메뉴 건너뛰기




Volumn 89, Issue 2, 1997, Pages 652-661

The amino terminal lectin-like domain of thrombomodulin is required for constitutive endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; LECTIN; MUTANT PROTEIN; PROTEIN C; SIGNAL PEPTIDE; THROMBIN; THROMBOMODULIN;

EID: 0031023957     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v89.2.652     Document Type: Article
Times cited : (44)

References (63)
  • 1
    • 0023096623 scopus 로고
    • The regulation of natural anticoagulant pathways
    • Esmon CT: The regulation of natural anticoagulant pathways. Science 235:1348, 1987
    • (1987) Science , vol.235 , pp. 1348
    • Esmon, C.T.1
  • 2
    • 0029112841 scopus 로고
    • Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface
    • Esmon C: Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J 9:946, 1995
    • (1995) FASEB J , vol.9 , pp. 946
    • Esmon, C.1
  • 3
    • 0024507770 scopus 로고
    • The clinical spectrum of heterozygous protein C deficiency in a large New England kindred
    • Bovill EG, Bauer KA, Dickerman JD, Callas P, West B: The clinical spectrum of heterozygous protein C deficiency in a large New England kindred. Blood 73:712, 1989
    • (1989) Blood , vol.73 , pp. 712
    • Bovill, E.G.1    Bauer, K.A.2    Dickerman, J.D.3    Callas, P.4    West, B.5
  • 5
    • 0028954459 scopus 로고
    • The first mutation identified in the thrombomodulin gene in a 45 year old man presenting with thromboembolic disease
    • Ohlin A-K, Marlar R: The first mutation identified in the thrombomodulin gene in a 45 year old man presenting with thromboembolic disease. Blood 85:330, 1995
    • (1995) Blood , vol.85 , pp. 330
    • Ohlin, A.-K.1    Marlar, R.2
  • 6
    • 0345173854 scopus 로고
    • Human thrombomodulin gene is intron depleted: Nucleic acid sequences of the cDNA and gene predict protein structure and suggest sites of regulatory control
    • Jackman RW, Beeler DL, Fritze L, Soff G, Rosenberg RD: Human thrombomodulin gene is intron depleted: Nucleic acid sequences of the cDNA and gene predict protein structure and suggest sites of regulatory control. Proc Natl Acad Sci USA 84:6425, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6425
    • Jackman, R.W.1    Beeler, D.L.2    Fritze, L.3    Soff, G.4    Rosenberg, R.D.5
  • 7
    • 0023943394 scopus 로고
    • A 10-kDa cyanogen bromide fragment from the epidermal growth factor homology domain of rabbit thrombomodulin contains the primary thrombin binding site
    • Kurosawa S, Stearns DJ, Jackson KW, Esmon CT: A 10-kDa cyanogen bromide fragment from the epidermal growth factor homology domain of rabbit thrombomodulin contains the primary thrombin binding site. J Biol Chem 263:5993, 1988
    • (1988) J Biol Chem , vol.263 , pp. 5993
    • Kurosawa, S.1    Stearns, D.J.2    Jackson, K.W.3    Esmon, C.T.4
  • 8
    • 0024559613 scopus 로고
    • A domain composed of epidermal growth factor-like structures of human thrombomodulin is essential for thrombin binding and for protein C activation
    • Suzuki K, Hayashi T, Nishioka J, Kosaka Y, Zushi M, Honda G, Yamamoto S: A domain composed of epidermal growth factor-like structures of human thrombomodulin is essential for thrombin binding and for protein C activation. J Biol Chem 264:4872, 1989
    • (1989) J Biol Chem , vol.264 , pp. 4872
    • Suzuki, K.1    Hayashi, T.2    Nishioka, J.3    Kosaka, Y.4    Zushi, M.5    Honda, G.6    Yamamoto, S.7
  • 9
    • 0024396997 scopus 로고
    • The last three consecutive epidermal growth factor-like structures of human thrombomodulin comprise the minimum functional domain for protein C-activating cofactor activity and anticoagulant activity
