메뉴 건너뛰기




Volumn 1, Issue 7, 2003, Pages 1515-1524

Thrombomodulin

Author keywords

Inflammation; Placenta; Thrombomodulin; Thrombosis

Indexed keywords

ANTICOAGULANT AGENT; PROTEIN C; THROMBIN; THROMBOMODULIN;

EID: 0141498158     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1046/j.1538-7836.2003.00306.x     Document Type: Review
Times cited : (231)

References (144)
  • 1
    • 0000650903 scopus 로고
    • Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Esmon CT, Owen WG. Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. Proc Natl Acad Sci USA 1981; 78: 2249-52.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2249-2252
    • Esmon, C.T.1    Owen, W.G.2
  • 2
    • 0019861825 scopus 로고
    • Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Owen WG, Esmon CT. Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. J Biol Chem 1981; 256: 5532-5.
    • (1981) J Biol Chem , vol.256 , pp. 5532-5535
    • Owen, W.G.1    Esmon, C.T.2
  • 3
    • 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
  • 4
    • 0022891349 scopus 로고
    • Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor
    • Jackman RW, Beeler DL, VanDeWater L, Rosenberg RD. Characterization of a thrombomodulin cDNA reveals structural similarity to the low density lipoprotein receptor. Proc Natl Acad Sci USA 1986; 83: 8834-8.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8834-8838
    • Jackman, R.W.1    Beeler, D.L.2    VanDeWater, L.3    Rosenberg, R.D.4
  • 5
    • 0025174705 scopus 로고
    • Structure and function of thrombomodulin: a natural anticoagulant
    • DittmanWA, 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
  • 6
    • 0034006172 scopus 로고    scopus 로고
    • Solution structure of the smallest cofactor-active fragment of thrombomodulin
    • Wood MJ, Sampoli Benitez BA, Komives EA. 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    Komives, E.A.3
  • 8
    • 0027567887 scopus 로고
    • Structure-function relationships of the thrombin-thrombomodulin interaction
    • Sadler JE, Lentz SR, Sheehan JP, Tsiang M, Wu Q. 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    Tsiang, M.4    Wu, Q.5
  • 10
    • 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
  • 11
    • 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, Gasque P. 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    Gasque, P.4
  • 12
    • 0031023957 scopus 로고    scopus 로고
    • The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis
    • Conway EM, Pollefeyt S, Collen D, Steiner-Mosonyi M. 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    Steiner-Mosonyi, M.4
  • 15
    • 0029958045 scopus 로고    scopus 로고
    • The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy
    • Weisel JW, Nagaswami C, Young TA, Light DR. 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    Light, D.R.4
  • 16
    • 0031558779 scopus 로고    scopus 로고
    • Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern
    • Sampoli Benitez BA, Hunter MJ, Meininger DP, Komives EA. Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern. J Mol Biol 1997; 273: 913-26.
    • (1997) J Mol Biol , vol.273 , pp. 913-926
    • Sampoli Benitez, B.A.1    Hunter, M.J.2    Meininger, D.P.3    Komives, E.A.4
  • 18
    • 0032560618 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin
    • Tolkatchev D, Ni F. Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin. Biochemistry 1998; 37: 9091-100.
    • (1998) Biochemistry , vol.37 , pp. 9091-9100
    • Tolkatchev, D.1    Ni, F.2
  • 19
    • 0025719626 scopus 로고
    • Aspartic acid 349 in the fourth epidermal growth factor-like structure of human thrombomodulin plays a role in its Ca (2+) -mediated binding to protein C
    • Zushi M, Gomi K, Honda G, Kondo S, Yamamoto S, Hayashi T, Suzuki K. Aspartic acid 349 in the fourth epidermal growth factor-like structure of human thrombomodulin plays a role in its Ca (2+) -mediated binding to protein C. J Biol Chem 1991; 266: 19886-9.
    • (1991) J Biol Chem , vol.266 , pp. 19886-19889
    • Zushi, M.1    Gomi, K.2    Honda, G.3    Kondo, S.4    Yamamoto, S.5    Hayashi, T.6    Suzuki, K.7
  • 20
    • 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
  • 22
    • 0032546399 scopus 로고    scopus 로고
    • The glycosylation sites and structural characteristics of oligosaccharides on recombinant human thrombomodulin
    • Edano T, Kumai N, Mizoguchi T, Ohkuchi M. The glycosylation sites and structural characteristics of oligosaccharides on recombinant human thrombomodulin. Int J Biochem Cell Biol 1998; 30: 77-88.
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 77-88
    • Edano, T.1    Kumai, N.2    Mizoguchi, T.3    Ohkuchi, M.4
  • 24
    • 0031909668 scopus 로고    scopus 로고
    • Protein C activation by recombinant thrombomodulin in plasma
    • Edano T, Komine N, Yoshizaki H, Ohkuchi M. Protein C activation by recombinant thrombomodulin in plasma. Biol Pharm Bull 1998; 21: 177-9.
    • (1998) Biol Pharm Bull , vol.21 , pp. 177-179
    • Edano, T.1    Komine, N.2    Yoshizaki, H.3    Ohkuchi, M.4
  • 25
    • 0025763975 scopus 로고
    • Different glycoforms of human thrombomodulin. Their glycosaminoglycan- dependent modulatory effects on thrombin inactivation by heparin cofactor II and antithrombin III
    • Koyama T, Parkinson JF, Sie P, Bang NU, Muller-Berghaus G, Preissner KT. Different glycoforms of human thrombomodulin. Their glycosaminoglycan- dependent modulatory effects on thrombin inactivation by heparin cofactor II and antithrombin III. Eur J Biochem 1991; 198: 563-70.
