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Volumn 65, Issue 6, 1998, Pages 844-853

α-Galactosyl epitope-mediated activation of porcine aortic endothelial cells: Type I activation

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHALASIN D; EPITOPE; GALACTOSE; GENISTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOGLOBULIN M ANTIBODY; LECTIN; LIPOPOLYSACCHARIDE; MONOCLONAL ANTIBODY; STAUROSPORINE; TUMOR NECROSIS FACTOR;

EID: 0032571264     PISSN: 00411337     EISSN: None     Source Type: Journal    
DOI: 10.1097/00007890-199803270-00013     Document Type: Article
Times cited : (50)

References (58)
  • 1
    • 0026654128 scopus 로고
    • Mechanism of complement activation in the hyperacute rejection of porcine organs transplanted into primate recipients
    • Dalmasso AP, Vercellotti GM, Fischel RJ, Bolman RM, Bach FH, Platt JL. Mechanism of complement activation in the hyperacute rejection of porcine organs transplanted into primate recipients. Am J Pathol 1992; 140: 1157.
    • (1992) Am J Pathol , vol.140 , pp. 1157
    • Dalmasso, A.P.1    Vercellotti, G.M.2    Fischel, R.J.3    Bolman, R.M.4    Bach, F.H.5    Platt, J.L.6
  • 2
    • 0028203991 scopus 로고
    • Xenotransplantation: Problems posed by endothelial cell activation
    • Bach FH, Blakely ML, Vanderwerf WJ, et al. Xenotransplantation: problems posed by endothelial cell activation. Transplant Proc 1994; 26: 1029.
    • (1994) Transplant Proc , vol.26 , pp. 1029
    • Bach, F.H.1    Blakely, M.L.2    Vanderwerf, W.J.3
  • 3
    • 0028171341 scopus 로고
    • Endothelial cell activation and thromboregulation during xenograft rejection
    • Bach FH, Robson SC, Ferran C, et al. Endothelial cell activation and thromboregulation during xenograft rejection. Immunol Rev 1994; 141: 5.
    • (1994) Immunol Rev , vol.141 , pp. 5
    • Bach, F.H.1    Robson, S.C.2    Ferran, C.3
  • 4
    • 0028905867 scopus 로고
    • Xenotransplantation: Endothelial cell activation and beyond
    • Bach FH, Robson SC, Ferran C, et al. Xenotransplantation: endothelial cell activation and beyond. Transplant Proc 1995; 27: 77.
    • (1995) Transplant Proc , vol.27 , pp. 77
    • Bach, F.H.1    Robson, S.C.2    Ferran, C.3
  • 5
    • 0026327234 scopus 로고
    • The role of natural antibodies in the activation of xenogenic endothelial cells
    • Platt JL, Lindman BJ, Geller RL, et al. The role of natural antibodies in the activation of xenogenic endothelial cells. Transplantation 1991; 52: 1037.
    • (1991) Transplantation , vol.52 , pp. 1037
    • Platt, J.L.1    Lindman, B.J.2    Geller, R.L.3
  • 6
    • 0028073428 scopus 로고
    • A perspective on xenograft rejection and accommodation
    • Platt JL. A perspective on xenograft rejection and accommodation. Immunol Rev 1994; 141: 127.
    • (1994) Immunol Rev , vol.141 , pp. 127
    • Platt, J.L.1
  • 7
    • 0000665022 scopus 로고
    • Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1-3Gal epitope in primates
    • Galili U, Clark MR, Shohet SB, Buehler J, Macher BA. Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1-3Gal epitope in primates. Proc Natl Acad Sci USA 1987; 84: 1369.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1369
    • Galili, U.1    Clark, M.R.2    Shohet, S.B.3    Buehler, J.4    Macher, B.A.5
  • 8
    • 0027517325 scopus 로고
    • Anti-pig IgM antibodies in human serum react predominantly with gal(alpha-1-3)gal epitopes
    • Sandrin MS, Vaughan HA, Dabkowski PL, McKenzie I. Anti-pig IgM antibodies in human serum react predominantly with gal(alpha-1-3)gal epitopes. Proc Natl Acad Sci USA 1993; 90: 11391.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11391
    • Sandrin, M.S.1    Vaughan, H.A.2    Dabkowski, P.L.3    McKenzie, I.4
  • 9
    • 0027508081 scopus 로고
    • Interaction of the natural anti-gal antibody with alpha-galactosyl epitopes: A major obstacle for xenotransplantation in humans
    • Galili U. Interaction of the natural anti-gal antibody with alpha-galactosyl epitopes: a major obstacle for xenotransplantation in humans. Immunol Today 1993; 14: 480.
