P.J. Sims, T. Wiedmer, C.T. Esmon, H.J. Weiss, and S.J. Shattil Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: an isolated defect in platelet procoagulant activity J Biol Chem 264 1989 17049 17057
    • (1989) J Biol Chem , vol.264 , pp. 17049-17057
    • Sims, P.J.1    Wiedmer, T.2    Esmon, C.T.3    Weiss, H.J.4    Shattil, S.J.5
  • 5
    • 0025738740 scopus 로고
    • Comparison of anticoagulant and procoagulant activities of stimulated platelets and platelet-derived microparticles
    • G. Tans, J. Rosing, M.C. Thomassen, M.J. Heeb, R.F. Zwaal, and J.H. Griffin Comparison of anticoagulant and procoagulant activities of stimulated platelets and platelet-derived microparticles Blood 77 1991 2641 2648
    • (1991) Blood , vol.77 , pp. 2641-2648
    • Tans, G.1    Rosing, J.2    Thomassen, M.C.3    Heeb, M.J.4    Zwaal, R.F.5    Griffin, J.H.6
  • 6
    • 0026752756 scopus 로고
    • Coagulation factor IXa binding to activated platelets and platelet-derived microparticles: A flow cytometric study
    • M. Hoffman, D.M. Monroe, and H.R. Roberts Coagulation factor IXa binding to activated platelets and platelet-derived microparticles: a flow cytometric study Thromb Haemost 68 1992 74 78
    • (1992) Thromb Haemost , vol.68 , pp. 74-78
    • Hoffman, M.1    Monroe, D.M.2    Roberts, H.R.3
  • 7
    • 0026056626 scopus 로고
    • Platelet-derived microparticles express high affinity receptors for factor VIII
    • G.E. Gilbert, P.J. Sims, T. Wiedmer, B. Furie, B.C. Furie, and S.J. Shattil Platelet-derived microparticles express high affinity receptors for factor VIII J Biol Chem 266 1991 17261 17268
    • (1991) J Biol Chem , vol.266 , pp. 17261-17268
    • Gilbert, G.E.1    Sims, P.J.2    Wiedmer, T.3    Furie, B.4    Furie, B.C.5    Shattil, S.J.6
  • 8
    • 4444297645 scopus 로고    scopus 로고
    • Binding studies of the enzyme (factor IXa) with the cofactor (factor VIIIa) in the assembly of factor-X activating complex on the activated platelet surface
    • S.S. Ahmad, F.S. London, and P.N. Walsh Binding studies of the enzyme (factor IXa) with the cofactor (factor VIIIa) in the assembly of factor-X activating complex on the activated platelet surface J Thromb Haemost 1 2003 2348 2355
    • (2003) J Thromb Haemost , vol.1 , pp. 2348-2355
    • Ahmad, S.S.1    London, F.S.2    Walsh, P.N.3
  • 9
    • 0019977242 scopus 로고
    • Radioimmunoassay of factor v in human plasma and platelets
    • P.B. Tracy, L.L. Eide, E.J. Bowie, and K.G. Mann Radioimmunoassay of factor V in human plasma and platelets Blood 60 1982 59 63
    • (1982) Blood , vol.60 , pp. 59-63
    • Tracy, P.B.1    Eide, L.L.2    Bowie, E.J.3    Mann, K.G.4
  • 11
    • 0019831499 scopus 로고
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X
    • G. van Dieijen, G. Tans, J. Rosing, and H.C. Hemker The role of phospholipid and factor VIIIa in the activation of bovine factor X J Biol Chem 256 1981 3433 3442
    • (1981) J Biol Chem , vol.256 , pp. 3433-3442
    • Van Dieijen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4
  • 12
    • 20444427991 scopus 로고    scopus 로고
    • The anticoagulant protein C pathway
    • B. Dahlback, and B.O. Villoutreix The anticoagulant protein C pathway FEBS Lett 579 2005 3310 3316
    • (2005) FEBS Lett , vol.579 , pp. 3310-3316
    • Dahlback, B.1    Villoutreix, B.O.2
  • 13
    • 0025888388 scopus 로고
    • Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. Identification of cleavage sites and correlation of proteolysis with cofactor activity
    • P.J. Fay, T.M. Smudzin, and F.J. Walker Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. Identification of cleavage sites and correlation of proteolysis with cofactor activity J Biol Chem 266 1991 20139 20145