    • (1991) Eur J Biochem , vol.198 , pp. 563-570
    • Koyama, T.1    Parkinson, J.F.2    Sie, P.3    Bang, N.U.4    Muller-Berghaus, G.5    Preissner, K.T.6
  • 27
    • 0033605330 scopus 로고    scopus 로고
    • Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin. SO4- 3GlcAbeta1-3Galbeta1-3 (+/-Siaalpha2-6) Galbeta1-4Xyl
    • Wakabayashi H, Natsuka S, Mega T, Otsuki N, Isaji M, Naotsuka M, Koyama S, Kanamori T, Sakai K, Hase S. Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4- 3GlcAbeta1-3Galbeta1-3 (+/-Siaalpha2-6) Galbeta1-4Xyl. J Biol Chem 1999; 274: 5436-42.
    • (1999) J Biol Chem , vol.274 , pp. 5436-5442
    • Wakabayashi, H.1    Natsuka, S.2    Mega, T.3    Otsuki, N.4    Isaji, M.5    Naotsuka, M.6    Koyama, S.7    Kanamori, T.8    Sakai, K.9    Hase, S.10
  • 28
    • 0026506310 scopus 로고
    • Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain
    • Parkinson JF, Vlahos CJ, Yan SC, Bang NU. Recombinant human thrombomodulin. Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain. Biochem J 1992; 283: 151-7.
    • (1992) Biochem J , vol.283 , pp. 151-157
    • Parkinson, J.F.1    Vlahos, C.J.2    Yan, S.C.3    Bang, N.U.4
  • 30
    • 0034615559 scopus 로고    scopus 로고
    • Regulation of blood coagulation
    • Esmon CT. Regulation of blood coagulation. Biochim Biophys Acta 2000; 1477: 349-60.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 349-360
    • Esmon, C.T.1
  • 31
    • 0035222641 scopus 로고    scopus 로고
    • The normal role of Activated Protein C in maintaining zhomeostasis and its relevance to critical illness
    • Esmon CT. The normal role of Activated Protein C in maintaining zhomeostasis and its relevance to critical illness. Crit Care 2001; 5: S7-S12.
    • (2001) Crit Care , vol.5
    • Esmon, C.T.1
  • 32
    • 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
  • 33
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, Nagashima M, Morser J, Bajzar L. 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    Nagashima, M.4    Morser, J.5    Bajzar, L.6
  • 34
    • 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
  • 35
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell WD, Lazoura E, Okada N, Okada H. 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    Okada, H.4
  • 36
    • 0034996440 scopus 로고    scopus 로고
    • Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis
    • CampbellW, Okada N, Okada H. Carboxypeptidase 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
  • 37
    • 0027413493 scopus 로고
    • Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin
    • de Munk GA, Parkinson JF, Groeneveld E, Bang NU, Rijken DC. Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin. Biochem J 1993; 290: 655-9.
    • (1993) Biochem J , vol.290 , pp. 655-659
    • de Munk, G.A.1    Parkinson, J.F.2    Groeneveld, E.3    Bang, N.U.4    Rijken, D.C.5
  • 38
    • 0035722791 scopus 로고    scopus 로고
    • Identification of the epidermal growth factor-like domains of thrombomodulin essential for the acceleration of thrombin-mediated inactivation of single-chain urokinase-type plasminogen activator
    • Schenk-Braat EA, Morser J, Rijken DC. Identification of the epidermal growth factor-like domains of thrombomodulin essential for the acceleration of thrombin-mediated inactivation of single-chain urokinase-type plasminogen activator. Eur J Biochem 2001; 268: 5562-9.
    • (2001) Eur J Biochem , vol.268 , pp. 5562-5569
    • Schenk-Braat, E.A.1    Morser, J.2    Rijken, D.C.3
  • 39
    • 0028500821 scopus 로고
    • Inactivation of receptorbound pro-urokinase-type plasminogen activator (pro-uPA) by thrombin and thrombin/thrombomodulin complex
    • Wilhelm S,Wilhelm O, Schmitt M, Graeff H. Inactivation of receptorbound pro-urokinase-type plasminogen activator (pro-uPA) by thrombin and thrombin/thrombomodulin complex. Biol Chem Hoppe Seyler 1994; 375: 603-8.
    • (1994) Biol Chem Hoppe Seyler , vol.375 , pp. 603-608
    • Wilhelm, S.1    Wilhelm, O.2    Schmitt, M.3    Graeff, H.4
  • 40
    • 0026594613 scopus 로고
    • Thrombomodulin is a cofactor for thrombin degradation of recombinant single-chain urokinase plasminogen activator in vitro and in a perfused rabbit heart model
    • Molinari A, Giorgetti C, Lansen J, Vaghi F, Orsini G, Faioni EM, Mannucci PM. Thrombomodulin is a cofactor for thrombin degradation of recombinant single-chain urokinase plasminogen activator in vitro and in a perfused rabbit heart model. Thromb Haemost 1992; 67: 226-32.
    • (1992) Thromb Haemost , vol.67 , pp. 226-232
    • Molinari, A.1    Giorgetti, C.2    Lansen, J.3    Vaghi, F.4    Orsini, G.5    Faioni, E.M.6    Mannucci, P.M.7
  • 41
    • 0026775230 scopus 로고
    • Functional domains of membranebound 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 membranebound 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
  • 42
    • 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, Ferrell G, Esmon CT. 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    Ferrell, G.4    Esmon, C.T.5
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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
  • 46
    • 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, Morser J, Leung LL. Thrombin interacts with thrombomodulin, protein C, and thrombin- activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 1999; 274: 25510-6.