    • Zushi M, Gomi K, Yamamoto S, Maruyama I, Hayashi T, Suzuki K: The last three consecutive epidermal growth factor-like structures of human thrombomodulin comprise the minimum functional domain for protein C-activating cofactor activity and anticoagulant activity. J Biol Chem 264:10351, 1989
    • (1989) J Biol Chem , vol.264 , pp. 10351
    • Zushi, M.1    Gomi, K.2    Yamamoto, S.3    Maruyama, I.4    Hayashi, T.5    Suzuki, K.6
  • 12
    • 0024284252 scopus 로고
    • The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins
    • Petersen T: The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins. FEBS Lett 231:51, 1988
    • (1988) FEBS Lett , vol.231 , pp. 51
    • Petersen, T.1
  • 13
    • 0023774665 scopus 로고
    • Detecting distant homologies of mosaic proteins. Analysis of the sequences of thrombomodulin, thrombospondin, complement components C9, C8 alpha and C8 beta, vitronectin and plasma cell membrane glycoprotein PC-1
    • Patthy L: Detecting distant homologies of mosaic proteins. Analysis of the sequences of thrombomodulin, thrombospondin, complement components C9, C8 alpha and C8 beta, vitronectin and plasma cell membrane glycoprotein PC-1. J Mol Biol 202:689, 1988
    • (1988) J Mol Biol , vol.202 , pp. 689
    • Patthy, L.1
  • 14
    • 0025878945 scopus 로고
    • Leukocyte interactions mediated by selectins
    • McEver R: Leukocyte interactions mediated by selectins. Thromb Haemost 66:80, 1991
    • (1991) Thromb Haemost , vol.66 , pp. 80
    • McEver, R.1
  • 15
    • 0024320616 scopus 로고
    • The active site of the thrombin-thrombomodulin complex
    • Lu R, Esmon NL, Esmon CT, Johnson AE: The active site of the thrombin-thrombomodulin complex. J Biol Chem 264:12956, 1989
    • (1989) J Biol Chem , vol.264 , pp. 12956
    • Lu, R.1    Esmon, N.L.2    Esmon, C.T.3    Johnson, A.E.4
  • 16
    • 0028039927 scopus 로고
    • Thrombomodulin lacking the cytoplasmic domain efficiently internalizes thrombin via nonclathrin-coated, pit-mediated endocytosis
    • Conway E, Nowakowski B, Steiner-Mosonyi M: Thrombomodulin lacking the cytoplasmic domain efficiently internalizes thrombin via nonclathrin-coated, pit-mediated endocytosis. J Cell Physiol 158:285, 1994
    • (1994) J Cell Physiol , vol.158 , pp. 285
    • Conway, E.1    Nowakowski, B.2    Steiner-Mosonyi, M.3
  • 17
    • 0026647573 scopus 로고
    • An ultrastructural study of thrombomodulin endocytosis: Internalization occurs via clathrin-coated and non-coated pits
    • Conway E, Boffa M, Nowakowski B, Steiner-Mosonyi M: An ultrastructural study of thrombomodulin endocytosis: Internalization occurs via clathrin-coated and non-coated pits. J Cell Physiol 151:604, 1992
    • (1992) J Cell Physiol , vol.151 , pp. 604
    • Conway, E.1    Boffa, M.2    Nowakowski, B.3    Steiner-Mosonyi, M.4
  • 18
    • 0023553120 scopus 로고
    • Development of a radioimmunoassay for quantitating prethrombin 2 in human plasma
    • Conway EM, Lau HK, Bauer KA, Rosenberg RD: Development of a radioimmunoassay for quantitating prethrombin 2 in human plasma. J Lab Clin Med 110:567, 1987
    • (1987) J Lab Clin Med , vol.110 , pp. 567
    • Conway, E.M.1    Lau, H.K.2    Bauer, K.A.3    Rosenberg, R.D.4
  • 20
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-pheno-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-pheno-chloroform extraction. Anal Biochem 162:156, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 21
    • 0027402654 scopus 로고
    • Biologically active thrombomodulin is synthesized by adherent synovial fluid cells and is elevated in synovial fluid of patients with rheumatoid arthritis
    • Conway E, Nowakowski B: Biologically active thrombomodulin is synthesized by adherent synovial fluid cells and is elevated in synovial fluid of patients with rheumatoid arthritis. Blood 81:726, 1993
