메뉴 건너뛰기




Volumn 65, Issue 10, 2013, Pages 807-818

Vitronectin - Master controller or micromanager?

Author keywords

coagulation; extracellular matrix; growth factor; multi protein complex; thrombogenesis; vitronectin

Indexed keywords

CELL SURFACE RECEPTOR; MONOMER; MULTIPROTEIN COMPLEX; POLYMER; POLYPEPTIDE; PROTEIN S; VITRONECTIN;

EID: 84884976902     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1203     Document Type: Review
Times cited : (102)

References (136)
  • 1
    • 0014059107 scopus 로고
    • Preparation from human serum of an alpha-one protein which induces the immediate growth of unadapted cells in vitro
    • Holmes, R., (1967) Preparation from human serum of an alpha-one protein which induces the immediate growth of unadapted cells in vitro. J. Cell Biol. 32, 297-308.
    • (1967) J. Cell Biol. , vol.32 , pp. 297-308
    • Holmes, R.1
  • 2
    • 0017729783 scopus 로고
    • Cell adhesion and spreading factor. Partial purification and properties
    • Grinnell, F., Hays, D. G., and, Minter, D., (1977) Cell adhesion and spreading factor. Partial purification and properties. Exp. Cell Res. 110, 175-190. (Pubitemid 8243348)
    • (1977) Experimental Cell Research , vol.110 , Issue.1 , pp. 175-190
    • Grinnell, F.1    Hays, D.G.2    Minter, D.3
  • 3
    • 84914268518 scopus 로고
    • The membrane attack mechanism of complement. Isolation and subunit composition of the C5b-9 complex
    • Kolb, W. P., and, Muller-Eberhard, H. J., (1975) The membrane attack mechanism of complement. Isolation and subunit composition of the C5b-9 complex. J. Exp. Med. 141, 24-35.
    • (1975) J. Exp. Med. , vol.141 , pp. 24-35
    • Kolb, W.P.1    Muller-Eberhard, H.J.2
  • 4
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin)
    • Declerck, P. J., De Mol M., Alessi M. C., Baudner S., Paques E. P., et al. (1988) Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J. Biol. Chem. 263, 15454-15461.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3    Baudner, S.4    Paques, E.P.5
  • 5
    • 0025774971 scopus 로고
    • Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin
    • Seiffert, D., and, Loskutoff D. J., (1991) Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin. J. Biol. Chem. 266, 2824-2830. (Pubitemid 21909141)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.5 , pp. 2824-2830
    • Seiffert, D.1    Loskutoff, D.J.2
  • 7
    • 0018691713 scopus 로고
    • Isolation of human S-protein, an inhibitor of the membrane attack complex of complement
    • Podack, E. R., and, Muller-Eberhard, H. J., (1979) Isolation of human S-protein, an inhibitor of the membrane attack complex of complement. J. Biol. Chem. 254, 9808-9814.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9808-9814
    • Podack, E.R.1    Muller-Eberhard, H.J.2
  • 8
    • 0030991956 scopus 로고    scopus 로고
    • A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development
    • DOI 10.1074/jbc.272.21.13527
    • Yang, M., Murray, M. T., and, Kurkinen, M., (1997) A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development. J. Biol. Chem. 272, 13527-13533. (Pubitemid 27224781)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13527-13533
    • Yang, M.1    Murray, M.T.2    Kurkinen, M.3
  • 9
    • 0031746579 scopus 로고    scopus 로고
    • Role of vitronectin and its receptors in haemostasis and vascular remodeling
    • DOI 10.1016/S0049-3848(97)00298-3, PII S0049384897002983
    • Preissner, K. T., and, Seiffert, D., (1998) Role of vitronectin and its receptors in haemostasis and vascular remodeling. Thromb. Res. 89, 1-21. (Pubitemid 28231482)
    • (1998) Thrombosis Research , vol.89 , Issue.1 , pp. 1-21
    • Preissner, K.T.1    Seiffert, D.2
  • 10
    • 0024562154 scopus 로고
    • Vitronectin exists in two structurally and distinct forms in human plasma
    • Izumi, M., Yamada, K. M., and, Hayashi, M., (1989) Vitronectin exists in two structurally and functionally distinct forms in human plasma. Biochim. Biophys. Acta 990, 101-108. (Pubitemid 19055401)
    • (1989) Biochimica et Biophysica Acta - General Subjects , vol.990 , Issue.2 , pp. 101-108
    • Izumi, M.1    Yamada, K.M.2    Hayashi, M.3
  • 11
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin
    • Preissner, K. T., (1991) Structure and biological role of vitronectin. Annu. Rev. Cell Biol. 7, 275-310.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 14
    • 0028978233 scopus 로고
    • Alpha v beta 5 integrin receptor-mediated endocytosis of vitronectin is protein kinase C-dependent
    • Panetti, T. S., Wilcox S. A., Horzempa C., and, McKeown-Longo, P. J., (1995) Alpha v beta 5 integrin receptor-mediated endocytosis of vitronectin is protein kinase C-dependent. J. Biol. Chem. 270, 18593-18597.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18593-18597
    • Panetti, T.S.1    Wilcox, S.A.2    Horzempa, C.3    McKeown-Longo, P.J.4
  • 15
    • 0030834258 scopus 로고    scopus 로고
    • Constitutive and regulated expression of vitronectin
    • Seiffert, D., (1997) Constitutive and regulated expression of vitronectin. Histol. Histopathol. 12, 787-797. (Pubitemid 27314710)
    • (1997) Histology and Histopathology , vol.12 , Issue.3 , pp. 787-797
    • Seiffert, D.1
  • 16
    • 0029074354 scopus 로고
    • Complement inhibition by human vitronectin involves non-heparin binding domains
    • Sheehan, M., Morris, C. A., Pussell, B. A., and, Charlesworth, J. A., (1995) Complement inhibition by human vitronectin involves non-heparin binding domains. Clin. Exp. Immunol. 101, 136-141.