    • (1991) J Biol Chem , vol.266 , pp. 20139-20145
    • Fay, P.J.1    Smudzin, T.M.2    Walker, F.J.3
  • 14
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor v and human factor Va by activated protein C
    • M. Kalafatis, M.D. Rand, and K.G. Mann The mechanism of inactivation of human factor V and human factor Va by activated protein C J Biol Chem 269 1994 31869 31880
    • (1994) J Biol Chem , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 15
    • 0031468611 scopus 로고    scopus 로고
    • Factor V, and protein S as cofactors to activated protein C
    • B. Dahlback Factor V, and protein S as cofactors to activated protein C Haematologica 82 1997 91 95
    • (1997) Haematologica , vol.82 , pp. 91-95
    • Dahlback, B.1
  • 16
    • 21544447526 scopus 로고    scopus 로고
    • Regulation of blood coagulation by the protein C anticoagulant pathway: Novel insights into structure-function relationships and molecular recognition
    • B. Dahlback, and B.O. Villoutreix Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition Arterioscler Thromb Vasc Biol 25 2005 1311 1320
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 1311-1320
    • Dahlback, B.1    Villoutreix, B.O.2
  • 17
    • 0040426308 scopus 로고
    • High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein
    • B. Dahlback, and J. Stenflo High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein Proc Natl Acad Sci U S A 78 1981 2512 2516
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2512-2516
    • Dahlback, B.1    Stenflo, J.2
  • 18
    • 42449084553 scopus 로고    scopus 로고
    • Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation
    • L.F. Maurissen, M.C. Thomassen, G.A. Nicolaes, B. Dahlback, G. Tans, and J. Rosing et al. Re-evaluation of the role of the protein S-C4b binding protein complex in activated protein C-catalyzed factor Va-inactivation Blood 111 2008 3034 3041
    • (2008) Blood , vol.111 , pp. 3034-3041
    • Maurissen, L.F.1    Thomassen, M.C.2    Nicolaes, G.A.3    Dahlback, B.4    Tans, G.5    Rosing, J.6
  • 19
    • 84855307880 scopus 로고    scopus 로고
    • The anticoagulant function of coagulation factor v
    • T.J. Cramer, and A.J. Gale The anticoagulant function of coagulation factor V Thromb Haemost 107 2012 15 21
    • (2012) Thromb Haemost , vol.107 , pp. 15-21
    • Cramer, T.J.1    Gale, A.J.2
  • 20
    • 0036124011 scopus 로고    scopus 로고
    • Factor v and thrombotic disease: Description of a janus-faced protein
    • G.A. Nicolaes, and B. Dahlback Factor V and thrombotic disease: description of a janus-faced protein Arterioscler Thromb Vasc Biol 22 2002 530 538
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 530-538
    • Nicolaes, G.A.1    Dahlback, B.2
  • 21
    • 0022411427 scopus 로고
    • Identification and quantitation of protein S in human platelets
    • H.P. Schwarz, M.J. Heeb, J.D. Wencel-Drake, and J.H. Griffin Identification and quantitation of protein S in human platelets Blood 66 1985 1452 1455
    • (1985) Blood , vol.66 , pp. 1452-1455
    • Schwarz, H.P.1    Heeb, M.J.2    Wencel-Drake, J.D.3    Griffin, J.H.4
  • 22
    • 47249084343 scopus 로고    scopus 로고
    • Advances in understanding pathogenic mechanisms of thrombophilic disorders
    • B. Dahlback Advances in understanding pathogenic mechanisms of thrombophilic disorders Blood 112 2008 19 27
    • (2008) Blood , vol.112 , pp. 19-27
    • Dahlback, B.1
  • 23
    • 79960970355 scopus 로고    scopus 로고
    • A filtration-based protocol to isolate human plasma membrane-derived vesicles and exosomes from blood plasma
    • R. Grant, E. Ansa-Addo, D. Stratton, S. Antwi-Baffour, S. Jorfi, and S. Kholia et al. A filtration-based protocol to isolate human plasma membrane-derived vesicles and exosomes from blood plasma J Immunol Methods 371 2011 143 151