    • (1999) J Biol Chem , vol.274 , pp. 25510-25516
    • Hall, S.W.1    Nagashima, M.2    Zhao, L.3    Morser, J.4    Leung, L.L.5
  • 47
    • 0034725622 scopus 로고    scopus 로고
    • Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation
    • WangW, Nagashima M, Schneider M, Morser J, Nesheim M. 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    Morser, J.4    Nesheim, M.5
  • 48
    • 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, Tschopp J, Muller-Berghaus G. 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    Tschopp, J.4    Muller-Berghaus, G.5
  • 49
    • 0027407874 scopus 로고
    • The chondroitin sulfate moiety of thrombomodulin binds a second molecule of thrombin
    • YeJ, 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
  • 51
    • 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, Edelman L, Boffa MC. 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    Edelman, L.4    Boffa, M.C.5
  • 52
    • 0031148841 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes adhere to the proteoglycan thrombomodulin in static and flow-based systems
    • Rogerson SJ, Novakovic S, Cooke BM, Brown GV. Plasmodium falciparum-infected erythrocytes adhere to the proteoglycan thrombomodulin in static and flow-based systems. Exp Parasitol 1997; 86: 8-18.
    • (1997) Exp Parasitol , vol.86 , pp. 8-18
    • Rogerson, S.J.1    Novakovic, S.2    Cooke, B.M.3    Brown, G.V.4
  • 53
    • 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, Horie S, Nishiki K, Kazama M. 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    Horie, S.4    Nishiki, K.5    Kazama, M.6
  • 55
    • 0036801821 scopus 로고    scopus 로고
    • Characterization of thrombomodulin gene mutations of the 5'-regulatory region
    • Nakazawa F, Koyama T, Shibamiya A, Hirosawa S. Characterization of thrombomodulin gene mutations of the 5'-regulatory region. Atherosclerosis 2002; 164: 385-7.
    • (2002) Atherosclerosis , vol.164 , pp. 385-387
    • Nakazawa, F.1    Koyama, T.2    Shibamiya, A.3    Hirosawa, S.4
  • 58
    • 0033968221 scopus 로고    scopus 로고
    • G-33A mutation in the promoter region of thrombomodulin gene and its association with coronary artery disease and plasma soluble thrombomodulin levels
    • Li YH, Chen JH,Wu HL, Shi GY, Huang HC, Chao TH, Tsai WC, Tsai LM, Guo HR, Wu WS, Chen ZC. G-33A mutation in the promoter region of thrombomodulin gene and its association with coronary artery disease and plasma soluble thrombomodulin levels. Am J Cardiol 2000; 85: 8-12.
    • (2000) Am J Cardiol , vol.85 , pp. 8-12
    • Li, Y.H.1    Chen, J.H.2    Wu, H.L.3    Shi, G.Y.4    Huang, H.C.5    Chao, T.H.6    Tsai, W.C.7    Tsai, L.M.8    Guo, H.R.9    Wu, W.S.10    Chen, Z.C.11
  • 60
    • 0036145726 scopus 로고    scopus 로고
    • Synergistic effect of thrombomodulin promoter -33G/A polymorphism and smoking on the onset of acute myocardial infarction
    • Li YH, Chen JH, Tsai WC, Chao TH, Guo HR, Tsai LM, Wu HL, Shi GY. Synergistic effect of thrombomodulin promoter -33G/A polymorphism and smoking on the onset of acute myocardial infarction. Thromb Haemost 2002; 87: 86-91.
    • (2002) Thromb Haemost , vol.87 , pp. 86-91
    • Li, Y.H.1    Chen, J.H.2    Tsai, W.C.3    Chao, T.H.4    Guo, H.R.5    Tsai, L.M.6    Wu, H.L.7    Shi, G.Y.8
  • 61
    • 0031775509 scopus 로고    scopus 로고
    • Manger Cats V, Ireland H. A mutation in the thrombomodulin gene, 127G to A coding for Ala25Thr, and the risk of myocardial infarction in men
    • Doggen CJ, Kunz G, Rosendaal FR, Lane DA, Vos HL, Stubbs PJ, Manger Cats V, Ireland H. A mutation in the thrombomodulin gene, 127G to A coding for Ala25Thr, and the risk of myocardial infarction in men. Thromb Haemost 1998; 80: 743-8.
    • (1998) Thromb Haemost , vol.80 , pp. 743-748
    • Doggen, C.J.1    Kunz, G.2    Rosendaal, F.R.3    Lane, D.A.4    Vos, H.L.5    Stubbs, P.J.6
  • 62
    • 1842413039 scopus 로고    scopus 로고
    • A novel thrombomodulin gene mutation in a patient suffering from sagittal sinus thrombosis
    • Norlund L, Zoller B, Ohlin AK. A novel thrombomodulin gene mutation in a patient suffering from sagittal sinus thrombosis. Thromb Haemost 1997; 78: 1164-6.
    • (1997) Thromb Haemost , vol.78 , pp. 1164-1166
    • Norlund, L.1    Zoller, B.2    Ohlin, A.K.3
  • 63
    • 0032589781 scopus 로고    scopus 로고
    • The Ala25-Thr mutation in the thrombomodulin gene is not frequent in Swedish patients suffering from ischemic heart disease
    • Norlund L, Holm J, Zoller B, Ohlin AK. The Ala25-Thr mutation in the thrombomodulin gene is not frequent in Swedish patients suffering from ischemic heart disease. Thromb Haemost 1999; 82: 1367-8.