    • (1995) Clin. Exp. Immunol. , vol.101 , pp. 136-141
    • Sheehan, M.1    Morris, C.A.2    Pussell, B.A.3    Charlesworth, J.A.4
  • 19
    • 79955773310 scopus 로고    scopus 로고
    • Interaction of late apoptotic and necrotic cells with vitronectin
    • Stepanek, O., Brdicka, T., Angelisova, P., Horvath, O., Spicka, J., et al. (2011) Interaction of late apoptotic and necrotic cells with vitronectin. PLoS One 6, e19243.
    • (2011) PLoS One , vol.6
    • Stepanek, O.1    Brdicka, T.2    Angelisova, P.3    Horvath, O.4    Spicka, J.5
  • 20
    • 0026334978 scopus 로고
    • Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells
    • Gladson, C. L., and, Cheresh, D. A., (1991) Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells. J. Clin. Invest. 88, 1924-1932.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1924-1932
    • Gladson, C.L.1    Cheresh, D.A.2
  • 21
    • 0028132865 scopus 로고
    • Vitronectin in colorectal adenocarcinoma - Synthesis by stromal cells in culture
    • DOI 10.1006/excr.1994.1262
    • Tomasini-Johansson, B. R., Sundberg, C., Lindmark, G., Gailit, J. O., and, Rubin, K., (1994) Vitronectin in colorectal adenocarcinoma-synthesis by stromal cells in culture. Exp. Cell Res. 214, 303-312. (Pubitemid 24302406)
    • (1994) Experimental Cell Research , vol.214 , Issue.1 , pp. 303-312
    • Tomasini-Johansson, B.R.1    Sundberg, C.2    Lindmark, G.3    Gailit, J.O.4    Rubin, K.5
  • 23
    • 0023900356 scopus 로고
    • Comparative distribution of fibronectin and vitronectin in human breast and colon carcinomas. An immunofluorescence study
    • Loridon-Rosa, B., Vielh, P., Cuadrado, C., and, Burtin, P., (1988) Comparative distribution of fibronectin and vitronectin in human breast and colon carcinomas. An immunofluorescence study. Am. J. Clin. Pathol. 90, 7-16.
    • (1988) Am. J. Clin. Pathol. , vol.90 , pp. 7-16
    • Loridon-Rosa, B.1    Vielh, P.2    Cuadrado, C.3    Burtin, P.4
  • 24
    • 0026780644 scopus 로고
    • Persistent complement activation on tumor cells in breast cancer
    • Niculescu, F., Rus, H. G., Retegan, M., and, Vlaicu, R., (1992) Persistent complement activation on tumor cells in breast cancer. Am. J. Pathol. 140, 1039-1043.
    • (1992) Am. J. Pathol. , vol.140 , pp. 1039-1043
    • Niculescu, F.1    Rus, H.G.2    Retegan, M.3    Vlaicu, R.4
  • 25
    • 0032544409 scopus 로고    scopus 로고
    • Phosphorylation of vitronectin by casein kinase II: Identification of the sites and their promotion of cell adhesion and spreading
    • DOI 10.1074/jbc.273.38.24805
    • Seger, D., Gechtman, Z., and, Shaltiel, S., (1998). Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. J. Biol. Chem. 273, 24805-24813. (Pubitemid 28454985)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.38 , pp. 24805-24813
    • Seger, D.1    Gechtman, Z.2    Shaltiel, S.3
  • 26
    • 0027505041 scopus 로고
    • Multimeric vitronectin. Identification and characterization of conformation-dependent self-association of the adhesive protein
    • Stockmann, A., Hess, S., Declerck, P., Timpl, R., and, Preissner, K. T., (1993) Multimeric vitronectin. Identification and characterization of conformation-dependent self-association of the adhesive protein. J. Biol. Chem. 268, 22874-22882. (Pubitemid 23318352)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22874-22882
    • Stockmann, A.1    Hess, S.2    Declerck, P.3    Timpl, R.4    Preissner, K.T.5
  • 27
    • 0029912634 scopus 로고    scopus 로고
    • Type 1 plasminogen activator inhibitor induces multimerization of plasma vitronectin: A suggested mechanism for the generation of the tissue form of vitronectin in vivo
    • DOI 10.1074/jbc.271.47.29644
    • Seiffert, D., and, Loskutoff, D. J., (1996) Type 1 plasminogen activator inhibitor induces multimerization of plasma vitronectin. A suggested mechanism for the generation of the tissue form of vitronectin in vivo. J. Biol. Chem. 271, 29644-29651. (Pubitemid 26389588)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 29644-29651
    • Seiffert, D.1    Loskutoff, D.J.2
  • 28
    • 0037627479 scopus 로고    scopus 로고
    • Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1
    • DOI 10.1042/BJ20021943
    • Gijsbers, R., Ceulemans, H., and, Bollen, M., (2003) Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1. Biochem. J. 371, 321-330. (Pubitemid 36547614)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 321-330
    • Gijsbers, R.1    Ceulemans, H.2    Bollen, M.3
  • 29
    • 0029347102 scopus 로고
    • Diversity of function is inherent in matricellular proteins: An appraisal of thrombospondin 1
    • Bornstein, P., (1995) Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1. J. Cell Biol. 130, 503-506.