    • (2011) J Immunol Methods , vol.371 , pp. 143-151
    • Grant, R.1    Ansa-Addo, E.2    Stratton, D.3    Antwi-Baffour, S.4    Jorfi, S.5    Kholia, S.6
  • 24
    • 33645551730 scopus 로고    scopus 로고
    • Circulating platelet-derived microparticles in systemic lupus erythematosus. Association with increased thrombin generation and procoagulant state
    • J. Pereira, G. Alfaro, M. Goycoolea, T. Quiroga, M. Ocqueteau, and L. Massardo et al. Circulating platelet-derived microparticles in systemic lupus erythematosus. Association with increased thrombin generation and procoagulant state Thromb Haemost 95 2006 94 99
    • (2006) Thromb Haemost , vol.95 , pp. 94-99
    • Pereira, J.1    Alfaro, G.2    Goycoolea, M.3    Quiroga, T.4    Ocqueteau, M.5    Massardo, L.6
  • 25
    • 77952010480 scopus 로고    scopus 로고
    • Role of platelet-derived microparticles in angiogenesis and tumor progression
    • D. Varon, and E. Shai Role of platelet-derived microparticles in angiogenesis and tumor progression Discov Med 8 2009 237 241
    • (2009) Discov Med , vol.8 , pp. 237-241
    • Varon, D.1    Shai, E.2
  • 26
    • 75149167003 scopus 로고    scopus 로고
    • Increased levels of circulating microparticles in primary Sjogren's syndrome, systemic lupus erythematosus and rheumatoid arthritis and relation with disease activity
    • J. Sellam, V. Proulle, A. Jungel, M. Ittah, C. Miceli Richard, and J.E. Gottenberg et al. Increased levels of circulating microparticles in primary Sjogren's syndrome, systemic lupus erythematosus and rheumatoid arthritis and relation with disease activity Arthritis Res Ther 11 2009 R156
    • (2009) Arthritis Res Ther , vol.11 , pp. 156
    • Sellam, J.1    Proulle, V.2    Jungel, A.3    Ittah, M.4    Miceli Richard, C.5    Gottenberg, J.E.6
  • 27
    • 0035988193 scopus 로고    scopus 로고
    • Detection of monocyte-derived microparticles in patients with Type II diabetes mellitus
    • S. Omoto, S. Nomura, A. Shouzu, M. Nishikawa, S. Fukuhara, and T. Iwasaka Detection of monocyte-derived microparticles in patients with Type II diabetes mellitus Diabetologia 45 2002 550 555
    • (2002) Diabetologia , vol.45 , pp. 550-555
    • Omoto, S.1    Nomura, S.2    Shouzu, A.3    Nishikawa, M.4    Fukuhara, S.5    Iwasaka, T.6
  • 28
    • 0033999142 scopus 로고    scopus 로고
    • Elevated levels of shed membrane microparticles with procoagulant potential in the peripheral circulating blood of patients with acute coronary syndromes
    • Z. Mallat, H. Benamer, B. Hugel, J. Benessiano, P.G. Steg, and J.M. Freyssinet et al. Elevated levels of shed membrane microparticles with procoagulant potential in the peripheral circulating blood of patients with acute coronary syndromes Circulation 101 2000 841 843
    • (2000) Circulation , vol.101 , pp. 841-843
    • Mallat, Z.1    Benamer, H.2    Hugel, B.3    Benessiano, J.4    Steg, P.G.5    Freyssinet, J.M.6
  • 29
    • 34548720409 scopus 로고    scopus 로고
    • Factor Va, bound to microparticles released during platelet storage, is resistant to inactivation by activated protein C
    • E.J. Magdeleyns, J.F. Keuren, and J. Curvers Factor Va, bound to microparticles released during platelet storage, is resistant to inactivation by activated protein C Transfusion 47 2007 1880 1888
    • (2007) Transfusion , vol.47 , pp. 1880-1888
    • Magdeleyns, E.J.1    Keuren, J.F.2    Curvers, J.3
  • 30
    • 1642576099 scopus 로고    scopus 로고
    • Unique in vivo modifications of coagulation factor v produce a physically and functionally distinct platelet-derived cofactor: Characterization of purified platelet-derived factor V/Va