    • (1999) Thromb Haemost , vol.82 , pp. 1367-1368
    • Norlund, L.1    Holm, J.2    Zoller, B.3    Ohlin, A.K.4
  • 64
    • 0037093228 scopus 로고    scopus 로고
    • Naturally occurring mutations in the thrombomodulin gene leading to impaired expression and function
    • Kunz G, Ohlin AK, Adami A, Zoller B, Svensson P, Lane DA. Naturally occurring mutations in the thrombomodulin gene leading to impaired expression and function. Blood 2002; 99: 3646-53.
    • (2002) Blood , vol.99 , pp. 3646-3653
    • Kunz, G.1    Ohlin, A.K.2    Adami, A.3    Zoller, B.4    Svensson, P.5    Lane, D.A.6
  • 65
    • 0027103736 scopus 로고
    • Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation
    • Glaser CB, Morser J, Clarke JH, Blasko E, McLean K, Kuhn I, Chang RJ, Lin JH, Vilander L, Andrews WH et al. Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation. J Clin Invest 1992; 90: 2565-73.
    • (1992) J Clin Invest , vol.90 , pp. 2565-2573
    • Glaser, C.B.1    Morser, J.2    Clarke, J.H.3    Blasko, E.4    McLean, K.5    Kuhn, I.6    Chang, R.J.7    Lin, J.H.8    Vilander, L.9    Andrews, W.H.10
  • 67
    • 0036038704 scopus 로고    scopus 로고
    • Mutations in the thrombomodulin gene are rare in patients with severe thrombophilia
    • Faioni EM, Franchi F, Castaman G, Biguzzi E, Rodeghiero F. Mutations in the thrombomodulin gene are rare in patients with severe thrombophilia. Br J Haematol 2002; 118: 595-9.
    • (2002) Br J Haematol , vol.118 , pp. 595-599
    • Faioni, E.M.1    Franchi, F.2    Castaman, G.3    Biguzzi, E.4    Rodeghiero, F.5
  • 70
    • 0031056791 scopus 로고    scopus 로고
    • A common thrombomodulin amino acid dimorphism is associated with myocardial infarction
    • Norlund L, Holm J, Zoller B, Ohlin AK. A common thrombomodulin amino acid dimorphism is associated with myocardial infarction. Thromb Haemost 1997; 77: 248-51.
    • (1997) Thromb Haemost , vol.77 , pp. 248-251
    • Norlund, L.1    Holm, J.2    Zoller, B.3    Ohlin, A.K.4
  • 71
    • 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, Sansores-Garcia L, Folsom AR, Juneja H, Chambless LE, Wu KK. 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    Sansores-Garcia, L.4    Folsom, A.R.5    Juneja, H.6    Chambless, L.E.7    Wu, K.K.8
  • 73
    • 0023924509 scopus 로고
    • A role for thrombomodulin in the pathogenesis of thrombin-induced thromboembolism in mice
    • Kumada T, Dittman WA, Majerus PW. A role for thrombomodulin in the pathogenesis of thrombin-induced thromboembolism in mice. Blood 1988; 71: 728-33.
    • (1988) Blood , vol.71 , pp. 728-733
    • Kumada, T.1    Dittman, W.A.2    Majerus, P.W.3
  • 75
    • 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, Weiler H. 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    Weiler, H.4
  • 76
    • 0035070573 scopus 로고    scopus 로고
    • Tissuerestricted 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, Wing M, Weiler H. Tissuerestricted 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    Wing, M.4    Weiler, H.5
  • 77
    • 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, Rayburn HB, Rosenberg RD. 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    Rayburn, H.B.4    Rosenberg, R.D.5
  • 78
    • 0029091542 scopus 로고
    • Reductions in tissue plasminogen activator and thrombomodulin in blood draining veins damaged by venous access devices
    • Horne MK 3rd, Merryman PK, Mayo DJ, Gralnick HR, Chang RC, Alexander HR Reductions in tissue plasminogen activator and thrombomodulin in blood draining veins damaged by venous access devices. Thromb Res 1995; 79: 369-76.
    • (1995) Thromb Res , vol.79 , pp. 369-376
    • Horne III, M.K.1    Merryman, P.K.2    Mayo, D.J.3    Gralnick, H.R.4    Chang, R.C.5    Alexander, H.R.6
  • 79
    • 0034850149 scopus 로고    scopus 로고
    • Downregulation of endothelial expression of endothelial cell protein C receptor and thrombomodulin in coronary atherosclerosis
    • Laszik ZG, Zhou XJ, Ferrell GL, Silva FG, Esmon CT. Downregulation of endothelial expression of endothelial cell protein C receptor and thrombomodulin in coronary atherosclerosis. Am J Pathol 2001; 159: 797-802.
    • (2001) Am J Pathol , vol.159 , pp. 797-802
    • Laszik, Z.G.1    Zhou, X.J.2    Ferrell, G.L.3    Silva, F.G.4    Esmon, C.T.5
  • 84
    • 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, Wing M, Cummiskey M, Kisanuki YY, Yanagisawa M, Weiler H. 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    Wing, M.4    Cummiskey, M.5    Kisanuki, Y.Y.6    Yanagisawa, M.7    Weiler, H.8
  • 87
    • 0033973089 scopus 로고    scopus 로고
    • Relationship between endothelial cell markers and arterial stenosis in peripheral and carotid artery disease
    • Blann AD, Farrell A, Picton A, McCollum CN. Relationship between endothelial cell markers and arterial stenosis in peripheral and carotid artery disease. Thromb Res 2000; 97: 209-16.