    • (1995) J. Cell Biol. , vol.130 , pp. 503-506
    • Bornstein, P.1
  • 30
    • 34547696986 scopus 로고    scopus 로고
    • Determination of the sites of tyrosine O-sulfation in peptides and proteins
    • Yu, Y., Hoffhines, A. J., Moore, K. L., and, Leary, J. A., (2007) Determination of the sites of tyrosine O-sulfation in peptides and proteins. Nat. Methods 4, 583-538.
    • (2007) Nat. Methods , vol.4 , pp. 583-538
    • Yu, Y.1    Hoffhines, A.J.2    Moore, K.L.3    Leary, J.A.4
  • 31
    • 12144259015 scopus 로고    scopus 로고
    • A model for the three-dimensional structure of human plasma vitronectin from small-angle scattering measurements
    • DOI 10.1021/bi048347s
    • Lynn, G. W., Heller, W. T., Mayasundari, A., Minor, K. H., and, Peterson, C. B., (2005) A model for the three-dimensional structure of human plasma vitronectin from small-angle scattering measurements. Biochemistry 44, 565-574. (Pubitemid 40105487)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 565-574
    • Lynn, G.W.1    Heller, W.T.2    Mayasundari, A.3    Minor, K.H.4    Peterson, C.B.5
  • 33
    • 0025213864 scopus 로고
    • Sequence location of a putative transglutaminase cross-linking site in human vitronectin
    • DOI 10.1016/0014-5793(90)80208-Z
    • Skorstengaard, K., Halkier, T., Hojrup, P., and, Mosher, D., (1990) Sequence location of a putative transglutaminase cross-linking site in human vitronectin. FEBS Lett. 262, 269-274. (Pubitemid 20104315)
    • (1990) FEBS Letters , vol.262 , Issue.2 , pp. 269-274
    • Skorstengaard, K.1    Halkier, T.2    Hojrup, P.3    Mosher, D.4
  • 34
    • 0017880606 scopus 로고
    • Primary structure of somatomedin B. A growth hormone-dependent serum factor with protease inhibiting activity
    • DOI 10.1016/0014-5793(78)80132-X
    • Fryklund, L., and, Sievertsson, H., (1978). Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity. FEBS Lett. 87, 55-60. (Pubitemid 8285600)
    • (1978) FEBS Letters , vol.87 , Issue.1 , pp. 55-60
    • Fryklund, L.1    Sievertsson, H.2
  • 36
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • DOI 10.1089/104454902753759717
    • Altruda, F., and, Tolosano, E., 2002. Hemopexin: structure, function, and regulation. DNA Cell Biol. 21, 297-306. (Pubitemid 34594543)
    • (2002) DNA and Cell Biology , vol.21 , Issue.4 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 37
    • 33947654354 scopus 로고    scopus 로고
    • Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins
    • DOI 10.1189/jlb.1006629
    • Piccard, H., Van den Steen, P. E., and, Opdenakker, G., (2007) Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J. Leukoc. Biol. 81, 870-892. (Pubitemid 46495636)
    • (2007) Journal of Leukocyte Biology , vol.81 , Issue.4 , pp. 870-892
    • Piccard, H.1    Van Den Steen, P.E.2    Opdenakker, G.3
  • 38
    • 0036141827 scopus 로고    scopus 로고
    • Molecular interactions and functional interference between vitronectin and transforming growth factor-β
    • Schoppet, M., Chavakis, T., Al-Fakhri, N., Kanse, S. M., and, Preissner, K. T., (2002). Molecular interactions and functional interference between vitronectin and transforming growth factor-beta. Lab. Invest. 82, 37-46. (Pubitemid 34072644)
    • (2002) Laboratory Investigation , vol.82 , Issue.1 , pp. 37-46
    • Schoppet, M.1    Chavakis, T.2    Al-Fakhri, N.3    Kanse, S.M.4    Preissner, K.T.5
  • 39
    • 0037661129 scopus 로고    scopus 로고
    • Structural and functional evidence for the interaction of insulin-like growth factors (IGFs) and IGF binding proteins with vitronectin
    • DOI 10.1210/en.2002-221086
    • Kricker, J. A., Towne, C. L., Firth, S. M., Herington, A. C., and, Upton, Z., (2003) Structural and functional evidence for the interaction of insulin-like growth factors (IGFs) and IGF binding proteins with vitronectin. Endocrinology 144, 2807-2815. (Pubitemid 36819880)
    • (2003) Endocrinology , vol.144 , Issue.7 , pp. 2807-2815
    • Kricker, J.A.1    Towne, C.L.2    Firth, S.M.3    Herington, A.C.4    Upton, Z.5
  • 40
    • 0036141045 scopus 로고    scopus 로고
    • Vitronectin binding to IGF binding protein-5 (IGFBP-5) alters IGFBP-5 modulation of IGF-I actions
    • DOI 10.1210/en.143.1.30
    • Nam, T., Moralez, A., and, Clemmons, D., (2002) Vitronectin binding to IGF binding protein-5 (IGFBP-5) alters IGFBP-5 modulation of IGF-I actions. Endocrinology 143, 30-36. (Pubitemid 34056400)
    • (2002) Endocrinology , vol.143 , Issue.1 , pp. 30-36
    • Taek, N.A.M.1    Moralez, A.2    Clemmons, D.3
  • 41
    • 0033279285 scopus 로고    scopus 로고
    • Identification of vitronectin as a novel insulin-like growth factor-II binding protein
    • DOI 10.1210/en.140.6.2928
    • Upton, Z., Webb, H., Hale, K., Yandell, C. A., McMurtry, J. P., et al. (1999) Identification of vitronectin as a novel insulin-like growth factor-II binding protein. Endocrinology 140, 2928-2931. (Pubitemid 32245176)
    • (1999) Endocrinology , vol.140 , Issue.6 , pp. 2928-2931
    • Upton, Z.1    Webb, H.2    Hale, K.3    Yandell, C.A.4    McMurtry, J.P.5    Francis, G.L.6    Ballard, F.J.7
  • 43
    • 25444495268 scopus 로고    scopus 로고
    • Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells
    • Rahman, S., Patel, Y., Murray, J., Patel, K. V., Sumathipala, R., et al. (2005). Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells. Biomed. Chromatogr. Cell Biol. 6, 8.