    • W.R. Gould, J.R. Silveira, and P.B. Tracy Unique in vivo modifications of coagulation factor V produce a physically and functionally distinct platelet-derived cofactor: characterization of purified platelet-derived factor V/Va J Biol Chem 279 2004 2383 2393
    • (2004) J Biol Chem , vol.279 , pp. 2383-2393
    • Gould, W.R.1    Silveira, J.R.2    Tracy, P.B.3
  • 31
    • 0032522957 scopus 로고    scopus 로고
    • Platelet-derived factor Va/Va Leiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C
    • R.M. Camire, M. Kalafatis, P. Simioni, A. Girolami, and P.B. Tracy Platelet-derived factor Va/Va Leiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C Blood 91 1998 2818 2829
    • (1998) Blood , vol.91 , pp. 2818-2829
    • Camire, R.M.1    Kalafatis, M.2    Simioni, P.3    Girolami, A.4    Tracy, P.B.5
  • 32
    • 0033153097 scopus 로고    scopus 로고
    • Activated protein C resistance: Effect of platelet activation, platelet-derived microparticles, and atherogenic lipoproteins
    • J. Taube, N. McWilliam, R. Luddington, C.D. Byrne, and T. Baglin Activated protein C resistance: effect of platelet activation, platelet-derived microparticles, and atherogenic lipoproteins Blood 93 1999 3792 3797
    • (1999) Blood , vol.93 , pp. 3792-3797
    • Taube, J.1    McWilliam, N.2    Luddington, R.3    Byrne, C.D.4    Baglin, T.5
  • 33
    • 0027076848 scopus 로고
    • Binding of anticoagulant vitamin K-dependent protein S to platelet-derived microparticles
    • B. Dahlback, T. Wiedmer, and P.J. Sims Binding of anticoagulant vitamin K-dependent protein S to platelet-derived microparticles Biochemistry 31 1992 12769 12777
    • (1992) Biochemistry , vol.31 , pp. 12769-12777
    • Dahlback, B.1    Wiedmer, T.2    Sims, P.J.3
  • 34
    • 0018909419 scopus 로고
    • Human coagluation factor v purification and thrombin-catalyzed activation
    • B. Dahlback Human coagluation factor V purification and thrombin-catalyzed activation J Clin Invest 66 1980 583 591
    • (1980) J Clin Invest , vol.66 , pp. 583-591
    • Dahlback, B.1
  • 35
    • 0015516443 scopus 로고
    • Bovine factors X 1 and X 2 (Stuart factor). Isolation and characterization
    • K. Fujikawa, M.E. Legaz, and E.W. Davie Bovine factors X 1 and X 2 (Stuart factor). Isolation and characterization Biochemistry 11 1972 4882 4891
    • (1972) Biochemistry , vol.11 , pp. 4882-4891
    • Fujikawa, K.1    Legaz, M.E.2    Davie, E.W.3
  • 36
    • 0015760648 scopus 로고
    • The mode of action of vitamin K. Isolation of a peptide containing the vitamin K-dependent portion of prothrombin
    • G.L. Nelsestuen, and J.W. Suttie The mode of action of vitamin K. Isolation of a peptide containing the vitamin K-dependent portion of prothrombin Proc Natl Acad Sci U S A 70 1973 3366 3370
    • (1973) Proc Natl Acad Sci U S A , vol.70 , pp. 3366-3370
    • Nelsestuen, G.L.1    Suttie, J.W.2
  • 37
    • 0031424043 scopus 로고    scopus 로고
    • Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: Studies related to proline-10
    • L. Shen, A.M. Shah, B. Dahlback, and G.L. Nelsestuen Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: studies related to proline-10 Biochemistry 36 1997 16025 16031
    • (1997) Biochemistry , vol.36 , pp. 16025-16031
    • Shen, L.1    Shah, A.M.2    Dahlback, B.3    Nelsestuen, G.L.4
  • 39
    • 78651314081 scopus 로고    scopus 로고
    • Lactadherin functions as a probe for phosphatidylserine exposure and as an anticoagulant in the study of stored platelets
    • J. Hou, Y. Fu, J. Zhou, W. Li, R. Xie, and F. Cao et al. Lactadherin functions as a probe for phosphatidylserine exposure and as an anticoagulant in the study of stored platelets Vox Sang 100 2011 187 195
    • (2011) Vox Sang , vol.100 , pp. 187-195
    • Hou, J.1    Fu, Y.2    Zhou, J.3    Li, W.4    Xie, R.5    Cao, F.6
  • 40
    • 0037100417 scopus 로고    scopus 로고