    • (2000) Thromb Res , vol.97 , pp. 209-216
    • Blann, A.D.1    Farrell, A.2    Picton, A.3    McCollum, C.N.4
  • 88
    • 16944363839 scopus 로고    scopus 로고
    • Circulating vascular cell adhesion molecule-1 correlates with the extent of human atherosclerosis in contrast to circulating intercellular adhesion molecule-1, E-selectin, Pselectin, and thrombomodulin
    • Peter K, Nawroth P, Conradt C, Nordt T, Weiss T, Boehme M, Wunsch A, Allenberg J, Kubler W, Bode C. Circulating vascular cell adhesion molecule-1 correlates with the extent of human atherosclerosis in contrast to circulating intercellular adhesion molecule-1, E-selectin, Pselectin, and thrombomodulin. Arterioscler Thromb Vasc Biol 1997; 17: 505-12.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 505-512
    • Peter, K.1    Nawroth, P.2    Conradt, C.3    Nordt, T.4    Weiss, T.5    Boehme, M.6    Wunsch, A.7    Allenberg, J.8    Kubler, W.9    Bode, C.10
  • 89
    • 0030658104 scopus 로고    scopus 로고
    • rhs-TM prevents ET-induced increase in pulmonary vascular permeability through protein C activation
    • Uchiba M, Okajima K, Murakami K, Johno M, Mohri M, Okabe H, Takatsuki K. rhs-TM prevents ET-induced increase in pulmonary vascular permeability through protein C activation. Am J Physiol 1997; 273: L889-94.
    • (1997) Am J Physiol , vol.273
    • Uchiba, M.1    Okajima, K.2    Murakami, K.3    Johno, M.4    Mohri, M.5    Okabe, H.6    Takatsuki, K.7
  • 90
    • 0031765785 scopus 로고    scopus 로고
    • Effects of recombinant human soluble thrombomodulin (rhs-TM) on clot- induced coagulation in human plasma
    • Mohri M, Suzuki M, Sugimoto E, Sata M, Yamamoto S, Maruyama I. Effects of recombinant human soluble thrombomodulin (rhs-TM) on clot- induced coagulation in human plasma. Thromb Haemost 1998; 80: 925-9.
    • (1998) Thromb Haemost , vol.80 , pp. 925-929
    • Mohri, M.1    Suzuki, M.2    Sugimoto, E.3    Sata, M.4    Yamamoto, S.5    Maruyama, I.6
  • 91
    • 0028199745 scopus 로고
    • Effects of recombinant human soluble thrombomodulin (rhs-TM) on a rat model of disseminated intravascular coagulation with decreased levels of plasma antithrombin III
    • Aoki Y, Ohishi R, Takei R, Matsuzaki O, Mohri M, Saitoh K, Gomi K, Sugihara T, Kiyota T, Yamamoto S et al. Effects of recombinant human soluble thrombomodulin (rhs-TM) on a rat model of disseminated intravascular coagulation with decreased levels of plasma antithrombin III. Thromb Haemost 1994; 71: 452-5.
    • (1994) Thromb Haemost , vol.71 , pp. 452-455
    • Aoki, Y.1    Ohishi, R.2    Takei, R.3    Matsuzaki, O.4    Mohri, M.5    Saitoh, K.6    Gomi, K.7    Sugihara, T.8    Kiyota, T.9    Yamamoto, S.10
  • 94
    • 0031674015 scopus 로고    scopus 로고
    • Expression of thrombomodulin in atherosclerotic lesions and mitogenic activity of recombinant thrombomodulin in vascular smooth muscle cells
    • Tohda G, Oida K, Okada Y, Kosaka S, Okada E, Takahashi S, Ishii H, Miyamori I. Expression of thrombomodulin in atherosclerotic lesions and mitogenic activity of recombinant thrombomodulin in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 1998; 18: 1861-9.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1861-1869
    • Tohda, G.1    Oida, K.2    Okada, Y.3    Kosaka, S.4    Okada, E.5    Takahashi, S.6    Ishii, H.7    Miyamori, I.8
  • 95
    • 0029939761 scopus 로고    scopus 로고
    • Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells
    • Grinnell BW, Berg DT. Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells. Am J Physiol 1996; 270: H603-9.
    • (1996) Am J Physiol , vol.270
    • Grinnell, B.W.1    Berg, D.T.2
  • 97
    • 0035853404 scopus 로고    scopus 로고
    • Thrombomodulin prolongs thrombin-induced extracellular signalregulated kinase phosphorylation and nuclear retention in endothelial cells
    • Olivot JM, Estebanell E, Lafay M, Brohard B, Aiach M, Rendu F. Thrombomodulin prolongs thrombin-induced extracellular signalregulated kinase phosphorylation and nuclear retention in endothelial cells. Circ Res 2001; 88: 681-7.
    • (2001) Circ Res , vol.88 , pp. 681-687
    • Olivot, J.M.1    Estebanell, E.2    Lafay, M.3    Brohard, B.4    Aiach, M.5    Rendu, F.6
  • 98
    • 0036170060 scopus 로고    scopus 로고
    • Prospective study on soluble thrombomodulin and von Willebrand factor and the risk of ischemic and hemorrhagic stroke
    • Johansson L, Jansson JH, Boman K, Nilsson TK, Stegmayr B, Hallmans G. Prospective study on soluble thrombomodulin and von Willebrand factor and the risk of ischemic and hemorrhagic stroke. Thromb Haemost 2002; 87: 211-7.
    • (2002) Thromb Haemost , vol.87 , pp. 211-217
    • Johansson, L.1    Jansson, J.H.2    Boman, K.3    Nilsson, T.K.4    Stegmayr, B.5    Hallmans, G.6
  • 99
    • 0025836103 scopus 로고
    • Regional distribution of thrombomodulin in human brain
    • Wong VL, Hofman FM, Ishii H, Fisher M. Regional distribution of thrombomodulin in human brain. Brain Res 1991; 556: 1-5.