    • (2005) Biomed. Chromatogr. Cell Biol. , vol.6 , pp. 8
    • Rahman, S.1    Patel, Y.2    Murray, J.3    Patel, K.V.4    Sumathipala, R.5
  • 44
    • 0024433525 scopus 로고
    • A novel β-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for β-endorphin upon interaction with heparin or surfaces
    • Hildebrand, A., Preissner, K. T., Müller-Berghaus, G., and, Teschemacher, H., (1989) A novel beta-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces. J. Biol. Chem. 264, 15429-15434. (Pubitemid 19242915)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.26 , pp. 15429-15434
    • Hildebrand, A.1    Preissner, K.T.2    Muller-Berghaus, G.3    Teschemacher, H.4
  • 45
    • 0024495948 scopus 로고
    • Regulation of cell adhesion receptors by transforming growth factor-β. Regulation of vitronectin receptor and LFA-1
    • Ignotz, R. A., Heino, J., and, Massague, J., (1989) Regulation of cell adhesion receptors by transforming growth factor-beta. Regulation of vitronectin receptor and LFA-1. J. Biol. Chem. 264, 389-392. (Pubitemid 19027616)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.1 , pp. 389-392
    • Ignotz, R.A.1    Heino, J.2    Massague, J.3
  • 46
    • 0033959532 scopus 로고    scopus 로고
    • Sonic hedgehog synergizes with the extracellular matrix protein Vitronectin to induce spinal motor neuron differentiation
    • Pons, S., and, Marti, E., (2000) Sonic hedgehog synergizes with the extracellular matrix protein vitronectin to induce spinal motor neuron differentiation. Development 127, 333-342. (Pubitemid 30087969)
    • (2000) Development , vol.127 , Issue.2 , pp. 333-342
    • Pons, S.1    Marti, E.2
  • 47
    • 0025911764 scopus 로고
    • Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1
    • Chain, D., Kreizman, T., Shapira, H., and, Shaltiel, S., (1991) Plasmin cleavage of vitronectin. Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1. FEBS Lett. 285, 251-256.
    • (1991) FEBS Lett. , vol.285 , pp. 251-256
    • Chain, D.1    Kreizman, T.2    Shapira, H.3    Shaltiel, S.4
  • 48
    • 0029931231 scopus 로고    scopus 로고
    • Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin
    • Deng, G., Royle, G., Wang, S., Crain, K., and, Loskutoff, D. J., (1996) Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin. J. Biol. Chem. 271, 12716-12723.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12716-12723
    • Deng, G.1    Royle, G.2    Wang, S.3    Crain, K.4    Loskutoff, D.J.5
  • 49
    • 0031983123 scopus 로고    scopus 로고
    • Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells
    • DOI 10.1074/jbc.273.1.143
    • Bafetti, L. M., Young, T. N., Itoh, Y., and, Stack, M. S., (1998) Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells. J. Biol. Chem. 273, 143-149. (Pubitemid 28042187)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.1 , pp. 143-149
    • Bafetti, L.M.1    Young, T.N.2    Itoh, Y.3    Stack, M.S.4
  • 50
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., et al. (1995) Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 270, 6691-6697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5
  • 51
    • 0035875151 scopus 로고    scopus 로고
    • Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin
    • DOI 10.1042/0264-6021:3560705
    • Marchenko, G. N., Ratnikov, B. I., Rozanov, D. V., Godzik, A., Deryugina, E. I., et al. (2001) Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin. Biochem. J. 356, 705-718. (Pubitemid 32588442)
    • (2001) Biochemical Journal , vol.356 , Issue.3 , pp. 705-718
    • Marchenko, G.N.1    Ratnikov, B.I.2    Rozanov, D.V.3    Godzik, A.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 52
    • 9244251607 scopus 로고    scopus 로고
    • Human kallikrein 6 degrades extracellular matrix proteins and may enhance the metastatic potential of tumour cells
    • DOI 10.1159/000081102
    • Ghosh, M. C., Grass, L., Soosaipillai, A., Sotiropoulou, G., and, Diamandis, E. P., (2004) Human kallikrein 6 degrades extracellular matrix proteins and may enhance the metastatic potential of tumour cells. Tumour Biol. 25, 193-199. (Pubitemid 39551746)
    • (2004) Tumor Biology , vol.25 , Issue.4 , pp. 193-199
    • Ghosh, M.C.1    Grass, L.2    Soosaipillai, A.3    Sotiropoulou, G.4    Diamandis, E.P.5
  • 53
    • 0031038474 scopus 로고    scopus 로고
    • Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin
    • Gechtman, Z., and, Shaltiel, S., (1997) Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. Eur. J. Biochem. 243, 493-501. (Pubitemid 27060708)
    • (1997) European Journal of Biochemistry , vol.243 , Issue.1-2 , pp. 493-501
    • Gechtman, Z.1    Shaltiel, S.2
  • 54
    • 0026769440 scopus 로고
    • Beta 1 and beta 3 integrins have different roles in the adhesion and migration of vascular smooth muscle cells on extracellular matrix
    • Clyman, R. I., Mauray, F., and, Kramer, R. H., (1992) Beta 1 and beta 3 integrins have different roles in the adhesion and migration of vascular smooth muscle cells on extracellular matrix. Exp. Cell Res. 200, 272-284.