    • (1993) Blood , vol.81 , pp. 726
    • Conway, E.1    Nowakowski, B.2
  • 22
    • 0020793569 scopus 로고
    • A technique for radiolabelling DNA restriction endouclease fragments to high specific activity
    • Feinberg AP, Vogelstein B: A technique for radiolabelling DNA restriction endouclease fragments to high specific activity. Anal Biochem 132:6, 1983
    • (1983) Anal Biochem , vol.132 , pp. 6
    • Feinberg, A.P.1    Vogelstein, B.2
  • 23
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions
    • Frens G: Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nat Phys Sci 241:20, 1973
    • (1973) Nat Phys Sci , vol.241 , pp. 20
    • Frens, G.1
  • 24
    • 0021840759 scopus 로고
    • Gold labeling of thrombin and ultrastructural studies of thrombin-gold conjugate binding by fibrin
    • Liu CY, Handley DA, Chien S: Gold labeling of thrombin and ultrastructural studies of thrombin-gold conjugate binding by fibrin. Anal Biochem 147:49, 1985
    • (1985) Anal Biochem , vol.147 , pp. 49
    • Liu, C.Y.1    Handley, D.A.2    Chien, S.3
  • 25
    • 0018631928 scopus 로고
    • Evaluation of colloidal gold as a cytochemical marker for transmission and scanning electron microscopy
    • Horisberger M: Evaluation of colloidal gold as a cytochemical marker for transmission and scanning electron microscopy. Biol Cell 36:253, 1979
    • (1979) Biol Cell , vol.36 , pp. 253
    • Horisberger, M.1
  • 26
    • 0004252445 scopus 로고
    • Englewood Cliffs, NJ, Prentice Hall
    • Zar J: Biostatistical Analysis. Englewood Cliffs, NJ, Prentice Hall, 1974
    • (1974) Biostatistical Analysis
    • Zar, J.1
  • 27
    • 0023802461 scopus 로고
    • Asialoglycoprotein receptor phosphorylation and receptor-mediated endocytosis in hepatoma cells
    • Fallon RJ, Schwartz AL: Asialoglycoprotein receptor phosphorylation and receptor-mediated endocytosis in hepatoma cells. J Biol Chem 263:13159, 1988
    • (1988) J Biol Chem , vol.263 , pp. 13159
    • Fallon, R.J.1    Schwartz, A.L.2
  • 28
    • 0021130929 scopus 로고
    • Primary structure of human transferrin receptor deduced from the mRNA sequence
    • Schneider C, Owen M, Banville D, Williams J: Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature 311:675, 1984
    • (1984) Nature , vol.311 , pp. 675
    • Schneider, C.1    Owen, M.2    Banville, D.3    Williams, J.4
  • 29
    • 0023850048 scopus 로고
    • A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells
    • Leytus S, Loegb K, Hagen F, Kurachi K, Davie E: A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells. Biochemistry 27:1067, 1988
    • (1988) Biochemistry , vol.27 , pp. 1067
    • Leytus, S.1    Loegb, K.2    Hagen, F.3    Kurachi, K.4    Davie, E.5
  • 30
    • 0028101918 scopus 로고
    • Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa
    • Altieri D: Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa. J Biol Chem 269:3139, 1994
    • (1994) J Biol Chem , vol.269 , pp. 3139
    • Altieri, D.1
  • 31
    • 0025755359 scopus 로고
    • Regulatory mechanisms for thrombomodulin expression in human umbilical vein endothelial cells in vitro
    • Hirokawa K, Aoki N: Regulatory mechanisms for thrombomodulin expression in human umbilical vein endothelial cells in vitro. J Cell Physiol 147:157, 1991
    • (1991) J Cell Physiol , vol.147 , pp. 157
    • Hirokawa, K.1    Aoki, N.2
  • 32
    • 0024591263 scopus 로고
    • Stability of the thrombin-thrombomodulin complex on the surface of endothelial cells from human saphenous vein or from the cell line EA.hy 926