    • (1991) Brain Res , vol.556 , pp. 1-5
    • Wong, V.L.1    Hofman, F.M.2    Ishii, H.3    Fisher, M.4
  • 100
    • 0031456833 scopus 로고    scopus 로고
    • Thrombomodulin expression in bovine brain capillaries. Anticoagulant function of the blood-brain barrier, regional differences, and regulatory mechanisms
    • Wang L, Tran ND, Kittaka M, Fisher MJ, Schreiber SS, Zlokovic BV. Thrombomodulin expression in bovine brain capillaries. Anticoagulant function of the blood-brain barrier, regional differences, and regulatory mechanisms. Arterioscler Thromb Vasc Biol 1997; 17: 3139-46.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 3139-3146
    • Wang, L.1    Tran, N.D.2    Kittaka, M.3    Fisher, M.J.4    Schreiber, S.S.5    Zlokovic, B.V.6
  • 101
    • 0021929962 scopus 로고
    • Thrombomodulin is found on endothelium of arteries, veins, capillaries, and lymphatics, and on syncytiotrophoblast of human placenta
    • Maruyama I, Bell CE, Majerus PW. Thrombomodulin is found on endothelium of arteries, veins, capillaries, and lymphatics, and on syncytiotrophoblast of human placenta. J Cell Biol 1985; 101: 363-71.
    • (1985) J Cell Biol , vol.101 , pp. 363-371
    • Maruyama, I.1    Bell, C.E.2    Majerus, P.W.3
  • 102
    • 0022636799 scopus 로고
    • Thrombomodulin, an endothelial anticoagulant protein, is absent from the human brain
    • Ishii H, Salem HH, Bell CE, Laposata EA, Majerus PW. Thrombomodulin, an endothelial anticoagulant protein, is absent from the human brain. Blood 1986; 67: 362-5.
    • (1986) Blood , vol.67 , pp. 362-365
    • Ishii, H.1    Salem, H.H.2    Bell, C.E.3    Laposata, E.A.4    Majerus, P.W.5
  • 104
    • 0032800292 scopus 로고    scopus 로고
    • Transforming growth factor-beta mediates astrocyte-specific regulation of brain endothelial anticoagulant factors
    • Tran ND, Correale J, Schreiber SS, Fisher M. Transforming growth factor-beta mediates astrocyte-specific regulation of brain endothelial anticoagulant factors. Stroke 1999; 30: 1671-8.
    • (1999) Stroke , vol.30 , pp. 1671-1678
    • Tran, N.D.1    Correale, J.2    Schreiber, S.S.3    Fisher, M.4
  • 105
    • 0030468826 scopus 로고    scopus 로고
    • Regulation of brain capillary endothelial thrombomodulin mRNA expression
    • [Discussion 2310-1]
    • Tran ND,Wong VL, Schreiber SS, Bready JV, Fisher M. Regulation of brain capillary endothelial thrombomodulin mRNA expression. Stroke 1996; 27: 2304-10 [Discussion 2310-1].
    • (1996) Stroke , vol.27 , pp. 2304-2310
    • Tran, N.D.1    Wong, V.L.2    Schreiber, S.S.3    Bready, J.V.4    Fisher, M.5
  • 106
    • 0031106293 scopus 로고    scopus 로고
    • Novel expression and localization of active thrombomodulin on the surface of mouse brain astrocytes
    • Pindon A, Hantai D, Jandrot-Perrus M, Festoff BW. Novel expression and localization of active thrombomodulin on the surface of mouse brain astrocytes. Glia 1997; 19: 259-68.
    • (1997) Glia , vol.19 , pp. 259-268
    • Pindon, A.1    Hantai, D.2    Jandrot-Perrus, M.3    Festoff, B.W.4
  • 107
    • 0034175489 scopus 로고    scopus 로고
    • Thrombomodulin as a new marker of lesion-induced astrogliosis: involvement of thrombin through the Gprotein-coupled protease- activated receptor-1
    • Pindon A, Berry M, Hantai D. Thrombomodulin as a new marker of lesion-induced astrogliosis: involvement of thrombin through the Gprotein-coupled protease- activated receptor-1. J Neurosci 2000; 20: 2543-50.
    • (2000) J Neurosci , vol.20 , pp. 2543-2550
    • Pindon, A.1    Berry, M.2    Hantai, D.3
  • 108
    • 0035799374 scopus 로고    scopus 로고
    • Anti-inflammatory, antithrombotic, and neuroprotective effects of activated protein C in a murine model of focal ischemic stroke
    • Shibata M, Kumar SR, Amar A, Fernandez JA, Hofman F, Griffin JH, Zlokovic BV. Anti-inflammatory, antithrombotic, and neuroprotective effects of activated protein C in a murine model of focal ischemic stroke. Circulation 2001; 103: 1799-805.
    • (2001) Circulation , vol.103 , pp. 1799-1805
    • Shibata, M.1    Kumar, S.R.2    Amar, A.3    Fernandez, J.A.4    Hofman, F.5    Griffin, J.H.6    Zlokovic, B.V.7
  • 111
    • 0027434627 scopus 로고
    • Detection of thrombomodulin in human lung cancer cells
    • Tamura A, Matsubara O, Hirokawa K, Aoki N. Detection of thrombomodulin in human lung cancer cells. Am J Pathol 1993; 142: 79-85.