    • Functional characterization of recombinant FV Hong Kong and FV Cambridge
    • E. Norstrom, E. Thorelli, and B. Dahlback Functional characterization of recombinant FV Hong Kong and FV Cambridge Blood 100 2002 524 530
    • (2002) Blood , vol.100 , pp. 524-530
    • Norstrom, E.1    Thorelli, E.2    Dahlback, B.3
  • 41
    • 0029133654 scopus 로고
    • Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C
    • G.A. Nicolaes, G. Tans, M.C. Thomassen, H.C. Hemker, I. Pabinger, and K. Varadi et al. Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C J Biol Chem 270 1995 21158 21166
    • (1995) J Biol Chem , vol.270 , pp. 21158-21166
    • Nicolaes, G.A.1    Tans, G.2    Thomassen, M.C.3    Hemker, H.C.4    Pabinger, I.5    Varadi, K.6
  • 42
    • 9144220292 scopus 로고    scopus 로고
    • Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C
    • Y.H. Sun, S. Tran, E.A. Norstrom, and B. Dahlback Enhanced rate of cleavage at Arg-306 and Arg-506 in coagulation factor Va by Gla domain-mutated human-activated protein C J Biol Chem 279 2004 47528 47535
    • (2004) J Biol Chem , vol.279 , pp. 47528-47535
    • Sun, Y.H.1    Tran, S.2    Norstrom, E.A.3    Dahlback, B.4
  • 43
    • 0025303669 scopus 로고
    • Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies
    • B. Dahlback, B. Hildebrand, and J. Malm Characterization of functionally important domains in human vitamin K-dependent protein S using monoclonal antibodies J Biol Chem 265 1990 8127 8135
    • (1990) J Biol Chem , vol.265 , pp. 8127-8135
    • Dahlback, B.1    Hildebrand, B.2    Malm, J.3
  • 44
    • 79957493898 scopus 로고    scopus 로고
    • Microparticles in hemostasis and thrombosis
    • A.P. Owens III, and N. Mackman Microparticles in hemostasis and thrombosis Circ Res 108 2011 1284 1297
    • (2011) Circ Res , vol.108 , pp. 1284-1297
    • Owens III, A.P.1    Mackman, N.2
  • 45
    • 0028810678 scopus 로고
    • Effects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein C
    • J. Rosing, L. Hoekema, G.A. Nicolaes, M.C. Thomassen, H.C. Hemker, and K. Varadi et al. Effects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein C J Biol Chem 270 1995 27852 27858
    • (1995) J Biol Chem , vol.270 , pp. 27852-27858
    • Rosing, J.1    Hoekema, L.2    Nicolaes, G.A.3    Thomassen, M.C.4    Hemker, H.C.5    Varadi, K.6
  • 46
    • 43749109436 scopus 로고    scopus 로고
    • Effects of prothrombin on the individual activated protein C-mediated cleavages of coagulation factor Va
    • S. Tran, E. Norstrom, and B. Dahlback Effects of prothrombin on the individual activated protein C-mediated cleavages of coagulation factor Va J Biol Chem 283 2008 6648 6655
    • (2008) J Biol Chem , vol.283 , pp. 6648-6655
    • Tran, S.1    Norstrom, E.2    Dahlback, B.3
  • 47
    • 77952704204 scopus 로고    scopus 로고
    • Flow cytometric analysis of circulating microparticles in plasma
    • A.F. Orozco, and D.E. Lewis Flow cytometric analysis of circulating microparticles in plasma Cytometry A 77 2010 502 514
    • (2010) Cytometry A , vol.77 , pp. 502-514
    • Orozco, A.F.1    Lewis, D.E.2
  • 48
    • 84858702151 scopus 로고    scopus 로고
    • High-sensitivity flow cytometry provides access to standardized measurement of small-size microparticles-brief report
    • S. Robert, R. Lacroix, P. Poncelet, K. Harhouri, T. Bouriche, and C. Judicone et al. High-sensitivity flow cytometry provides access to standardized measurement of small-size microparticles-brief report Arterioscler Thromb Vasc Biol 32 2012 1054 1058
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 1054-1058
    • Robert, S.1    Lacroix, R.2    Poncelet, P.3    Harhouri, K.4    Bouriche, T.5    Judicone, C.6
  • 49
    • 0023091788 scopus 로고