    • (1993) Immunol Today , vol.14 , pp. 480
    • Galili, U.1
  • 10
    • 0028171342 scopus 로고
    • Oligosaccharides and discordant xenotransplantation
    • Cooper DK, Koren E, Oriol R. Oligosaccharides and discordant xenotransplantation [Review]. Immunol Rev 1994; 141: 31.
    • (1994) Immunol Rev , vol.141 , pp. 31
    • Cooper, D.K.1    Koren, E.2    Oriol, R.3
  • 11
    • 0028171201 scopus 로고
    • Gal α(1,3)Gal is the major xenoepitope expressed on pig endothelial cells recognized by naturally occurring cytotoxic human antibodies
    • Vaughan HA, Loveland BE, Sandrin MS. Gal α(1,3)Gal is the major xenoepitope expressed on pig endothelial cells recognized by naturally occurring cytotoxic human antibodies. Transplantation 1994; 58: 879.
    • (1994) Transplantation , vol.58 , pp. 879
    • Vaughan, H.A.1    Loveland, B.E.2    Sandrin, M.S.3
  • 12
    • 0029039406 scopus 로고
    • Cardiac xenografts between primate species provide evidence for the importance of the alpha-galactosyl determinant in hyperacute rejection
    • Collins BH, Cotterell AH, McCurry KR, et al. Cardiac xenografts between primate species provide evidence for the importance of the alpha-galactosyl determinant in hyperacute rejection. J Immunol 1995; 154: 5500.
    • (1995) J Immunol , vol.154 , pp. 5500
    • Collins, B.H.1    Cotterell, A.H.2    McCurry, K.R.3
  • 13
    • 0027716847 scopus 로고
    • Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation
    • Oriol R, Ye Y, Koren E, Cooper D. Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man organ xenotransplantation. Transplantation 1993; 56: 1433.
    • (1993) Transplantation , vol.56 , pp. 1433
    • Oriol, R.1    Ye, Y.2    Koren, E.3    Cooper, D.4
  • 14
    • 0024297335 scopus 로고
    • Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells
    • Galili U, Shohet SB, Kobrin E, Stults CL, Macher BA. Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells. J Biol Chem 1988; 263: 17755.
    • (1988) J Biol Chem , vol.263 , pp. 17755
    • Galili, U.1    Shohet, S.B.2    Kobrin, E.3    Stults, C.L.4    Macher, B.A.5
  • 15
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-alpha-galactosyl specificity
    • Galili U, Rachmilewitz EA, Peleg A, Flechner I. A unique natural human IgG antibody with anti-alpha-galactosyl specificity. J Exp Med 1984; 160: 1519.
    • (1984) J Exp Med , vol.160 , pp. 1519
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 16
    • 0022260876 scopus 로고
    • Human natural anti-alpha-galactosyl IgG: II. The specific recognition of alpha (1-3)-linked galactose residues
    • Galili U, Macher BA, Buehler J, Shohet SB. Human natural anti-alpha-galactosyl IgG: II. The specific recognition of alpha (1-3)-linked galactose residues. J Exp Med 1985; 162: 573.
    • (1985) J Exp Med , vol.162 , pp. 573
    • Galili, U.1    Macher, B.A.2    Buehler, J.3    Shohet, S.B.4
  • 17
    • 0027367160 scopus 로고
    • One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody
    • Galili U, Anaraki F, Thall A, Hill BC, Radic M. One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody. Blood 1993; 82: 2485.
    • (1993) Blood , vol.82 , pp. 2485
    • Galili, U.1    Anaraki, F.2    Thall, A.3    Hill, B.C.4    Radic, M.5
  • 18
    • 85047235720 scopus 로고
    • Contribution of anti-Gal to primate and human IgG binding to porcine endothelial cells
    • Galili U, Gregory CR, Morris RE. Contribution of anti-Gal to primate and human IgG binding to porcine endothelial cells. Transplantation 1995; 60: 210.
