메뉴 건너뛰기




Volumn 92, Issue 3, 2004, Pages 467-477

Mouse models of thrombosis: Thrombomodulin

Author keywords

Mouse models; Protein C; Thrombomodulin

Indexed keywords

ANTICOAGULANT AGENT; PROTEIN C; THROMBIN; THROMBOMODULIN; ANTICOAGULANT PROTEIN;

EID: 12344277910     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH04-05-0307     Document Type: Review
Times cited : (33)

References (87)
  • 1
    • 0025174705 scopus 로고
    • Structure and function of thrombomodulin: A natural anticoagulant
    • Dittman WA, Majerus PW. Structure and function of thrombomodulin: a natural anticoagulant. Blood 1990; 75: 329-36.
    • (1990) Blood , vol.75 , pp. 329-336
    • Dittman, W.A.1    Majerus, P.W.2
  • 2
    • 0030843884 scopus 로고    scopus 로고
    • Thrombomodulin structure and function
    • Sadler JE. Thrombomodulin structure and function. Thromb Haemost 1997; 78: 392-5.
    • (1997) Thromb. Haemost. , vol.78 , pp. 392-395
    • Sadler, J.E.1
  • 3
    • 0032845209 scopus 로고    scopus 로고
    • Regulation and functions of the protein C anticoagulant pathway
    • Esmon CT, Gu JM, Xu J, et al. Regulation and functions of the protein C anticoagulant pathway. Haematologica 1999; 84: 363-8.
    • (1999) Haematologica , vol.84 , pp. 363-368
    • Esmon, C.T.1    Gu, J.M.2    Xu, J.3
  • 4
    • 0035222641 scopus 로고    scopus 로고
    • The normal role of Activated Protein C in maintaining homeostasis and its relevance to critical illness
    • Esmon CT. The normal role of Activated Protein C in maintaining homeostasis and its relevance to critical illness. Crit Care 2001; 5: S7-S12.
    • (2001) Crit. Care , vol.5
    • Esmon, C.T.1
  • 5
    • 0035869411 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor plays an important role in protein C activation in vivo
    • Taylor FB, Jr., Peer GT, Lockhart MS, et al. Endothelial cell protein C receptor plays an important role in protein C activation in vivo. Blood 2001; 97: 1685-8.
    • (2001) Blood , vol.97 , pp. 1685-1688
    • Taylor Jr., F.B.1    Peer, G.T.2    Lockhart, M.S.3
  • 6
    • 0033525831 scopus 로고    scopus 로고
    • Reconstitution of the human endothelial cell protein C receptor with thrombomodulin in phosphatidylcholine vesicles enhances protein C activation
    • Xu J, Esmon NL, Esmon CT. Reconstitution of the human endothelial cell protein C receptor with thrombomodulin in phosphatidylcholine vesicles enhances protein C activation. J Biol Chem 1999; 274: 6704-10.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6704-6710
    • Xu, J.1    Esmon, N.L.2    Esmon, C.T.3
  • 7
    • 0036336456 scopus 로고    scopus 로고
    • Distribution of endothelial cell protein C/activated protein C receptor (EPCR) during mouse embryo development
    • Crawley JT, Gu JM, Ferrell G, et al. Distribution of endothelial cell protein C/activated protein C receptor (EPCR) during mouse embryo development. Thromb Haemost 2002; 88: 259-66.
    • (2002) Thromb. Haemost. , vol.88 , pp. 259-266
    • Crawley, J.T.1    Gu, J.M.2    Ferrell, G.3
  • 8
    • 0030776168 scopus 로고    scopus 로고
    • Human protein C receptor is present primarily on endothelium, of large blood vessels: Implications for the control of the protein C pathway
    • Laszik Z, Mitro A, Taylor FB, Jr., et al. Human protein C receptor is present primarily on endothelium, of large blood vessels: implications for the control of the protein C pathway. Circulation 1997; 96: 3633-40.
    • (1997) Circulation , vol.96 , pp. 3633-3640
    • Laszik, Z.1    Mitro, A.2    Taylor Jr., F.B.3
  • 9
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • Broze GJ, Jr., Higuchi DA. Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma. Blood 1996; 88: 3815-23.
    • (1996) Blood , vol.88 , pp. 3815-3823
    • Broze Jr., G.J.1    Higuchi, D.A.2
  • 10
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, et al. Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb Haemost 1997; 78: 386-91.