    • (1992) Exp. Cell Res. , vol.200 , pp. 272-284
    • Clyman, R.I.1    Mauray, F.2    Kramer, R.H.3
  • 55
    • 0028173629 scopus 로고
    • Role of the integrin alpha v beta 6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor
    • Weinacker, A., Chen, A., Agrez, M., Cone, R. I., Nishimura, S., et al. (1994) Role of the integrin alpha v beta 6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor. J. Biol. Chem. 269, 6940-6948.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6940-6948
    • Weinacker, A.1    Chen, A.2    Agrez, M.3    Cone, R.I.4    Nishimura, S.5
  • 57
    • 0028981367 scopus 로고
    • The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp, L. M., Hatch, N., Ramos, D. M., Klimanskaya, I. V., Sheppard, D., et al. (1995) The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. J. Biol. Chem. 270, 23196-23202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5
  • 58
    • 0029920554 scopus 로고    scopus 로고
    • Limited plasmin proteolysis of vitronectin. Characterization of the adhesion protein as morpho-regulatory and angiostatin-binding factor
    • Kost, C., Benner, K., Stockmann, A., Linder, D., and, Preissner, K. T., (1996) Limited plasmin proteolysis of vitronectin. Characterization of the adhesion protein as morpho-regulatory and angiostatin-binding factor. Eur. J. Biochem. 236, 682-688.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 682-688
    • Kost, C.1    Benner, K.2    Stockmann, A.3    Linder, D.4    Preissner, K.T.5
  • 59
    • 0034661540 scopus 로고    scopus 로고
    • Different mechanisms define the antiadhesive function of high molecular weight kininogen in integrin- and urokinase receptor-dependent interactions
    • Chavakis, T., Kanse, S. M., Lupu, F., Hammes, H. P., Muller-Esterl, W., et al. (2000) Different mechanisms define the antiadhesive function of high molecular weight kininogen in integrin- and urokinase receptor-dependent interactions. Blood 96, 514-522. (Pubitemid 30463370)
    • (2000) Blood , vol.96 , Issue.2 , pp. 514-522
    • Chavakis, T.1    Kanse, S.M.2    Lupu, F.3    Hammes, H.-P.4    Muller-Esterl, W.5    Pixley, R.A.6    Colman, R.W.7    Preissner, K.T.8
  • 60
    • 0037436320 scopus 로고    scopus 로고
    • Amphiphysin1 inhibits vitronectin-mediated cell adhesion, spreading, and migration in vitro
    • DOI 10.1016/S0006-291X(03)00040-8
    • Otsuka, A., Hirose, K., Kilimann, M. W., and, Kamata, T., (2003). Amphiphysin1 inhibits vitronectin-mediated cell adhesion, spreading, and migration in vitro. Biochem. Biophys. Res. Commun. 301, 769-775. (Pubitemid 36268956)
    • (2003) Biochemical and Biophysical Research Communications , vol.301 , Issue.3 , pp. 769-775
    • Otsuka, A.1    Hirose, K.2    Kilimann, M.W.3    Kamata, T.4
  • 61
  • 62
    • 0022393939 scopus 로고
    • Association of thrombin-antithrombin III complex with vitronectin in serum
    • Ill, C. R., and, Ruoslahti, E., (1985) Association of thrombin-antithrombin III complex with vitronectin in serum. J. Biol. Chem. 260, 15610-15615. (Pubitemid 16173185)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.29 , pp. 15610-15615
    • Ill, C.R.1    Ruoslahti, E.2
  • 63
    • 0025972869 scopus 로고
    • Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which 'buries' Ser-378, its site of phosphorylation by protein kinase A
    • Chain, D., Korc-Grodzicki, B., Kreizman, T., and, Shaltiel, S., (1991) Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which 'buries' Ser-378, its site of phosphorylation by protein kinase A. Biochem. J. 274, 387-394.
