메뉴 건너뛰기




Volumn 29, Issue 12, 1997, Pages 643-645

Integrin chatter and vascular function in diabetic retinopathy

Author keywords

Advanced Glycation Endproducts; Diabetic Retinopathy; Plasminogen Activation; Vascular Integrins; Vitronectin Receptors

Indexed keywords

INTEGRIN; VITRONECTIN RECEPTOR;

EID: 0031453118     PISSN: 00185043     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-979118     Document Type: Conference Paper
Times cited : (22)

References (28)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O.: Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25 (1992)
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • Meredith, J. E., B. Fazeli, M. A. Schwartz: The extracellular matrix as a cell survival factor. Mol Biol Cell 4: 953-961 (1993)
    • (1993) Mol Biol Cell , vol.4 , pp. 953-961
    • Meredith, J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 5
    • 0028968007 scopus 로고
    • Fibronectin, laminin, vitronectin and their receptors at newly-formed capillaries in proliferative diabetic retinopathy
    • Casaroli Marano, R. P., K. T. Preissner, S. Vilaro: Fibronectin, laminin, vitronectin and their receptors at newly-formed capillaries in proliferative diabetic retinopathy. Exp Eye Res 60: 5-17 (1995)
    • (1995) Exp Eye Res , vol.60 , pp. 5-17
    • Casaroli Marano, R.P.1    Preissner, K.T.2    Vilaro, S.3
  • 6
    • 0028887861 scopus 로고
    • Vessel wall-dependent metabolic pathways of the adhesive proteins, von-Willebrand-factor and vitro-nectin
    • Preissner, K. T., B. Pötzsch: Vessel wall-dependent metabolic pathways of the adhesive proteins, von-Willebrand-factor and vitro-nectin. Histol Histopathol 10: 239-251 (1995)
    • (1995) Histol Histopathol , vol.10 , pp. 239-251
    • Preissner, K.T.1    Pötzsch, B.2
  • 7
    • 0029830984 scopus 로고    scopus 로고
    • Modification of vitronectin by advanced glycation alters functional properties in vitro and in the diabetic retina
    • Hommes, H. P., A. Weiss, S. Hess, N. Araki, S. Horiuchi, M. Brownlee, K. T. Preissner: Modification of vitronectin by advanced glycation alters functional properties in vitro and in the diabetic retina. Lab Invest 75: 325-338 (1996)
    • (1996) Lab Invest , vol.75 , pp. 325-338
    • Hommes, H.P.1    Weiss, A.2    Hess, S.3    Araki, N.4    Horiuchi, S.5    Brownlee, M.6    Preissner, K.T.7
  • 8
    • 0028174337 scopus 로고
    • Glioblastoma growth inhibited in vivo by a dominant-negative Flk-1 mutant
    • Millauer, B., L. K. Shawver, K. H. Plate, W. Risau, A. Ullrich: Glioblastoma growth inhibited in vivo by a dominant-negative Flk-1 mutant. Nature 367: 576-579 (1994)
    • (1994) Nature , vol.367 , pp. 576-579
    • Millauer, B.1    Shawver, L.K.2    Plate, K.H.3    Risau, W.4    Ullrich, A.5
  • 9
    • 0028343059 scopus 로고
    • Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors
    • Novogrodsky, A., A. Vanichkin, M. Patya, A. Gazit, N. Osherov, A. Levitzki: Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors. Science 264: 1319-1322 (1994)
    • (1994) Science , vol.264 , pp. 1319-1322
    • Novogrodsky, A.1    Vanichkin, A.2    Patya, M.3    Gazit, A.4    Osherov, N.5    Levitzki, A.6
  • 10
    • 0029925079 scopus 로고    scopus 로고
    • Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization
    • Hammes, H. P., M. Brownlee, A. Joncyk, A. Sutter, K. T. Preissner: Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization. Nature Med 2: 529-533 (1996)
    • (1996) Nature Med , vol.2 , pp. 529-533
    • Hammes, H.P.1    Brownlee, M.2    Joncyk, A.3    Sutter, A.4    Preissner, K.T.5
  • 14
    • 0028058734 scopus 로고
    • Pericellular enzymatic hydrolysis: Implications for the regulation of cell proliferation in the vessel wall and the bone marrow
    • Brunner, G., K. T. Preissner: Pericellular enzymatic hydrolysis: implications for the regulation of cell proliferation in the vessel wall and the bone marrow. Blood Coagul Fibrinol 5: 625-639 (1994)
    • (1994) Blood Coagul Fibrinol , vol.5 , pp. 625-639