    • (1997) Thromb. Haemost. , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3
  • 11
    • 0033675696 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway
    • Bajzar L. Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway. Arterioscler Thromb Vasc Biol 2000; 20: 2511-8.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2511-2518
    • Bajzar, L.1
  • 12
    • 0345803939 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation
    • Myles T, Nishimura T, Yun TH, et al. Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation. J Biol Chem 2003; 278: 51059-67.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51059-51067
    • Myles, T.1    Nishimura, T.2    Yun, T.H.3
  • 13
    • 0034996440 scopus 로고    scopus 로고
    • Carboxy-peptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis
    • Campbell W, Okada N, Okada H. Carboxy-peptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis. Immunol Rev 2001; 180: 162-7.
    • (2001) Immunol. Rev. , vol.180 , pp. 162-167
    • Campbell, W.1    Okada, N.2    Okada, H.3
  • 14
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell WD, Lazoura E, Okada N, et al. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol Immunol 2002; 46: 131-4.
    • (2002) Microbiol. Immunol. , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3
  • 15
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • Riewald M, Petrovan RJ, Donner A, et al. Activation of endothelial cell protease activated receptor 1 by the protein C pathway. Science 2002; 296: 1880-2.
    • (2002) Science , vol.296 , pp. 1880-1882
    • Riewald, M.1    Petrovan, R.J.2    Donner, A.3
  • 16
    • 0036271051 scopus 로고    scopus 로고
    • Orchestration of coagulation protease signaling by tissue factor
    • Riewald M, Ruf W. Orchestration of coagulation protease signaling by tissue factor. Trends Cardiovasc Med 2002; 12: 149-54.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 149-154
    • Riewald, M.1    Ruf, W.2
  • 17
    • 0022891349 scopus 로고
    • Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor
    • Jackman RW, Beeler DL, VanDeWater L, et al. Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor. Proc Natl Acad Sci U S A 1986; 83: 8834-8.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8834-8838
    • Jackman, R.W.1    Beeler, D.L.2    VanDeWater, L.3
  • 18
    • 0034006172 scopus 로고    scopus 로고
    • Solution structure of the smallest cofactor-active fragment of thrombomodulin
    • Wood MJ, Sampoli Benitez BA, et al. Solution structure of the smallest cofactor-active fragment of thrombomodulin. Nat Struct Biol 2000; 7: 200-4.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 200-204
    • Wood, M.J.1    Sampoli Benitez, B.A.2
  • 19
    • 0034732094 scopus 로고    scopus 로고
    • Structural basis for the anticoagulant activity of the thrombin- thrombomodulin complex
    • Fuentes-Prior P, Iwanaga Y, Huber R, et al. Structural basis for the anticoagulant activity of the thrombin- thrombomodulin complex. Nature 2000; 404: 518-25.
    • (2000) Nature , vol.404 , pp. 518-525
    • Fuentes-Prior, P.1    Iwanaga, Y.2    Huber, R.3
  • 20
    • 0035831506 scopus 로고    scopus 로고
    • Molecular cloning and characterization of endosialin, a C-type lectin-like cell surface receptor of tumor endothelium
    • Christian S, Ahorn H, Koehler A, et al. Molecular cloning and characterization of endosialin, a C-type lectin-like cell surface receptor of tumor endothelium. J Biol Chem 2001; 276: 7408-14.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7408-7414
    • Christian, S.1    Ahorn, H.2    Koehler, A.3
  • 21
    • 0024284252 scopus 로고
    • The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins
    • Petersen TE. The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins. FEBS Lett 1988; 231: 51-3.
    • (1988) FEBS Lett. , vol.231 , pp. 51-53
    • Petersen, T.E.1
  • 22
    • 0034602262 scopus 로고    scopus 로고
    • Molecular and cellular properties of the rat AA4 antigen, a C-type lectin-like receptor with structural homology to thrombomodulin
    • Dean YD, McGreal EP, Akatsu H, et al. Molecular and cellular properties of the rat AA4 antigen, a C-type lectin-like receptor with structural homology to thrombomodulin. J Biol Chem 2000; 275: 34382-92.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34382-34392
    • Dean, Y.D.1    McGreal, E.P.2    Akatsu, H.3
  • 23
    • 0031023957 scopus 로고    scopus 로고
    • The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis
    • Conway EM, Pollefeyt S, Collen D, et al. The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis. Blood 1997; 89: 652-61.
    • (1997) Blood , vol.89 , pp. 652-661
    • Conway, E.M.1    Pollefeyt, S.2    Collen, D.3
  • 24
    • 0000686636 scopus 로고    scopus 로고
    • Thrombomodulin modulates growth of tumor cells independent of its anticoagulant activity
    • Zhang Y, Weiler-Guettler H, Chen J, et al. Thrombomodulin modulates growth of tumor cells independent of its anticoagulant activity. J Clin Invest 1998; 101: 1301-9.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1301-1309
    • Zhang, Y.1    Weiler-Guettler, H.2    Chen, J.3
  • 25
    • 0036719075 scopus 로고    scopus 로고
    • The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor kappaB and mitogen-activated protein kinase pathways
    • Conway EM, Van de Wouwer M, Pollefeyt S, et al. The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor kappaB and mitogen-activated protein kinase pathways. J Exp Med 2002; 196: 565-77.