    • (1995) Transplantation , vol.60 , pp. 210
    • Galili, U.1    Gregory, C.R.2    Morris, R.E.3
  • 19
    • 0025971245 scopus 로고
    • Natural antibody targets on discordant endothelium: Molecular characterization and consequences of antibody binding
    • Platt JL, Lindman BJ, Bach FH. Natural antibody targets on discordant endothelium: molecular characterization and consequences of antibody binding. Transplant Proc 1991; 23: 815.
    • (1991) Transplant Proc , vol.23 , pp. 815
    • Platt, J.L.1    Lindman, B.J.2    Bach, F.H.3
  • 20
    • 0028836883 scopus 로고
    • Biochemical studies of pig xenoantigens detected by naturally occurring human anti-bodies and the galactose α(1-3)galactose reactive lectin
    • Vaughan HA, McKenzie IF, Sandrin MS. Biochemical studies of pig xenoantigens detected by naturally occurring human anti-bodies and the galactose α(1-3)galactose reactive lectin. Transplantation 1995; 59: 102.
    • (1995) Transplantation , vol.59 , pp. 102
    • Vaughan, H.A.1    McKenzie, I.F.2    Sandrin, M.S.3
  • 21
    • 0028799580 scopus 로고
    • Removal of baboon and human antiporcine IgG and IgM natural antibodies by immunoadsorption: Results of in vitro and in vivo studies
    • Leventhal JR, John R, Fryer JP, et al. Removal of baboon and human antiporcine IgG and IgM natural antibodies by immunoadsorption: results of in vitro and in vivo studies. Transplantation 1995; 59: 294.
    • (1995) Transplantation , vol.59 , pp. 294
    • Leventhal, J.R.1    John, R.2    Fryer, J.P.3
  • 22
    • 0029101190 scopus 로고
    • Antibody removal by column immunoabsorption prevents tissue injury in an ex vivo model of pig-to-human xenograft hyperacute rejection
    • Kroshus TJ, Dalmasso AP, Leventhal JR, John R, Matas AJ, Bolman RM. Antibody removal by column immunoabsorption prevents tissue injury in an ex vivo model of pig-to-human xenograft hyperacute rejection. J Surg Res 1995; 59: 43.
    • (1995) J Surg Res , vol.59 , pp. 43
    • Kroshus, T.J.1    Dalmasso, A.P.2    Leventhal, J.R.3    John, R.4    Matas, A.J.5    Bolman, R.M.6
  • 23
    • 0029996878 scopus 로고    scopus 로고
    • Removal of terminal α-galactosyl residues from xenogeneic porcine endothelial cells: Decrease in complement-mediated cytotoxicity but persistence of IgG1-mediated antibody-dependent cell-mediated cytotoxicity
    • Watier H, Guillaumin JM, Piller F, et al. Removal of terminal α-galactosyl residues from xenogeneic porcine endothelial cells: decrease in complement-mediated cytotoxicity but persistence of IgG1-mediated antibody-dependent cell-mediated cytotoxicity. Transplantation 1996; 62: 105.
    • (1996) Transplantation , vol.62 , pp. 105
    • Watier, H.1    Guillaumin, J.M.2    Piller, F.3
  • 24
    • 0030000292 scopus 로고    scopus 로고
    • Selective IgM depletion prolongs organ survival in an ex vivo model of pig-to-human xenotransplantation
    • Kroshus TJ, Bolman RR, Dalmasso AP. Selective IgM depletion prolongs organ survival in an ex vivo model of pig-to-human xenotransplantation. Transplantation 1996; 62: 5.
    • (1996) Transplantation , vol.62 , pp. 5
    • Kroshus, T.J.1    Bolman, R.R.2    Dalmasso, A.P.3
  • 25
    • 0025304016 scopus 로고
    • Cytokines and endothelial cell biology
    • Pober JS, Cotran RS. Cytokines and endothelial cell biology [Review]. Physiol Rev 1990; 70: 427.
    • (1990) Physiol Rev , vol.70 , pp. 427
    • Pober, J.S.1    Cotran, R.S.2
  • 26
    • 0028938634 scopus 로고
    • Transient perturbation of endothelial integrity induced by natural antibodies and complement
    • Saadi S, Platt JL. Transient perturbation of endothelial integrity induced by natural antibodies and complement. J Exp Med 1995; 181: 21.