    • Brunner, G.1    Preissner, K.T.2
  • 15
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin
    • Preissner, K. T.: Structure and biological role of vitronectin. Ann Rev Cell Biol 7: 275-310 (1991)
    • (1991) Ann Rev Cell Biol , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 16
    • 0029156876 scopus 로고
    • Role of the plasminogen/plasmin system in thrombosis, hemostasis, restenosis and atherosclerosis
    • Carmeliet, P., D. Collen: Role of the plasminogen/plasmin system in thrombosis, hemostasis, restenosis and atherosclerosis.Trends Cardiovasc Med 5: 117-122 (1995)
    • (1995) Trends Cardiovasc Med , vol.5 , pp. 117-122
    • Carmeliet, P.1    Collen, D.2
  • 17
    • 0026341460 scopus 로고
    • In vivo paracrine interaction between urokinase and its receptor: Effect on tumor cell invasion
    • Ossowski, L., G. Clunie, M.-T. Masucci, F. Blasi: In vivo paracrine interaction between urokinase and its receptor: effect on tumor cell invasion. J Cell Biol 115: 1107-1112 (1991)
    • (1991) J Cell Biol , vol.115 , pp. 1107-1112
    • Ossowski, L.1    Clunie, G.2    Masucci, M.-T.3    Blasi, F.4
  • 19
    • 0029670093 scopus 로고    scopus 로고
    • Cooperative effect of TNF α, bFGF, and VEGF on the formation of tubular structures of human microvascular endothelial cells in a fibrin matrix. Role of urokinase activity
    • Koolwijk, P., M. G. M. van Erck, W. J. A. de Vree, M. A. Vermeer, H. A. Weich, R. Hanemaaijer, V. W. M. van Hinsbergh: Cooperative effect of TNF α, bFGF, and VEGF on the formation of tubular structures of human microvascular endothelial cells in a fibrin matrix. Role of urokinase activity. J Cell Biol 132: 1177-1188 (1996)
    • (1996) J Cell Biol , vol.132 , pp. 1177-1188
    • Koolwijk, P.1    Van Erck, M.G.M.2    De Vree, W.J.A.3    Vermeer, M.A.4    Weich, H.A.5    Hanemaaijer, R.6    Van Hinsbergh, V.W.M.7
  • 21
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Wie, Y., D. A. Waltz, N. Rao, R. J. Drummond, S. Rosenberg, H. A. Chapman: Identification of the urokinase receptor as an adhesion receptor for vitronectin. J Biol Chem 269: 32 380-32 388 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 32380-32388
    • Wie, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 22
    • 0028331139 scopus 로고
    • The urokinase receptor is required for human monocyte chemotaxis in vitro
    • Gyetko, M. R., R. F. Todd III, C. C. Wilkinson, R. C. Sitrin: The urokinase receptor is required for human monocyte chemotaxis in vitro. J Clin Invest 93: 1380-1387 (1994)
    • (1994) J Clin Invest , vol.93 , pp. 1380-1387
    • Gyetko, M.R.1    Todd III, R.F.2    Wilkinson, C.C.3    Sitrin, R.C.4
  • 23
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin binding protein on endothelial cells
    • Kanse, S. M., C. Kost, O. G. Wilhelm, P. A. Andreasen, K. T. Preissner: The urokinase receptor is a major vitronectin binding protein on endothelial cells. Exp Cell Res 224: 344-353 (1996)
    • (1996) Exp Cell Res , vol.224 , pp. 344-353
    • Kanse, S.M.1    Kost, C.2    Wilhelm, O.G.3    Andreasen, P.A.4    Preissner, K.T.5
  • 25
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjoller, L., S. M. Kanse, T. Kirkegaard, K. W. Rodenburg, E. Ronne, S. L: Goodman, K. T. Preissner, L. Ossowski, P. A. Andreasen: Plasminogen activator inhibitor-1 represses integrin-and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation. Exp Cell Res 232: 420-429 (1997)
    • (1997) Exp Cell Res , vol.232 , pp. 420-429
    • Kjoller, L.1    Kanse, S.M.2    Kirkegaard, T.3    Rodenburg, K.W.4    Ronne, E.5    Goodman, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 28
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Resnati, M., M. Guttinger, S. Valcamonica, N. Sidenius, F. Blasi, F. Fazioli: Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J 15: 1572-1582 (1996)
    • (1996) EMBO J , vol.15 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3    Sidenius, N.4    Blasi, F.5    Fazioli, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.