    • (2002) J. Exp. Med. , vol.196 , pp. 565-577
    • Conway, E.M.1    Van de Wouwer, M.2    Pollefeyt, S.3
  • 26
    • 0029958045 scopus 로고    scopus 로고
    • The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy
    • Weisel JW, Nagaswami C, Young TA, et al. The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy. J Biol Chem 1996; 271: 31485-90.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31485-31490
    • Weisel, J.W.1    Nagaswami, C.2    Young, T.A.3
  • 28
    • 0025050474 scopus 로고
    • Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan
    • Bourin MC, Lundgren-Akerlund E, Lindahl U. Isolation and characterization of the glycosaminoglycan component of rabbit thrombomodulin proteoglycan. J Biol Chem 1990; 265: 15424-31.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15424-15431
    • Bourin, M.C.1    Lundgren-Akerlund, E.2    Lindahl, U.3
  • 29
    • 0027567887 scopus 로고
    • Structure-function relationships of the thrombin-thrombomodulin interaction
    • Sadler JE, Lentz SR, Sheehan JP, et al. Structure-function relationships of the thrombin-thrombomodulin interaction. Haemostasis 1993; 23 Suppl 1: 183-93.
    • (1993) Haemostasis , vol.23 , Issue.SUPPL. 1 , pp. 183-193
    • Sadler, J.E.1    Lentz, S.R.2    Sheehan, J.P.3
  • 30
    • 0026775230 scopus 로고
    • Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity
    • Tsiang M, Lentz SR, Sadler JE. Functional domains of membrane-bound human thrombomodulin. EGF-like domains four to six and the serine/threonine-rich domain are required for cofactor activity. J Biol Chem 1992; 267: 6164-70.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6164-6170
    • Tsiang, M.1    Lentz, S.R.2    Sadler, J.E.3
  • 31
    • 0032524918 scopus 로고    scopus 로고
    • Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C
    • Kokame K, Zheng X, Sadler JE. Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C. J Biol Chem 1998; 273: 12135-9.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12135-12139
    • Kokame, K.1    Zheng, X.2    Sadler, J.E.3
  • 32
    • 0034532008 scopus 로고    scopus 로고
    • Dissociation of thrombin's substrate interactions using site-directed mutagenesis
    • Leung LL, Hall SW. Dissociation of thrombin's substrate interactions using site-directed mutagenesis. Trends Cardiovasc Med 2000; 10: 89-92.
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 89-92
    • Leung, L.L.1    Hall, S.W.2
  • 33
    • 0033520366 scopus 로고    scopus 로고
    • Thrombin interacts with thrombomodulin, protein C, and thrombin- activatable fibrinolysis inhibitor via specific and distinct domains
    • Hall SW, Nagashima M, Zhao L, et al. Thrombin interacts with thrombomodulin, protein C, and thrombin- activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 1999; 274: 25510-16.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25510-25516
    • Hall, S.W.1    Nagashima, M.2    Zhao, L.3
  • 34
    • 0034725622 scopus 로고    scopus 로고
    • Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation
    • Wang W, Nagashima M, Schneider M, et al. Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation. J Biol Chem 2000; 275: 22942-7.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22942-22947
    • Wang, W.1    Nagashima, M.2    Schneider, M.3
  • 35
    • 0025228843 scopus 로고
    • Domain structure of the endothelial cell receptor thrombomodulin as deduced from modulation of its anticoagulant functions. Evidence for a glycosaminoglycan-dependent secondary binding site for thrombin
    • Preissner KT, Koyama T, Muller D, et al. Domain structure of the endothelial cell receptor thrombomodulin as deduced from modulation of its anticoagulant functions. Evidence for a glycosaminoglycan-dependent secondary binding site for thrombin. J Biol Chem 1990; 265: 4915-22.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4915-4922
    • Preissner, K.T.1    Koyama, T.2    Muller, D.3
  • 36
    • 0027407874 scopus 로고
    • The chondroitin sulfate moiety of thrombomodulin binds a second molecule of thrombin
    • Ye J, Esmon CT, Johnson AE. The chondroitin sulfate moiety of thrombomodulin binds a second molecule of thrombin. J Biol Chem 1993; 268: 2373-9.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2373-2379
    • Ye, J.1    Esmon, C.T.2    Johnson, A.E.3
  • 37
    • 0032910609 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes: A mutational analysis of cytoadherence via murine thrombomodulin
    • Rabhi-Sabile S, Steiner-Mosonyi M, Pollefeyt S, et al. Plasmodium falciparum-infected erythrocytes: a mutational analysis of cytoadherence via murine thrombomodulin. Thromb Haemost 1999; 81: 815-21.