    • Beretz A, Freysinnet J-M, Gauchy J, Schmitt DA, Klein-Soyer C, Edgell C-JS, Cazenave J-P: Stability of the thrombin-thrombomodulin complex on the surface of endothelial cells from human saphenous vein or from the cell line EA.hy 926. Biochem J 259:35, 1989
    • (1989) Biochem J , vol.259 , pp. 35
    • Beretz, A.1    Freysinnet, J.-M.2    Gauchy, J.3    Schmitt, D.A.4    Klein-Soyer, C.5    Edgell, C.-J.S.6    Cazenave, J.-P.7
  • 34
    • 0021929962 scopus 로고
    • Thrombomodulin is found on endothelium of arteries, capilalaries, and lymphatics, and on syncytiotrophoblast of human placenta
    • Maruyama I, Bell C, Majerus P: Thrombomodulin is found on endothelium of arteries, capilalaries, and lymphatics, and on syncytiotrophoblast of human placenta. J Cell Biol 101:363, 1985
    • (1985) J Cell Biol , vol.101 , pp. 363
    • Maruyama, I.1    Bell, C.2    Majerus, P.3
  • 35
    • 0023274160 scopus 로고
    • Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells
    • Maruyama I, Majerus P: Protein C inhibits endocytosis of thrombin-thrombomodulin complexes in A549 lung cancer cells and human umbilical vein endothelial cells. Blood 69:1481, 1987
    • (1987) Blood , vol.69 , pp. 1481
    • Maruyama, I.1    Majerus, P.2
  • 36
    • 0024589205 scopus 로고
    • Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelial cells in culture
    • Moore KL, Esmon CT, Esmon NL: Tumor necrosis factor leads to the internalization and degradation of thrombomodulin from the surface of bovine aortic endothelial cells in culture. Blood 73:159, 1989
    • (1989) Blood , vol.73 , pp. 159
    • Moore, K.L.1    Esmon, C.T.2    Esmon, N.L.3
  • 37
    • 0026334536 scopus 로고
    • Plasma thrombomodulin as a marker of endothelium damage
    • Boffa M, Karochkine M, Berard M: Plasma thrombomodulin as a marker of endothelium damage. Nouv Rev Fr Hematol 33:529, 1991
    • (1991) Nouv Rev Fr Hematol , vol.33 , pp. 529
    • Boffa, M.1    Karochkine, M.2    Berard, M.3
  • 38
    • 0028064867 scopus 로고
    • Heat shock of vascular endothelial cells induces an upregulatory transcriptional response of the thrombomodulin gene that is delayed in onset and does not attenuate
    • Conway E, Liu L, Nowakowski B, Steiner-Mosonyi M, Jackman R: Heat shock of vascular endothelial cells induces an upregulatory transcriptional response of the thrombomodulin gene that is delayed in onset and does not attenuate. J Biol Chem 269:22804, 1994
    • (1994) J Biol Chem , vol.269 , pp. 22804
    • Conway, E.1    Liu, L.2    Nowakowski, B.3    Steiner-Mosonyi, M.4    Jackman, R.5
  • 39
    • 0028243040 scopus 로고
    • Dual function of macrophage galactose/N-acetylgalactosamine-specific lectins: Glycoprotein uptake and tumoricidal cellular recognition
    • Kawakami K, Yamamoto K, Toyoshima S, Osawa T, Irimura T: Dual function of macrophage galactose/N-acetylgalactosamine-specific lectins: Glycoprotein uptake and tumoricidal cellular recognition. Jpn J Cancer Res 85:744, 1994
    • (1994) Jpn J Cancer Res , vol.85 , pp. 744
    • Kawakami, K.1    Yamamoto, K.2    Toyoshima, S.3    Osawa, T.4    Irimura, T.5
  • 40
    • 0028491927 scopus 로고
    • Plasma kallikrein clearance by the liver: A review
    • Borges D, Kouyoumdjian M: Plasma kallikrein clearance by the liver: A review. Braz J Med Biol Res 27:2033, 1994
    • (1994) Braz J Med Biol Res , vol.27 , pp. 2033
    • Borges, D.1    Kouyoumdjian, M.2
  • 41
    • 0027953730 scopus 로고
    • Reconstitution of antibody-dependent phagocytosis in fibroblasts expressing Fcγ and the complement receptor type 3
    • Krauss J, Poo H, Xue W, Mayo-Bond L, Todd R III, Petty H: Reconstitution of antibody-dependent phagocytosis in fibroblasts expressing Fcγ and the complement receptor type 3. J Immunol 153:1769, 1994