    • (1995) J Exp Med , vol.181 , pp. 21
    • Saadi, S.1    Platt, J.L.2
  • 27
    • 0017760373 scopus 로고
    • Tissue-factor coagulant activity of cultured human endothelial and smooth muscle cells and fibroblasts
    • Maynard JR, Dreyer BE, Stemerman MB, Pitlick FA. Tissue-factor coagulant activity of cultured human endothelial and smooth muscle cells and fibroblasts. Blood 1977; 50: 387.
    • (1977) Blood , vol.50 , pp. 387
    • Maynard, J.R.1    Dreyer, B.E.2    Stemerman, M.B.3    Pitlick, F.A.4
  • 29
    • 0029040071 scopus 로고
    • Identification of porcine endothelial cell membrane antigens recognized by human xenoreactive natural antibodies
    • Holzknecht ZE, Platt JL. Identification of porcine endothelial cell membrane antigens recognized by human xenoreactive natural antibodies. J Immunol 1995; 154: 4565.
    • (1995) J Immunol , vol.154 , pp. 4565
    • Holzknecht, Z.E.1    Platt, J.L.2
  • 30
    • 0030017263 scopus 로고    scopus 로고
    • MAP kinase activation by flow in endothelial cells: Role of beta 1 integrins and tyrosine kinases
    • Ishida T, Peterson TE, Kovach NL, Berk BC. MAP kinase activation by flow in endothelial cells: role of beta 1 integrins and tyrosine kinases. Circ Res 1996; 79: 310.
    • (1996) Circ Res , vol.79 , pp. 310
    • Ishida, T.1    Peterson, T.E.2    Kovach, N.L.3    Berk, B.C.4
  • 31
    • 0028855838 scopus 로고
    • Matrix/integrin interaction activates the mitogen-activated protein kinase, p44Erk-1 and p42Erk-2
    • Morino N, Mimura T, Hamasaki K, et al. Matrix/integrin interaction activates the mitogen-activated protein kinase, p44Erk-1 and p42Erk-2. J Biol Chem 1995; 270: 269.
    • (1995) J Biol Chem , vol.270 , pp. 269
    • Morino, N.1    Mimura, T.2    Hamasaki, K.3
  • 32
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen Q, Kinch MS, Lin TH, Burridge K, Juliano RL. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J Biol Chem 1994; 269: 26602.
    • (1994) J Biol Chem , vol.269 , pp. 26602
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 33
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle PA, Baltimore D. NF-κB: ten years after. Cell 1996; 87: 13.
    • (1996) Cell , vol.87 , pp. 13
    • Baeuerle, P.A.1    Baltimore, D.2
  • 34
    • 0029101772 scopus 로고
    • Transcriptional regulation of endothelial cell adhesion molecules: NF-κB and cytokine-inducible enhancers
    • Collins T, Read MA, Neish AS, Whitley MZ, Thanos D, Maniatis T. Transcriptional regulation of endothelial cell adhesion molecules: NF-κB and cytokine-inducible enhancers [Review]. FASEB J 1995; 9: 899.
    • (1995) FASEB J , vol.9 , pp. 899
    • Collins, T.1    Read, M.A.2    Neish, A.S.3    Whitley, M.Z.4    Thanos, D.5    Maniatis, T.6
  • 35
    • 0029163568 scopus 로고
    • Multi-step activation of NF-κB/Rel transcription factors
    • Schmitz ML, Baeuerle PA. Multi-step activation of NF-κB/Rel transcription factors [Review]. Immunobiology 1995; 193; 116.
    • (1995) Immunobiology , vol.193 , pp. 116
    • Schmitz, M.L.1    Baeuerle, P.A.2
  • 36
    • 0029863521 scopus 로고    scopus 로고
    • The Rel family of eukaryotic transcription factors
    • Chytil M, Verdine GL. The Rel family of eukaryotic transcription factors. Curr Opin Struct Biol 1996; 6: 91.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 91
    • Chytil, M.1    Verdine, G.L.2
  • 37
    • 0029617910 scopus 로고
    • Evidence for a role of MEK and MAPK during signal transduction by protein kinase C zeta
    • Berra E, Diaz MM, Lozano J, et al. Evidence for a role of MEK and MAPK during signal transduction by protein kinase C zeta. EMBO J 1995; 14: 6157.