    • (1999) Thromb. Haemost. , vol.81 , pp. 815-821
    • Rabhi-Sabile, S.1    Steiner-Mosonyi, M.2    Pollefeyt, S.3
  • 38
    • 0030740121 scopus 로고    scopus 로고
    • Chondroitin sulfate of thrombomodulin is an adhesion receptor for Plasmodium falciparum-infected erythrocytes
    • Gysin J, Pouvelle B, Le Tonqueze M, et al. Chondroitin sulfate of thrombomodulin is an adhesion receptor for Plasmodium falciparum-infected erythrocytes. Mol Biochem Parasitol 1997; 88: 267-71.
    • (1997) Mol. Biochem. Parasitol. , vol.88 , pp. 267-271
    • Gysin, J.1    Pouvelle, B.2    Le Tonqueze, M.3
  • 39
    • 0029050715 scopus 로고
    • The epidermal growth factor-like domain of recombinant human thrombomodulin exhibits mitogenic activity for Swiss 3T3 cells
    • Hamada H, Ishii H, Sakyo K, et al. The epidermal growth factor-like domain of recombinant human thrombomodulin exhibits mitogenic activity for Swiss 3T3 cells. Blood 1995; 86: 225-33.
    • (1995) Blood , vol.86 , pp. 225-233
    • Hamada, H.1    Ishii, H.2    Sakyo, K.3
  • 40
    • 0034161456 scopus 로고    scopus 로고
    • Role of hemostatic gene polymorphisms in venous and arterial thrombotic disease
    • Lane DA, Grant PJ. Role of hemostatic gene polymorphisms in venous and arterial thrombotic disease. Blood 2000; 95: 1517-32.
    • (2000) Blood , vol.95 , pp. 1517-1532
    • Lane, D.A.1    Grant, P.J.2
  • 41
    • 0027986812 scopus 로고
    • Factor V Leiden - An unselfish gene?
    • Hajjar KA. Factor V Leiden - an unselfish gene? N Engl J Med 1994; 331: 1585-7.
    • (1994) N. Engl. J. Med. , vol.331 , pp. 1585-1587
    • Hajjar, K.A.1
  • 42
    • 0028765167 scopus 로고
    • Human genetics. Bad blood by mutation
    • Majerus PW. Human genetics. Bad blood by mutation. Nature 1994; 369: 14-15.
    • (1994) Nature , vol.369 , pp. 14-15
    • Majerus, P.W.1
  • 43
    • 0142245617 scopus 로고    scopus 로고
    • Survival advantage associated with heterozygous factor V Leiden mutation in patients with severe sepsis and in mouse endotoxemia
    • Kerlin BA, Yan SB, Isermann BH, et al. Survival advantage associated with heterozygous factor V Leiden mutation in patients with severe sepsis and in mouse endotoxemia. Blood 2003; 102: 3085-92.
    • (2003) Blood , vol.102 , pp. 3085-3092
    • Kerlin, B.A.1    Yan, S.B.2    Isermann, B.H.3
  • 44
    • 0037093228 scopus 로고    scopus 로고
    • Naturally occurring mutations in the thrombomodulin gene leading to impaired expression and function
    • Kunz G, Ohlin AK, Adami A, et al. Naturally occurring mutations in the thrombomodulin gene leading to impaired expression and function. Blood 2002;9 9: 3646-53.
    • (2002) Blood , vol.99 , pp. 3646-3653
    • Kunz, G.1    Ohlin, A.K.2    Adami, A.3
  • 45
    • 0033594760 scopus 로고    scopus 로고
    • Soluble thrombomodulin as a predictor of incident coronary heart disease and symptomless carotid artery atherosclerosis in the Atherosclerosis Risk in Communities (ARIC) Study: A case-cohort study
    • Salomaa V, Matei C, Aleksic N, et al. Soluble thrombomodulin as a predictor of incident coronary heart disease and symptomless carotid artery atherosclerosis in the Atherosclerosis Risk in Communities (ARIC) Study: a case-cohort study. Lancet 1999; 353: 1729-34.