    • (1994) J Immunol , vol.153 , pp. 1769
    • Krauss, J.1    Poo, H.2    Xue, W.3    Mayo-Bond, L.4    Todd III, R.5    Petty, H.6
  • 42
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer R, Ferrige A, Moncada S: Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327:524, 1987
    • (1987) Nature , vol.327 , pp. 524
    • Palmer, R.1    Ferrige, A.2    Moncada, S.3
  • 43
    • 0000797922 scopus 로고
    • Human endothelial cells in culture produce platelet-activating factor (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) when stimulated with thrombin
    • Prescott S, Zimmerman G, McIntyre T: Human endothelial cells in culture produce platelet-activating factor (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) when stimulated with thrombin. Proc Natl Acad Sci USA 81:3534, 1984
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3534
    • Prescott, S.1    Zimmerman, G.2    McIntyre, T.3
  • 44
    • 0026705069 scopus 로고
    • Vascular effects of thrombin
    • Glusa E: Vascular effects of thrombin. Semin Thromb Hemost 18:296, 1992
    • (1992) Semin Thromb Hemost , vol.18 , pp. 296
    • Glusa, E.1
  • 46
    • 0026713946 scopus 로고
    • Regulation of the urokinase-type plasminogen activator receptor on vascular smooth muscle cells is under the control of thrombin and other mitogens
    • Reuning U, Bang N: Regulation of the urokinase-type plasminogen activator receptor on vascular smooth muscle cells is under the control of thrombin and other mitogens. Arteroscler Thromb 12:1161, 1992
    • (1992) Arteroscler Thromb , vol.12 , pp. 1161
    • Reuning, U.1    Bang, N.2
  • 47
    • 0017152878 scopus 로고
    • Mitogenicity of thrombin and surface alterations on mouse splenocytes
    • Chen L, Teng N, Buchanan J: Mitogenicity of thrombin and surface alterations on mouse splenocytes. Exp Cell Res 101:41, 1976
    • (1976) Exp Cell Res , vol.101 , pp. 41
    • Chen, L.1    Teng, N.2    Buchanan, J.3
  • 48
    • 0344908213 scopus 로고
    • Identification of a thrombin sequence with growth factor activity on macrophages
    • Bar-Shavit R, Kahn AJ, Mann KG, Wilner GD: Identification of a thrombin sequence with growth factor activity on macrophages. Proc Natl Acad Sci USA 83:976, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 976
    • Bar-Shavit, R.1    Kahn, A.J.2    Mann, K.G.3    Wilner, G.D.4
  • 50
    • 0024439913 scopus 로고
    • Thrombin's effects on osteoblastic cells. I. Cytolosolic calcium and phosphoinositides
    • Tatakis D, Dolce C, Dziak R: Thrombin's effects on osteoblastic cells. I. Cytolosolic calcium and phosphoinositides. Biochem Biophys Res Commun 164:119, 1989
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 119
    • Tatakis, D.1    Dolce, C.2    Dziak, R.3
  • 52
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR: Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64:1057, 1991
    • (1991) Cell , vol.64 , pp. 1057
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 53
    • 0028907488 scopus 로고
    • Regulation of thrombin receptors on human umbilical vein endothelial cells
    • Woolkalis M, DeMelfi TJ, Blanchard N, Hoxie J, Brass L: Regulation of thrombin receptors on human umbilical vein endothelial cells. J Biol Chem 270:9868, 1995
    • (1995) J Biol Chem , vol.270 , pp. 9868
    • Woolkalis, M.1    DeMelfi, T.J.2    Blanchard, N.3    Hoxie, J.4    Brass, L.5
  • 54
    • 0028111114 scopus 로고
    • Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling
    • Brass LF, Pizarro S, Ahuja M, Belmonte E, Blanchard N, Stadel JM, Hoxie JA: Changes in the structure and function of the human thrombin receptor during receptor activation, internalization, and recycling. J Biol Chem 269:2943, 1994