    • (1993) Am J Pathol , vol.142 , pp. 79-85
    • Tamura, A.1    Matsubara, O.2    Hirokawa, K.3    Aoki, N.4
  • 114
    • 0031712963 scopus 로고    scopus 로고
    • Thrombomodulin, a receptor for the serine protease thrombin, is decreased in primary tumors and metastases but increased in ascitic fluids of patients with advanced ovarian cancer FIGO IIIc
    • Wilhelm S, Schmitt M, Parkinson J, Kuhn W, Graeff H, Wilhelm OG. Thrombomodulin, a receptor for the serine protease thrombin, is decreased in primary tumors and metastases but increased in ascitic fluids of patients with advanced ovarian cancer FIGO IIIc. Int J Oncol 1998; 13: 645-51.
    • (1998) Int J Oncol , vol.13 , pp. 645-651
    • Wilhelm, S.1    Schmitt, M.2    Parkinson, J.3    Kuhn, W.4    Graeff, H.5    Wilhelm, O.G.6
  • 116
    • 0029947498 scopus 로고    scopus 로고
    • Prognostic value and clinicopathological correlation of thrombomodulin in squamous cell carcinoma of the human lung
    • Hamatake M, Ishida T, Mitsudomi T, Akazawa K, Sugimachi K. Prognostic value and clinicopathological correlation of thrombomodulin in squamous cell carcinoma of the human lung. Clin Cancer Res 1996; 2: 763-6.
    • (1996) Clin Cancer Res , vol.2 , pp. 763-766
    • Hamatake, M.1    Ishida, T.2    Mitsudomi, T.3    Akazawa, K.4    Sugimachi, K.5
  • 118
    • 0031193375 scopus 로고    scopus 로고
    • An immunohistochemical study of thrombomodulin in oral squamous cell carcinoma and its association with invasive and metastatic potential
    • Tabata M, Sugihara K, Yonezawa S, Yamashita S, Maruyama I. An immunohistochemical study of thrombomodulin in oral squamous cell carcinoma and its association with invasive and metastatic potential. J Oral Pathol Med 1997; 26: 258-64.
    • (1997) J Oral Pathol Med , vol.26 , pp. 258-264
    • Tabata, M.1    Sugihara, K.2    Yonezawa, S.3    Yamashita, S.4    Maruyama, I.5
  • 120
    • 0032523739 scopus 로고    scopus 로고
    • A subcloned human esophageal squamous cell carcinoma cell line with low thrombomodulin expression showed increased invasiveness compared with a high thrombomodulin-expressing clone - thrombomodulin as a possible candidate for an adhesion molecule of squamous cell carcinoma
    • Matsushita Y, Yoshiie K, Imamura Y, Ogawa H, Imamura H, Takao S, Yonezawa S, Aikou T, Maruyama I, Sato E. A subcloned human esophageal squamous cell carcinoma cell line with low thrombomodulin expression showed increased invasiveness compared with a high thrombomodulin-expressing clone - thrombomodulin as a possible candidate for an adhesion molecule of squamous cell carcinoma. Cancer Lett 1998; 127: 195-201.
    • (1998) Cancer Lett , vol.127 , pp. 195-201
    • Matsushita, Y.1    Yoshiie, K.2    Imamura, Y.3    Ogawa, H.4    Imamura, H.5    Takao, S.6    Yonezawa, S.7    Aikou, T.8    Maruyama, I.9    Sato, E.10
  • 121
    • 0034695191 scopus 로고    scopus 로고
    • Inhibition of invasion and experimental metastasis of murine melanoma cells by human soluble thrombomodulin
    • Hosaka Y, Higuchi T, Tsumagari M, Ishii H. Inhibition of invasion and experimental metastasis of murine melanoma cells by human soluble thrombomodulin. Cancer Lett 2000; 161: 231-40.
    • (2000) Cancer Lett , vol.161 , pp. 231-240
    • Hosaka, Y.1    Higuchi, T.2    Tsumagari, M.3    Ishii, H.4
  • 122
    • 0034651718 scopus 로고    scopus 로고
    • Introduction: are natural anticoagulant candidates for modulating the inflammatory response to endotoxin?
    • Esmon CT. Introduction: are natural anticoagulant candidates for modulating the inflammatory response to endotoxin? Blood 2000; 95: 1113-6.
    • (2000) Blood , vol.95 , pp. 1113-1116
    • Esmon, C.T.1
  • 123
    • 0036719236 scopus 로고    scopus 로고
    • New mechanisms for vascular control of inflammation mediated by natural anticoagulant proteins
    • Esmon CT. New mechanisms for vascular control of inflammation mediated by natural anticoagulant proteins. J Exp Med 2002; 196: 561-4.
    • (2002) J Exp Med , vol.196 , pp. 561-564
    • Esmon, C.T.1
  • 124
    • 0027998013 scopus 로고
    • Selective inhibitory effects of the anticoagulant activated protein C on the responses of human mononuclear phagocytes to LPS, IFN-gamma, or phorbol ester
    • Grey ST, Tsuchida A, Hau H, Orthner CL, Salem HH, Hancock WW. Selective inhibitory effects of the anticoagulant activated protein C on the responses of human mononuclear phagocytes to LPS, IFN-gamma, or phorbol ester. J Immunol 1994; 153: 3664-72.
    • (1994) J Immunol , vol.153 , pp. 3664-3672
    • Grey, S.T.1    Tsuchida, A.2    Hau, H.3    Orthner, C.L.4    Salem, H.H.5    Hancock, W.W.6
  • 125
    • 0029873131 scopus 로고    scopus 로고
    • A physiologic anti-inflammatory pathway based on thrombomodulin expression and generation of activated protein C by human mononuclear phagocytes
    • Grey ST, Hancock WW. A physiologic anti-inflammatory pathway based on thrombomodulin expression and generation of activated protein C by human mononuclear phagocytes. J Immunol 1996; 156: 2256-63.