    • (1999) Lancet , vol.353 , pp. 1729-1734
    • Salomaa, V.1    Matei, C.2    Aleksic, N.3
  • 46
    • 0028876697 scopus 로고
    • Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system
    • Healy AM, Rayburn HB, Rosenberg RD, et al. Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system. Proc Natl Acad Sci USA 1995; 92: 850-4.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 850-854
    • Healy, A.M.1    Rayburn, H.B.2    Rosenberg, R.D.3
  • 47
    • 0030054055 scopus 로고    scopus 로고
    • Targeting of transgene expression to the vascular endothelium of mice by homologous recombination at the thrombomodulin locus
    • Weiler-Guettler H, Aird WC, Husain M, et al. Targeting of transgene expression to the vascular endothelium of mice by homologous recombination at the thrombomodulin locus. Circ Res 1996; 78: 180-7.
    • (1996) Circ. Res. , vol.78 , pp. 180-187
    • Weiler-Guettler, H.1    Aird, W.C.2    Husain, M.3
  • 48
    • 0030040061 scopus 로고    scopus 로고
    • Developmentally regulated gene expression of thrombomodulin in postimplantation mouse embryos
    • Weiler-Guettler H, Aird WC, Rayburn H, et al. Developmentally regulated gene expression of thrombomodulin in postimplantation mouse embryos. Development 1996; 122: 2271-81.
    • (1996) Development , vol.122 , pp. 2271-2281
    • Weiler-Guettler, H.1    Aird, W.C.2    Rayburn, H.3
  • 49
    • 0034892611 scopus 로고    scopus 로고
    • Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis
    • Isermann B, Hendrickson SB, Zogg M, et al. Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis. J Clin Invest 2001; 108: 537-46.
    • (2001) J. Clin. Invest. , vol.108 , pp. 537-546
    • Isermann, B.1    Hendrickson, S.B.2    Zogg, M.3
  • 50
    • 0032080409 scopus 로고    scopus 로고
    • A targeted point mutation in thrombomodulin generates viable mice with a prethrombotic state
    • Weiler-Guettler H, Christie PD, Beeler DL, et al. A targeted point mutation in thrombomodulin generates viable mice with a prethrombotic state. J Clin Invest 1998; 101: 1983-91.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1983-1991
    • Weiler-Guettler, H.1    Christie, P.D.2    Beeler, D.L.3
  • 51
    • 0035572892 scopus 로고    scopus 로고
    • Characterization of a mouse model for thrombomodulin deficiency
    • Weiler H, Lindner V, Kerlin B, et al. Characterization of a mouse model for thrombomodulin deficiency. Arterioscler Thromb Vasc Biol 2001; 21: 1531-7.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1531-1537
    • Weiler, H.1    Lindner, V.2    Kerlin, B.3
  • 52
    • 0033562859 scopus 로고    scopus 로고
    • Structure-function analyses of thrombomodulin by gene-targeting in mice: The cytoplasmic domain is not required for normal fetal development
    • Conway EM, Pollefeyt S, Cornelissen J, et al. Structure-function analyses of thrombomodulin by gene-targeting in mice: the cytoplasmic domain is not required for normal fetal development. Blood 1999; 93: 3442-50.
    • (1999) Blood , vol.93 , pp. 3442-3450
    • Conway, E.M.1    Pollefeyt, S.2    Cornelissen, J.3
  • 54
    • 0035406530 scopus 로고    scopus 로고
    • Placental development: Lessons from mouse mutants
    • Rossant J, Cross JC. Placental development: lessons from mouse mutants. Nat Rev Genet 2001; 2: 538-48.
    • (2001) Nat. Rev. Genet , vol.2 , pp. 538-548
    • Rossant, J.1    Cross, J.C.2
  • 55
    • 0033933153 scopus 로고    scopus 로고
    • The labyrinthine placenta
    • Rinkenberger J, Werb Z. The labyrinthine placenta. Nat Genet 2000; 25: 248-50.
    • (2000) Nat. Genet , vol.25 , pp. 248-250
    • Rinkenberger, J.1    Werb, Z.2
  • 56
    • 0036399622 scopus 로고    scopus 로고
    • Interactions between trophoblast cells and the maternal and fetal circulation in the mouse placenta
    • Adamson SL, Lu Y, Whiteley KJ, et al. Interactions between trophoblast cells and the maternal and fetal circulation in the mouse placenta. Dev Biol 2002; 250: 358-73.
    • (2002) Dev. Biol. , vol.250 , pp. 358-373
    • Adamson, S.L.1    Lu, Y.2    Whiteley, K.J.3
  • 57
    • 0019378232 scopus 로고
    • Review article: Trophoblast invasion and the establishment of haemochorial placentation in man and laboratory animals
    • Pijnenborg R, Robertson WB, Brosens I, et al. Review article: trophoblast invasion and the establishment of haemochorial placentation in man and laboratory animals. Placenta 1981; 2: 71-91.