    • (1994) J Biol Chem , vol.269 , pp. 2943
    • Brass, L.F.1    Pizarro, S.2    Ahuja, M.3    Belmonte, E.4    Blanchard, N.5    Stadel, J.M.6    Hoxie, J.A.7
  • 55
    • 0030008312 scopus 로고    scopus 로고
    • Role of the thrombin receptor in development and evidence for a second receptor
    • Connolly A, Ishihara H, Kahn M, Farese R Jr, Coughlin S: Role of the thrombin receptor in development and evidence for a second receptor. Nature 381:516, 1996
    • (1996) Nature , vol.381 , pp. 516
    • Connolly, A.1    Ishihara, H.2    Kahn, M.3    Farese Jr., R.4    Coughlin, S.5
  • 57
    • 0026662994 scopus 로고
    • Human neutrophils synthesize thrombomodulin that does not promote thrombin-dependent protein C activation
    • Conway E, Nowakowski B, Steiner-Mosonyi M: Human neutrophils synthesize thrombomodulin that does not promote thrombin-dependent protein C activation. Blood 80:1254, 1992
    • (1992) Blood , vol.80 , pp. 1254
    • Conway, E.1    Nowakowski, B.2    Steiner-Mosonyi, M.3
  • 58
    • 0026328854 scopus 로고
    • Thrombomodulin expression by human blood monocytes and by human synovial tissue lining macrophages
    • McCachren SS, Diggs J, Weinberg JB, Dittman WA: Thrombomodulin expression by human blood monocytes and by human synovial tissue lining macrophages. Blood 78:3128, 1991
    • (1991) Blood , vol.78 , pp. 3128
    • McCachren, S.S.1    Diggs, J.2    Weinberg, J.B.3    Dittman, W.A.4
  • 59
    • 0025981411 scopus 로고
    • Expression of thrombomodulin by smooth muscle cells in culture: Different effects of tumor necrosis factor and cyclic adenosine monophosphate on thrombomodulin expression by endothelial cells and smooth muscle cells in culture
    • Soff GA, Jackman RW, Rosenberg RD: Expression of thrombomodulin by smooth muscle cells in culture: Different effects of tumor necrosis factor and cyclic adenosine monophosphate on thrombomodulin expression by endothelial cells and smooth muscle cells in culture. Blood 77:515, 1991
    • (1991) Blood , vol.77 , pp. 515
    • Soff, G.A.1    Jackman, R.W.2    Rosenberg, R.D.3
  • 60
    • 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 W, Husain M, Rayburn H, Rosenberg R: Targeting of transgene expression to the vascular endothelium of mice by homologous recombination at the thrombomodulin locus. Circ Res 78:180, 1996
    • (1996) Circ Res , vol.78 , pp. 180
    • Weiler-Guettler, H.1    Aird, W.2    Husain, M.3    Rayburn, H.4    Rosenberg, R.5
  • 61
    • 0025311255 scopus 로고
    • Identification of fetomodulin, a surface marker protein of fetal development, as thrombomodulin by gene cloning and functional assays
    • Imada S, Yamaguchi H, Nagumo M, Katayanagi S, Iwasaki H, Imada M: Identification of fetomodulin, a surface marker protein of fetal development, as thrombomodulin by gene cloning and functional assays. Dev Biol 140:113, 1990
    • (1990) Dev Biol , vol.140 , pp. 113
    • Imada, S.1    Yamaguchi, H.2    Nagumo, M.3    Katayanagi, S.4    Iwasaki, H.5    Imada, M.6
  • 62
    • 0028876697 scopus 로고
    • Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system
    • Healy A, Rayburn H, Rosenberg R, 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 92:850, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 850
    • Healy, A.1    Rayburn, H.2    Rosenberg, R.3    Weiler, H.4
  • 63
    • 0028872958 scopus 로고
    • Use of lectins as diagnostic and therapeutic tools for cancer
    • Mody R, Joshi S, Chaney W: Use of lectins as diagnostic and therapeutic tools for cancer. J Pharmacol Toxicol Methods 33:1, 1995
    • (1995) J Pharmacol Toxicol Methods , vol.33 , pp. 1
    • Mody, R.1    Joshi, S.2    Chaney, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.