    • (1996) J Immunol , vol.156 , pp. 2256-2263
    • Grey, S.T.1    Hancock, W.W.2
  • 126
    • 0035815747 scopus 로고    scopus 로고
    • Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis
    • Joyce DE, Gelbert L, Ciaccia A, DeHoff B, Grinnell BW. Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis. J Biol Chem 2001; 276: 11199-203.
    • (2001) J Biol Chem , vol.276 , pp. 11199-11203
    • Joyce, D.E.1    Gelbert, L.2    Ciaccia, A.3    DeHoff, B.4    Grinnell, B.W.5
  • 127
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • Riewald M, Petrovan RJ, Donner A, Mueller BM, Ruf W. 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    Mueller, B.M.4    Ruf, W.5
  • 128
    • 0000952010 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor (EPCR) constitutively translocates into the nucleus and also mediates activated protein C, but not protein C, nuclear translocation
    • Xu JEC. Endothelial cell protein C receptor (EPCR) constitutively translocates into the nucleus and also mediates activated protein C, but not protein C, nuclear translocation. Thromb Haemost 1999; 82 (Suppl.): 206.
    • (1999) Thromb Haemost , vol.82 , Issue.SUPPL. , pp. 206
    • Xu, J.E.C.1
  • 131
    • 0023755932 scopus 로고
    • Tumor necrosis factor suppresses transcription of the thrombomodulin gene in endothelial cells
    • Conway EM, Rosenberg RD. Tumor necrosis factor suppresses transcription of the thrombomodulin gene in endothelial cells. Mol Cell Biol 1988; 8: 5588-92.
    • (1988) Mol Cell Biol , vol.8 , pp. 5588-5592
    • Conway, E.M.1    Rosenberg, R.D.2
  • 132
    • 0025963529 scopus 로고
    • Regulation of thrombomodulin by tumor necrosis factor-alpha: comparison of transcriptional and posttranscriptional mechanisms
    • Lentz SR, Tsiang M, Sadler JE. Regulation of thrombomodulin by tumor necrosis factor-alpha: comparison of transcriptional and posttranscriptional mechanisms. Blood 1991; 77: 542-50.
    • (1991) Blood , vol.77 , pp. 542-550
    • Lentz, S.R.1    Tsiang, M.2    Sadler, J.E.3
  • 133
    • 0027724580 scopus 로고
    • Ets transcription factor binding site is required for positive and TNF alpha-induced negative promoter regulation
    • von der Ahe D, Nischan C, Kunz C, Otte J, Knies U, Oderwald H, Wasylyk B. Ets transcription factor binding site is required for positive and TNF alpha-induced negative promoter regulation. Nucl Acids Res 1993; 21: 5636-43.
    • (1993) Nucl Acids Res , vol.21 , pp. 5636-5643
    • von der Ahe, D.1    Nischan, C.2    Kunz, C.3    Otte, J.4    Knies, U.5    Oderwald, H.6    Wasylyk, B.7
  • 134
    • 0030066667 scopus 로고    scopus 로고
    • Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils: in vivo and in vitro studies
    • Boehme MW, Deng Y, Raeth U, Bierhaus A, Ziegler R, Stremmel W, Nawroth PP. Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils: in vivo and in vitro studies. Immunology 1996; 87: 134-40.
    • (1996) Immunology , vol.87 , pp. 134-140
    • Boehme, M.W.1    Deng, Y.2    Raeth, U.3    Bierhaus, A.4    Ziegler, R.5    Stremmel, W.6    Nawroth, P.P.7
  • 135
    • 84858769443 scopus 로고    scopus 로고
    • Modulation of thrombomodulin-dependent activation of human protein C through differential expression of endothelial Smads
    • Sandusky G, Berg DT, Richardson MA, Myers L, Grinnell BW. Modulation of thrombomodulin-dependent activation of human protein C through differential expression of endothelial Smads. J Biol Chem 2002; 28: 28.
    • (2002) J Biol Chem , vol.28 , pp. 28
    • Sandusky, G.1    Berg, D.T.2    Richardson, M.A.3    Myers, L.4    Grinnell, B.W.5
  • 136
    • 0030040061 scopus 로고    scopus 로고
    • Developmentally regulated gene expression of thrombomodulin in postimplantation mouse embryos
    • Weiler-Guettler H, Aird WC, Rayburn H, Husain M, Rosenberg RD. 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    Husain, M.4    Rosenberg, R.D.5
  • 140
    • 0032006548 scopus 로고    scopus 로고
    • Low levels of tissue factor are compatible with development and hemostasis in mice
    • Parry GC, Erlich JH, Carmeliet P, Luther T, Mackman N. Low levels of tissue factor are compatible with development and hemostasis in mice. J Clin Invest 1998; 101: 560-9.
    • (1998) J Clin Invest , vol.101 , pp. 560-569
    • Parry, G.C.1    Erlich, J.H.2    Carmeliet, P.3    Luther, T.4    Mackman, N.5
  • 141
    • 0030008312 scopus 로고    scopus 로고
    • Role of the thrombin receptor in development and evidence for a second receptor
    • Connolly AJ, Ishihara H, Kahn ML, Farese RV Jr, Coughlin SR. Role of the thrombin receptor in development and evidence for a second receptor. Nature 1996; 381: 516-9.
    • (1996) Nature , vol.381 , pp. 516-519
    • Connolly, A.J.1    Ishihara, H.2    Kahn, M.L.3    Farese Jr., R.V.4    Coughlin, S.R.5
  • 143
    • 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, Esmon CT. 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    Esmon, C.T.4
  • 144
    • 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, Zhang F, Li W, Esmon NL, Esmon CT. 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    Zhang, F.4    Li, W.5    Esmon, N.L.6    Esmon, C.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.