    • (1981) Placenta , vol.2 , pp. 71-91
    • Pijnenborg, R.1    Robertson, W.B.2    Brosens, I.3
  • 58
    • 0035070573 scopus 로고    scopus 로고
    • Tissue-restricted expression of thrombomodulin in the placenta rescues thrombomodulin-deficient mice from early lethality and reveals a secondary developmental block
    • Isermann B, Hendrickson SB, Hutley K, et al. Tissue-restricted expression of thrombomodulin in the placenta rescues thrombomodulin-deficient mice from early lethality and reveals a secondary developmental block. Development 2001; 128: 827-38.
    • (2001) Development , vol.128 , pp. 827-838
    • Isermann, B.1    Hendrickson, S.B.2    Hutley, K.3
  • 59
    • 0037349926 scopus 로고    scopus 로고
    • The thrombomodulin-protein C system is essential for the maintenance of pregnancy
    • Isermann B, Sood R, Pawlinski R, et al. The thrombomodulin-protein C system is essential for the maintenance of pregnancy. Nat Med 2003; 9: 331-7.
    • (2003) Nat. Med. , vol.9 , pp. 331-337
    • Isermann, B.1    Sood, R.2    Pawlinski, R.3
  • 60
    • 16044369784 scopus 로고    scopus 로고
    • Increased fetal loss in women with heritable thrombophilia
    • Preston FE, Rosendaal FR, Walker ID, et al. Increased fetal loss in women with heritable thrombophilia. Lancet 1996; 348: 913-6.
    • (1996) Lancet , vol.348 , pp. 913-916
    • Preston, F.E.1    Rosendaal, F.R.2    Walker, I.D.3
  • 61
    • 0034610031 scopus 로고    scopus 로고
    • Mutations in coagulation factors in women with unexplained late fetal loss
    • Martinelli I, Taioli E, Cetin I, et al. Mutations in coagulation factors in women with unexplained late fetal loss. N Engl J Med 2000; 343: 1015-8.
    • (2000) N. Engl. J. Med. , vol.343 , pp. 1015-1018
    • Martinelli, I.1    Taioli, E.2    Cetin, I.3
  • 62
    • 0033531184 scopus 로고    scopus 로고
    • Increased frequency of genetic thrombophilia in women with complications of pregnancy
    • Kupferminc MJ, Eldor A, Steinman N, et al. Increased frequency of genetic thrombophilia in women with complications of pregnancy. N Engl J Med 1999; 340: 9-13.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 9-13
    • Kupferminc, M.J.1    Eldor, A.2    Steinman, N.3
  • 63
    • 0034786207 scopus 로고    scopus 로고
    • Mutations in the thrombomodulin and endothelial protein C receptor genes in women with late fetal loss
    • Franchi F, Biguzzi E, Cetin I, et al. Mutations in the thrombomodulin and endothelial protein C receptor genes in women with late fetal loss. Br J Haematol 2001; 114: 641-6.
    • (2001) Br. J. Haematol. , vol.114 , pp. 641-646
    • Franchi, F.1    Biguzzi, E.2    Cetin, I.3
  • 64
    • 0037443934 scopus 로고    scopus 로고
    • Thrombophilic disorders and fetal loss: A meta-analysis
    • Rey E, Kahn SR, David M, et al. Thrombophilic disorders and fetal loss: a meta-analysis. Lancet 2003; 361: 901-8.
    • (2003) Lancet , vol.361 , pp. 901-908
    • Rey, E.1    Kahn, S.R.2    David, M.3
  • 67
    • 0034922910 scopus 로고    scopus 로고
    • Thrombophilia, thrombosis and pregnancy
    • Eldor A. Thrombophilia, thrombosis and pregnancy. Thromb Haemost 2001; 86: 104-11.
    • (2001) Thromb. Haemost. , vol.86 , pp. 104-111
    • Eldor, A.1
  • 68
    • 0037019327 scopus 로고    scopus 로고
    • Clotting and hemorrhage in the placenta - A delicate balance
    • Roberts D, Schwartz RS. Clotting and hemorrhage in the placenta - a delicate balance. N Engl J Med 2002; 347: 57-9.
    • (2002) N. Engl. J. Med. , vol.347 , pp. 57-59
    • Roberts, D.1    Schwartz, R.S.2
  • 69
    • 0035696180 scopus 로고    scopus 로고
    • Pathologic features of the placenta in women with severe pregnancy complications and thrombophilia
    • Many A, Schreiber L, Rosner S, et al. Pathologic features of the placenta in women with severe pregnancy complications and thrombophilia. Obstet Gynecol 2001; 98: 1041-4.