    • (1991) Biochem. J. , vol.274 , pp. 387-394
    • Chain, D.1    Korc-Grodzicki, B.2    Kreizman, T.3    Shaltiel, S.4
  • 64
    • 0042733027 scopus 로고    scopus 로고
    • 3 integrin-containing membrane microdomains
    • DOI 10.1074/jbc.M304166200
    • Mueller, S., and, Wimmer, E., (2003) Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomains. J. Biol. Chem. 278, 31251-31260. (Pubitemid 36994642)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31251-31260
    • Mueller, S.1    Wimmer, E.2
  • 65
    • 0035811834 scopus 로고    scopus 로고
    • The poliovirus receptor CD155 mediates cell-to-matrix contacts by specifically binding to vitronectin
    • DOI 10.1006/viro.2001.0943
    • Lange, R., Peng, X., Wimmer, E., Lipp, M., and, Bernhardt, G., (2001). The poliovirus receptor CD155 mediates cell-to-matrix contacts by specifically binding to vitronectin. Virology 285, 218-227. (Pubitemid 32641883)
    • (2001) Virology , vol.285 , Issue.2 , pp. 218-227
    • Lange, R.1    Peng, X.2    Wimmer, E.3    Lipp, M.4    Bernhardt, G.5
  • 68
    • 0030970685 scopus 로고    scopus 로고
    • Differential modulation of cell adhesion by interaction between adhesive and counter-adhesive proteins: Characterization of the binding of vitronectin to osteonectin (BM40, SPARC)
    • Rosenblatt, S., Bassuk, J. A., Alpers, C. E., Sage, E. H., Timpl, R., and, Preissner, K. T., (1997) Differential modulation of cell adhesion by interaction between adhesive and counter-adhesive proteins: characterization of the binding of vitronectin to osteonectin (BM40, SPARC). Biochem. J. 324, 311-319. (Pubitemid 27229398)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 311-319
    • Rosenblatt, S.1    Bassuk, J.A.2    Alpers, C.E.3    Sage, E.H.4    Timpl, R.5    Preissner, K.T.6
  • 69
    • 0346398517 scopus 로고    scopus 로고
    • Vitronectin's basic domain is a syndecan ligand which functions in trans to regulate vitronectin turnover
    • Wilkins-Port, C. E., Sanderson, R. D., Tominna-Sebald, E., and, McKeown-Longo, P. J., (2003) Vitronectin's basic domain is a syndecan ligand which functions in trans to regulate vitronectin turnover. Cell Commun. Adhes. 10, 85-103. (Pubitemid 38035558)
    • (2003) Cell Communication and Adhesion , vol.10 , Issue.2 , pp. 85-103
    • Wilkins-Port, C.E.1    Sanderson, R.D.2    Tominna-Sebald, E.3    McKeown-Longo, P.J.4
  • 70
    • 0028906349 scopus 로고
    • Inhibition of thrombin by antithrombin III and heparin cofactor II in vivo
    • Liu, L., Dewar, L., Song, Y., Kulczycky, M., Blajchman, M. A., et al. (1995) Inhibition of thrombin by antithrombin III and heparin cofactor II in vivo. Thromb. Haemost. 73, 405-412.
    • (1995) Thromb. Haemost. , vol.73 , pp. 405-412
    • Liu, L.1    Dewar, L.2    Song, Y.3    Kulczycky, M.4    Blajchman, M.A.5
  • 71
    • 72449210453 scopus 로고    scopus 로고
    • Syndecans as receptors and organizers of the extracellular matrix
    • Xian, X., Gopal, S., and, Couchman, J. R., (2010) Syndecans as receptors and organizers of the extracellular matrix. Cell Tissue Res. 339, 31-46.
    • (2010) Cell Tissue Res. , vol.339 , pp. 31-46
    • Xian, X.1    Gopal, S.2    Couchman, J.R.3
  • 72
    • 0029925079 scopus 로고    scopus 로고
    • Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization
    • DOI 10.1038/nm0596-529
    • Hammes, H.-P., Brownlee, M., Jonczyk, A., Sutter, A., and, Preissner, K. T., (1996) Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization. Nat. Med. 2, 529-533. (Pubitemid 26151516)
    • (1996) Nature Medicine , vol.2 , Issue.5 , pp. 529-533
    • Hammes, H.-P.1    Brownlee, M.2    Jonzcyk, A.3    Sutter, A.4    Preissner, K.T.5
  • 73
    • 0032770311 scopus 로고    scopus 로고
    • Regulation of the heparan sulfate proteoglycan, perlecan, by injury and interleukin-1α
    • DOI 10.1046/j.1471-4159.1999.0730812.x
    • García de Yébenes, E., Ho, A., Damani, T., Fillit, H., and, Blum, M., (1999) Regulation of the heparan sulfate proteoglycan, perlecan, by injury and interleukin-1alpha. J. Neurochem. 73, 812-820. (Pubitemid 29339857)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.2 , pp. 812-820
    • Garcia De Yebenes, E.1    Ho, A.2    Damani, T.3    Fillit, H.4    Blum, M.5
  • 74
    • 0034737470 scopus 로고    scopus 로고
    • Syndecan-2 is involved in the mitogenic activity and signaling of granulocyte-macrophage colony-stimulating factor in osteoblasts
    • DOI 10.1074/jbc.275.13.9178
    • Modrowski, D., Baslé, D., Lomri, A., and, Marie, P. J., (2000) Syndecan-2 Is Involved in the mitogenic activity and signaling of granulocyte-macrophage colony-stimulating factor in osteoblasts. J. Biol. Chem. 275, 9178-9185. (Pubitemid 30185134)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9178-9185
    • Modrowski, D.1    Basle, M.2    Lomri, A.3    Marie, P.J.4
  • 76
    • 0025340173 scopus 로고
    • Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin
    • Smith, J. W., Vestal, D. J., Irwin, S. V., Burke, T. A., and, Cheresh, D. A., (1990) Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin. J. Biol. Chem. 265, 11008-110013.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11008-110013
    • Smith, J.W.1    Vestal, D.J.2    Irwin, S.V.3    Burke, T.A.4    Cheresh, D.A.5