    • Cleavage of protein S by a platelet membrane protease
    • C.A. Mitchell, and H.H. Salem Cleavage of protein S by a platelet membrane protease J Clin Invest 79 1987 374 379
    • (1987) J Clin Invest , vol.79 , pp. 374-379
    • Mitchell, C.A.1    Salem, H.H.2
  • 50
    • 0043092166 scopus 로고    scopus 로고
    • Importance of protein S and phospholipid for activated protein C-mediated cleavages in factor Va
    • E.A. Norstrom, M. Steen, S. Tran, and B. Dahlback Importance of protein S and phospholipid for activated protein C-mediated cleavages in factor Va J Biol Chem 278 2003 24904 24911
    • (2003) J Biol Chem , vol.278 , pp. 24904-24911
    • Norstrom, E.A.1    Steen, M.2    Tran, S.3    Dahlback, B.4
  • 51
    • 77956487994 scopus 로고    scopus 로고
    • Zn(2)(+) -containing protein S inhibits extrinsic factor X-activating complex independently of tissue factor pathway inhibitor
    • N. Fernandes, L.O. Mosnier, L. Tonnu, and M.J. Heeb Zn(2)(+) -containing protein S inhibits extrinsic factor X-activating complex independently of tissue factor pathway inhibitor J Thromb Haemost 8 2010 1976 1985
    • (2010) J Thromb Haemost , vol.8 , pp. 1976-1985
    • Fernandes, N.1    Mosnier, L.O.2    Tonnu, L.3    Heeb, M.J.4
  • 52
    • 68549127071 scopus 로고    scopus 로고
    • Plasma protein S contains zinc essential for efficient activated protein C-independent anticoagulant activity and binding to factor Xa, but not for efficient binding to tissue factor pathway inhibitor
    • M.J. Heeb, D. Prashun, J.H. Griffin, and B.N. Bouma Plasma protein S contains zinc essential for efficient activated protein C-independent anticoagulant activity and binding to factor Xa, but not for efficient binding to tissue factor pathway inhibitor FASEB J 23 2009 2244 2253
    • (2009) FASEB J , vol.23 , pp. 2244-2253
    • Heeb, M.J.1    Prashun, D.2    Griffin, J.H.3    Bouma, B.N.4
  • 53
    • 84874709181 scopus 로고    scopus 로고
    • Platelet protein S directly inhibits procoagulant activity on platelets and microparticles
    • F. Stavenuiter, N.F. Davis, E. Duan, A.J. Gale, and M.J. Heeb Platelet protein S directly inhibits procoagulant activity on platelets and microparticles Thromb Haemost 109 2013 229 237
    • (2013) Thromb Haemost , vol.109 , pp. 229-237
    • Stavenuiter, F.1    Davis, N.F.2    Duan, E.3    Gale, A.J.4    Heeb, M.J.5
  • 54
    • 33644772164 scopus 로고    scopus 로고
    • Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor
    • T.M. Hackeng, K.M. Sere, G. Tans, and J. Rosing Protein S stimulates inhibition of the tissue factor pathway by tissue factor pathway inhibitor Proc Natl Acad Sci U S A 103 2006 3106 3111
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3106-3111
    • Hackeng, T.M.1    Sere, K.M.2    Tans, G.3    Rosing, J.4
  • 55
    • 9444273450 scopus 로고    scopus 로고
    • Inhibition of thrombin generation by protein S at low procoagulant stimuli: Implications for maintenance of the hemostatic balance
    • K.M. Sere, J. Rosing, and T.M. Hackeng Inhibition of thrombin generation by protein S at low procoagulant stimuli: implications for maintenance of the hemostatic balance Blood 104 2004 3624 3630
    • (2004) Blood , vol.104 , pp. 3624-3630
    • Sere, K.M.1    Rosing, J.2    Hackeng, T.M.3
  • 56
    • 74749084650 scopus 로고    scopus 로고
    • Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma
    • E. Castoldi, P. Simioni, D. Tormene, J. Rosing, and T.M. Hackeng Hereditary and acquired protein S deficiencies are associated with low TFPI levels in plasma J Thromb Haemost 8 2010 294 300
    • (2010) J Thromb Haemost , vol.8 , pp. 294-300
    • Castoldi, E.1    Simioni, P.2    Tormene, D.3    Rosing, J.4    Hackeng, T.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.