    • (2001) Obstet. Gynecol. , vol.98 , pp. 1041-1044
    • Many, A.1    Schreiber, L.2    Rosner, S.3
  • 70
    • 0036547768 scopus 로고    scopus 로고
    • Placental pathology in early onset pre-eclampsia and intra-uterine growth restriction in women with and without thrombophilia
    • Sikkema JM, Franx A, Bruinse HW, et al. Placental pathology in early onset pre-eclampsia and intra-uterine growth restriction in women with and without thrombophilia. Placenta 2002; 23: 337-42.
    • (2002) Placenta , vol.23 , pp. 337-342
    • Sikkema, J.M.1    Franx, A.2    Bruinse, H.W.3
  • 71
    • 0033868908 scopus 로고    scopus 로고
    • Do placental lesions reflect thrombophilia state in women with adverse pregnancy outcome?
    • Mousa HA, Alfirevic Z. Do placental lesions reflect thrombophilia state in women with adverse pregnancy outcome? Hum Reprod 2000; 15: 1830-3.
    • (2000) Hum. Reprod. , vol.15 , pp. 1830-1833
    • Mousa, H.A.1    Alfirevic, Z.2
  • 72
    • 0033803337 scopus 로고    scopus 로고
    • Frequency of factor V(Leiden) and prothrombin G20210A in placentas and their relationship with placental lesions
    • Vern TZ, Alles AJ, Kowal-Vern A, et al. Frequency of factor V(Leiden) and prothrombin G20210A in placentas and their relationship with placental lesions. Hum Pathol 2000; 31: 1036-43.
    • (2000) Hum. Pathol. , vol.31 , pp. 1036-1043
    • Vern, T.Z.1    Alles, A.J.2    Kowal-Vern, A.3
  • 73
    • 0033662205 scopus 로고    scopus 로고
    • Placental defects in ARNT-knockout conceptus correlate with localized decreases in VEGF-R2, Ang-1, and Tie-2
    • Abbott BD, Buckalew AR. Placental defects in ARNT-knockout conceptus correlate with localized decreases in VEGF-R2, Ang-1, and Tie-2. Dev Dyn 2000; 219: 526-38.
    • (2000) Dev. Dyn. , vol.219 , pp. 526-538
    • Abbott, B.D.1    Buckalew, A.R.2
  • 74
    • 0033870151 scopus 로고    scopus 로고
    • Angiopoietin-1 and angiopoietin-2 activate trophoblast Tie-2 to promote growth and migration during placental development
    • Dunk C, Shams M, Nijjar S, et al. Angiopoietin-1 and angiopoietin-2 activate trophoblast Tie-2 to promote growth and migration during placental development. Am J Pathol 2000; 156: 2185-99.
    • (2000) Am. J. Pathol. , vol.156 , pp. 2185-2199
    • Dunk, C.1    Shams, M.2    Nijjar, S.3
  • 75
    • 0033960046 scopus 로고    scopus 로고
    • Tie-2 and angiopoietin-2 expression at the fetal-maternal interface: A receptor ligand model for vascular remodelling
    • Goldman-Wohl DS, Ariel I, Greenfield C, et al. Tie-2 and angiopoietin-2 expression at the fetal-maternal interface: a receptor ligand model for vascular remodelling. Mol Hum Reprod 2000; 6: 81-7.
    • (2000) Mol. Hum. Reprod. , vol.6 , pp. 81-87
    • Goldman-Wohl, D.S.1    Ariel, I.2    Greenfield, C.3
  • 76
    • 0030922747 scopus 로고    scopus 로고
    • Human cytotrophoblasts adopt a vascular phenotype as they differentiate. A strategy for successful endovascular invasion?
    • Zhou Y, Fisher SJ, Janatpour M, et al. Human cytotrophoblasts adopt a vascular phenotype as they differentiate. A strategy for successful endovascular invasion? J Clin Invest 1997; 99: 2139-51.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2139-2151
    • Zhou, Y.1    Fisher, S.J.2    Janatpour, M.3
  • 77
    • 0030979721 scopus 로고    scopus 로고
    • Preeclampsia is associated with failure of human cytotrophoblasts to mimic a vascular adhesion phenotype. One cause of defective endovascular invasion in this syndrome?
    • Zhou Y, Damsky CH, Fisher SJ. Preeclampsia is associated with failure of human cytotrophoblasts to mimic a vascular adhesion phenotype. One cause of defective endovascular invasion in this syndrome? J Clin Invest 1997; 99: 2152-64.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2152-2164
    • Zhou, Y.1    Damsky, C.H.2    Fisher, S.J.3
  • 78
    • 0036143120 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life
    • Nagashima M, Yin ZF, Zhao L, et al. Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life. J Clin Invest 2002; 109: 101-10.