  • 77
  • 78
    • 0038706557 scopus 로고    scopus 로고
    • A steady-state competition model describes the modulating effects of thrombomodulin on thrombin inhibition by plasminogen activator inhibitor-1 in the absence and presence of vitronectin
    • DOI 10.1046/j.1432-1033.2003.03552.x
    • Dekker, R. J., Pannekoek, H., and, Horrevoets, A. J., (2003) A steady-state competition model describes the modulating effects of thrombomodulin on thrombin inhibition by plasminogen activator inhibitor-1 in the absence and presence of vitronectin. Eur. J. Biochem. 270, 1942-1951. (Pubitemid 36560815)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.9 , pp. 1942-1951
    • Dekker, R.J.1    Pannekoek, H.2    Horrevoets, A.J.G.3
  • 79
    • 0037454744 scopus 로고    scopus 로고
    • Galectin 1 inhibits incorporation of vitronectin and chondroitin sulfate B into the extracellular matrix of human vascular smooth muscle cells
    • DOI 10.1016/S0304-4165(02)00447-6
    • Moiseeva, E. P., Williams, B., and, Samani, N. J., (2003) Galectin 1 inhibits incorporation of vitronectin and chondroitin sulfate B into the extracellular matrix of human vascular smooth muscle cells. Biochim. Biophys. Acta 1619, 125-132. (Pubitemid 36078348)
    • (2003) Biochimica et Biophysica Acta - General Subjects , vol.1619 , Issue.2 , pp. 125-132
    • Moiseeva, E.P.1    Williams, B.2    Samani, N.J.3
  • 80
  • 81
    • 0029953975 scopus 로고    scopus 로고
    • Two functionally distinct pools of vitronectin (Vn) in the blood circulation: Identification of a heparin-binding competent population of Vn within platelet α-granules
    • Seiffert, D., and, Schleef, R. R., (1996) Two functionally distinct pools of vitronectin (Vn) in the blood circulation: identification of a heparin-binding competent population of Vn within platelet alpha-granules. Blood 88, 552-560. (Pubitemid 26240387)
    • (1996) Blood , vol.88 , Issue.2 , pp. 552-560
    • Seiffert, D.1    Schleef, R.R.2
  • 82
    • 0009448606 scopus 로고    scopus 로고
    • Vitronectin and substitution of a β-strand 5A lysine residue potentiate activity-neutralization of PA inhibitor-1 by monoclonal antibodies against α-helix F
    • Schousboe, S. L., Egelund, R., Kirkegaard, T., Preissner, K. T., Rodenburg, K. W., et al. (2000) Vitronectin and substitution of a beta-strand 5A lysine residue potentiate activity-neutralization of PA inhibitor-1 by monoclonal antibodies against alpha-helix F. Thromb. Haemost. 83, 742-751. (Pubitemid 30248525)
    • (2000) Thrombosis and Haemostasis , vol.83 , Issue.5 , pp. 742-751
    • Schousboe, S.L.1    Egelund, R.2    Kirkegaard, T.3    Preissner, K.T.4    Rodenburg, K.W.5    Andreasen, P.A.6
  • 83
    • 0030853494 scopus 로고    scopus 로고
    • The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: Evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies
    • Gechtman, Z., Belleli, A., Lechpammer, S., and, Shaltiel, S., (1997) The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies. Biochem. J. 325, 339-349.
    • (1997) Biochem. J. , vol.325 , pp. 339-349
    • Gechtman, Z.1    Belleli, A.2    Lechpammer, S.3    Shaltiel, S.4
  • 84
    • 0033621351 scopus 로고    scopus 로고
    • Vitronectin interaction with glycosaminoglycans. Kinetics, structural determinants, and role in binding to endothelial cells
    • DOI 10.1074/jbc.274.53.37611
    • Francois, P. P., Preissner, K. T., Herrmann, M., Haugland, R. P., Vaudaux, P., et al. (1999). Vitronectin interaction with glycosaminoglycans. Kinetics, structural determinants, and role in binding to endothelial cells. J. Biol. Chem. 274, 37611-37619. (Pubitemid 30026817)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 37611-37619
    • Francois, P.P.1    Preissner, K.T.2    Herrmann, M.3    Haugland, R.P.4    Vaudaux, P.5    Lew, D.L.6    Krause, K.-H.7
  • 85
    • 0025347305 scopus 로고
    • Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties
    • Ehrlich, H. J., Gebbink, R. K., Keijer, J., Linders, M., Preissner, K. T., et al. (1990) Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties. J. Biol. Chem. 265, 13029-13035.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13029-13035
    • Ehrlich, H.J.1    Gebbink, R.K.2    Keijer, J.3    Linders, M.4    Preissner, K.T.5
  • 86
    • 0033559292 scopus 로고    scopus 로고
    • Vitronectin inhibits the thrombotic response to arterial injury in mice
    • Fay, W. P., Parker, A. C., Ansari, M. N., Zheng, X., and, Ginsburg, D., (1999) Vitronectin inhibits the thrombotic response to arterial injury in mice. Blood 93, 1825-1830. (Pubitemid 29128482)
    • (1999) Blood , vol.93 , Issue.6 , pp. 1825-1830
    • Fay, W.P.1    Parker, A.C.2    Ansari, M.N.3    Zheng, X.4    Ginsburg, D.5
  • 87
    • 84919885398 scopus 로고    scopus 로고
    • Molecular and cellular basis of fibrinolysis
    • 5. (Hoffman, R. Benz, E. J. J. Shattil, S. J. and Furie, B. eds.). Churchill Livingstone/Elsevier, Philadelphia, PA
    • Lijnen, H. R., and, Collen, D., (2008) Molecular and cellular basis of fibrinolysis. In Hematology: Basic Principles and Practice, Vol. 5. (, Hoffman, R., Benz, E. J. J., Shattil, S. J., and, Furie, B., eds.). Churchill Livingstone/Elsevier, Philadelphia, PA.