    • (1995) EMBO J , vol.14 , pp. 6157
    • Berra, E.1    Diaz, M.M.2    Lozano, J.3
  • 38
    • 0030896415 scopus 로고    scopus 로고
    • Early activation signals in endothelial cells: Stimulation by cytokines
    • Introna M, Mantovani A. Early activation signals in endothelial cells: stimulation by cytokines [Review]. Arterioscler Thromb Vasc Biol 1997; 17: 423.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 423
    • Introna, M.1    Mantovani, A.2
  • 39
    • 0017413222 scopus 로고
    • Five alpha-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds
    • Murphy LA, Goldstein IJ. Five alpha-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds. J Biol Chem 1977; 252: 4739.
    • (1977) J Biol Chem , vol.252 , pp. 4739
    • Murphy, L.A.1    Goldstein, I.J.2
  • 40
    • 0018039445 scopus 로고
    • A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides
    • Kisailus EC, Kabat EA. A study of the specificity of Bandeiraea simplicifolia lectin I by competitive-binding assay with blood-group substances and with blood-group A and B active and other oligosaccharides. Carbohydr Res 1978; 67: 243.
    • (1978) Carbohydr Res , vol.67 , pp. 243
    • Kisailus, E.C.1    Kabat, E.A.2
  • 41
    • 0028028804 scopus 로고
    • Human xenoreactive natural antibodies of the IgM isotype activate pig endothelial cells
    • Vanhove B, deMartin R, Lipp J, Bach FH. Human xenoreactive natural antibodies of the IgM isotype activate pig endothelial cells. Xenotransplant 1994; 1: 17.
    • (1994) Xenotransplant , vol.1 , pp. 17
    • Vanhove, B.1    DeMartin, R.2    Lipp, J.3    Bach, F.H.4
  • 43
    • 0002164801 scopus 로고    scopus 로고
    • Human IgM xenoreactive natural antibodies can induce resistance of porcine endothelial cells to complement-mediated injury
    • Dalmasso AP, He T, Benson BA. Human IgM xenoreactive natural antibodies can induce resistance of porcine endothelial cells to complement-mediated injury. Xenotransplant 1996; 3: 54.
    • (1996) Xenotransplant , vol.3 , pp. 54
    • Dalmasso, A.P.1    He, T.2    Benson, B.A.3
  • 44
    • 0028179224 scopus 로고
    • NF-kappa B and I kappa B alpha: An inducible regulatory system in endothelial activation
    • Read MA, Whitley MZ, Williams AJ, Collins T. NF-kappa B and I kappa B alpha: an inducible regulatory system in endothelial activation. J Exp Med 1994; 179: 503.
    • (1994) J Exp Med , vol.179 , pp. 503
    • Read, M.A.1    Whitley, M.Z.2    Williams, A.J.3    Collins, T.4
  • 45
    • 0031027505 scopus 로고    scopus 로고
    • Inhibition of bovine endothelial cell activation in vitro by regulated expression of a transdominant inhibitor of NF-κB
    • Anrather J, Csizmadia V, Brostjan C, Soares MP, Bach FH, Winkler H. Inhibition of bovine endothelial cell activation in vitro by regulated expression of a transdominant inhibitor of NF-κB. J Clin Invest 1997; 99: 763.
    • (1997) J Clin Invest , vol.99 , pp. 763
    • Anrather, J.1    Csizmadia, V.2    Brostjan, C.3    Soares, M.P.4    Bach, F.H.5    Winkler, H.6
  • 46
    • 0024309730 scopus 로고
    • Tumor necrosis factor/cachectin increases permeability of endothelial cell monolayers by a mechanism involving regulatory G proteins
    • Brett J, Gerlach H, Nawroth P, Steinberg S, Godman G, Stern D. Tumor necrosis factor/cachectin increases permeability of endothelial cell monolayers by a mechanism involving regulatory G proteins. J Exp Med 1989; 169: 1977.
    • (1989) J Exp Med , vol.169 , pp. 1977
    • Brett, J.1    Gerlach, H.2    Nawroth, P.3    Steinberg, S.4    Godman, G.5    Stern, D.6
  • 47
    • 0026013429 scopus 로고
    • The role of integrins in the maintenance of endothelial monolayer integrity
    • Lampugnani MG, Resnati M, Dejana E, Marchisio PC. The role of integrins in the maintenance of endothelial monolayer integrity. J Cell Biol 1991; 112: 479.