    • (2002) J. Clin. Invest. , vol.109 , pp. 101-110
    • Nagashima, M.1    Yin, Z.F.2    Zhao, L.3
  • 79
    • 0842311473 scopus 로고    scopus 로고
    • Impaired healing of cutaneous wounds and colonic anastomoses in mice lacking thrombin-activatable fibrinolysis inhibitor
    • te Velde EA, Wagenaar GT, Reijerkerk A, et al. Impaired healing of cutaneous wounds and colonic anastomoses in mice lacking thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost 2003; 1: 2087-96.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2087-2096
    • te Velde, E.A.1    Wagenaar, G.T.2    Reijerkerk, A.3
  • 80
    • 0038115187 scopus 로고    scopus 로고
    • Aggravation of endotoxin-induced disseminated intravascular coagulation and cytokine activation in heterozygous protein-C-deficient mice
    • Levi M, Dorffler-Melly J, Reitsma P, et al. Aggravation of endotoxin-induced disseminated intravascular coagulation and cytokine activation in heterozygous protein-C-deficient mice. Blood 2003; 101: 4823-7.
    • (2003) Blood , vol.101 , pp. 4823-4827
    • Levi, M.1    Dorffler-Melly, J.2    Reitsma, P.3
  • 81
    • 0242383506 scopus 로고    scopus 로고
    • Functional thrombomodulin deficiency causes enhanced thrombus growth in a murine model of carotid artery thrombosis
    • Dorffler-Melly J, de Kruif M, Schwarte LA, et al. Functional thrombomodulin deficiency causes enhanced thrombus growth in a murine model of carotid artery thrombosis. Basic Res Cardiol 2003; 98: 347-52.
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 347-352
    • Dorffler-Melly, J.1    de Kruif, M.2    Schwarte, L.A.3
  • 82
    • 0032402132 scopus 로고    scopus 로고
    • Intravascular coagulation activation in a murine model of thrombomodulin deficiency: Effects of lesion size, age, and hypoxia on fibrin deposition
    • Healy AM, Hancock WW, Christie PD, et al. Intravascular coagulation activation in a murine model of thrombomodulin deficiency: effects of lesion size, age, and hypoxia on fibrin deposition. Blood 1998; 92: 4188-97.
    • (1998) Blood , vol.92 , pp. 4188-4197
    • Healy, A.M.1    Hancock, W.W.2    Christie, P.D.3
  • 83
    • 0032702982 scopus 로고    scopus 로고
    • A murine model of myocardial microvascular thrombosis
    • Christie PD, Edelberg JM, Picard MH, et al. A murine model of myocardial microvascular thrombosis. J Clin Invest 1999; 104: 533-9.
    • (1999) J. Clin. Invest. , vol.104 , pp. 533-539
    • Christie, P.D.1    Edelberg, J.M.2    Picard, M.H.3
  • 84
    • 10744231546 scopus 로고    scopus 로고
    • Cause-effect relation between hyperfibrinogenemia and vascular disease
    • Kerlin B, Cooley BC, Isermann BH, et al. Cause-effect relation between hyperfibrinogenemia and vascular disease. Blood 2004; 103: 1728-34.
    • (2004) Blood , vol.103 , pp. 1728-1734
    • Kerlin, B.1    Cooley, B.C.2    Isermann, B.H.3
  • 85
    • 0032532678 scopus 로고    scopus 로고
    • Inactivation of the gene for anticoagulant protein C causes lethal perinatal consumptive coagulopathy in mice
    • Jalbert LR, Rosen ED, Moons L, et al. Inactivation of the gene for anticoagulant protein C causes lethal perinatal consumptive coagulopathy in mice. J Clin Invest 1998; 102: 1481-8.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1481-1488
    • Jalbert, L.R.1    Rosen, E.D.2    Moons, L.3
  • 86
    • 0037044806 scopus 로고    scopus 로고
    • Disruption of the endothelial cell protein C receptor gene in mice causes placental thrombosis and early embryonic lethality
    • Gu JM, Crawley JT, Ferrell G, et al. Disruption of the endothelial cell protein C receptor gene in mice causes placental thrombosis and early embryonic lethality. J Biol Chem 2002; 277: 43335-43.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43335-43343
    • Gu, J.M.1    Crawley, J.T.2    Ferrell, G.3
  • 87
    • 0034672363 scopus 로고    scopus 로고
    • Spontaneous thrombosis in mice carrying the factor V Leiden mutation
    • Cui J, Eitzman DT, Westrick RJ, et al. Spontaneous thrombosis in mice carrying the factor V Leiden mutation. Blood 2000; 96: 4222-6.
    • (2000) Blood , vol.96 , pp. 4222-4226
    • Cui, J.1    Eitzman, D.T.2    Westrick, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.