    • (1991) J Cell Biol , vol.112 , pp. 479
    • Lampugnani, M.G.1    Resnati, M.2    Dejana, E.3    Marchisio, P.C.4
  • 48
    • 0029906950 scopus 로고    scopus 로고
    • The immunological barriers to xenotransplantation
    • Platt JL. The immunological barriers to xenotransplantation. Crit Rev Immunol 1996; 16: 331.
    • (1996) Crit Rev Immunol , vol.16 , pp. 331
    • Platt, J.L.1
  • 49
    • 0028901094 scopus 로고
    • Stimulation of tyrosine phosphorylation of distinct proteins in response to antibody-mediated ligation and clustering of alpha 3 and alpha 6 integrins
    • Jewell K, Kapron BC, Jeevaratnam P, Dedhar S. Stimulation of tyrosine phosphorylation of distinct proteins in response to antibody-mediated ligation and clustering of alpha 3 and alpha 6 integrins. J Cell Sci 1995; 108: 1165.
    • (1995) J Cell Sci , vol.108 , pp. 1165
    • Jewell, K.1    Kapron, B.C.2    Jeevaratnam, P.3    Dedhar, S.4
  • 50
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins
    • Kornberg LJ, Earp HS, Turner CE, Prockop C, Juliano RL. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins. Proc Natl Acad Sci USA 1991; 88: 8392.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8392
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 51
    • 0029670904 scopus 로고    scopus 로고
    • Stimulation of beta1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF beta-receptors
    • Sundberg C, Rubin K. Stimulation of beta1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF beta-receptors. J Cell Biol 1996; 132: 741.
    • (1996) J Cell Biol , vol.132 , pp. 741
    • Sundberg, C.1    Rubin, K.2
  • 52
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson A, Parsons JT. Signal transduction through integrins: a central role for focal adhesion kinase? [Review]. BioEssays 1995; 17: 229.
    • (1995) BioEssays , vol.17 , pp. 229
    • Richardson, A.1    Parsons, J.T.2
  • 53
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons JT. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins [Review]. Curr Opin Cell Biol 1996; 8: 146.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 146
    • Parsons, J.T.1
  • 54
    • 0029034873 scopus 로고
    • Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs
    • Nojima Y, Morino N, Mimura T, et al. Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs. J Biol Chem 1995; 270: 15398.
    • (1995) J Biol Chem , vol.270 , pp. 15398
    • Nojima, Y.1    Morino, N.2    Mimura, T.3
  • 55
    • 0028981376 scopus 로고
    • Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix
    • Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix. J Biol Chem 1995; 270: 22259.
    • (1995) J Biol Chem , vol.270 , pp. 22259
    • Vuori, K.1    Ruoslahti, E.2
  • 56
    • 0030980701 scopus 로고    scopus 로고
    • Porcine and bovine cartilage transplants in cynomolgus monkey: II. Changes in anti-Gal response during chronic rejection
    • Galili U, LaTemple DC, Walgenbach AW, Stone KR. Porcine and bovine cartilage transplants in cynomolgus monkey: II. Changes in anti-Gal response during chronic rejection. Transplantation 1997; 63: 646.
    • (1997) Transplantation , vol.63 , pp. 646
    • Galili, U.1    LaTemple, D.C.2    Walgenbach, A.W.3    Stone, K.R.4
  • 57
    • 0028119564 scopus 로고
    • Tyrosine kinase inhibitors impair fibroblast growth factor signaling in coronary endothelial cells
    • Hawker JJ, Granger HJ. Tyrosine kinase inhibitors impair fibroblast growth factor signaling in coronary endothelial cells. Am J Physiol 1994; 266: 107.
    • (1994) Am J Physiol , vol.266 , pp. 107
    • Hawker, J.J.1    Granger, H.J.2
  • 58
    • 0030046992 scopus 로고    scopus 로고
    • Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane-associated 80-kD protein
    • Xia Y, Gil SG, Carter WG. Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane-associated 80-kD protein. J Cell Biol 1996; 132: 727.
    • (1996) J Cell Biol , vol.132 , pp. 727
    • Xia, Y.1    Gil, S.G.2    Carter, W.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.