    • (2008) In Hematology: Basic Principles and Practice
    • Lijnen, H.R.1    Collen, D.2
  • 89
    • 0003596839 scopus 로고    scopus 로고
    • Life at the Cell and Below-Cell Level
    • Pacific Press, New York, ISBN 0-9707322-0-1
    • Ling, G. N., (2001) Life at the Cell and Below-Cell Level. The Hidden History of a Fundamental Revolution in Biology. pp. 74-108, Pacific Press, New York, ISBN 0-9707322-0-1.
    • (2001) The Hidden History of A Fundamental Revolution in Biology , pp. 74-108
    • Ling, G.N.1
  • 90
    • 0033839433 scopus 로고    scopus 로고
    • The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma
    • Uchibori-Iwaki, H., Yoneda, A., Oda-Tamai, S., Kato, S., Akamatsu, N., et al. (2000) The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma. Glycobiology 10, 865-874.
    • (2000) Glycobiology , vol.10 , pp. 865-874
    • Uchibori-Iwaki, H.1    Yoneda, A.2    Oda-Tamai, S.3    Kato, S.4    Akamatsu, N.5
  • 91
    • 34447326970 scopus 로고    scopus 로고
    • Changes in glycosylation of vitronectin modulate multimerization and collagen binding during liver regeneration
    • DOI 10.1093/glycob/cwm031
    • Sano, K., Asanuma-Date, K., Arisaka, F., Hattori, S., and, Ogawa, H., (2007) Changes in glycosylation of vitronectin modulate multimerization and collagen binding during liver regeneration. Glycobiology 17, 784-794. (Pubitemid 47050665)
    • (2007) Glycobiology , vol.17 , Issue.7 , pp. 784-794
    • Sano, K.1    Asanuma-Date, K.2    Arisaka, F.3    Hattori, S.4    Ogawa, H.5
  • 92
    • 0031022574 scopus 로고    scopus 로고
    • Effect of extracellular matrix glycation on endothelial cell adhesion and spreading: Involvement of vitronectin
    • Bobbink, I. W.G., de Boer, H. C., Tekelenburg, W. L. H., Banga, J.-D., and, de Groot, P. G., (1997) Effect of extracellular matrix glycation on endothelial cell adhesion and spreading. Diabetes 46, 87-93. (Pubitemid 27009955)
    • (1997) Diabetes , vol.46 , Issue.1 , pp. 87-93
    • Bobbink, I.W.G.1    De Boer, H.C.2    Tekelenburg, W.L.H.3    Banga, J.-D.4    De Groot, P.G.5
  • 93
    • 84876054126 scopus 로고    scopus 로고
    • Apoptotic cells selectively uptake minor glycoforms of vitronectin from serum
    • Malagolini, N., Catera, M., Osorio, H., Reis, C. A., Chiricolo, M., et al. (2013) Apoptotic cells selectively uptake minor glycoforms of vitronectin from serum. Apoptosis 18, 373-384.
    • (2013) Apoptosis , vol.18 , pp. 373-384
    • Malagolini, N.1    Catera, M.2    Osorio, H.3    Reis, C.A.4    Chiricolo, M.5
  • 94
    • 84861773596 scopus 로고    scopus 로고
    • Vitronectin inhibits neutrophil apoptosis through activation of integrin-associated signaling pathways
    • Bae, H. B., Zmijewski, J. W., Deshane, J. S., Zhi, D., Thompson, L. C., et al. (2012) Vitronectin inhibits neutrophil apoptosis through activation of integrin-associated signaling pathways. Am. J. Respir. Cell Mol. Biol. 46, 790-796.
    • (2012) Am. J. Respir. Cell Mol. Biol. , vol.46 , pp. 790-796
    • Bae, H.B.1    Zmijewski, J.W.2    Deshane, J.S.3    Zhi, D.4    Thompson, L.C.5
  • 95
    • 79961097221 scopus 로고    scopus 로고
    • Vitronectin in vascular context: Facets of a multitalented matricellular protein
    • Preissner, K. T., and, Reuning, U., (2011). Vitronectin in vascular context: facets of a multitalented matricellular protein. Semin. Thromb. Hemost. 37, 408-424.
    • (2011) Semin. Thromb. Hemost. , vol.37 , pp. 408-424
    • Preissner, K.T.1    Reuning, U.2
  • 97
    • 0033121275 scopus 로고    scopus 로고
    • The role of αv integrins during angiogenesis: Insights into potential mechanisms of action and clinical development
    • Eliceiri, B. P., and, Cheresh, D. A., (1999). The role of alphav integrins during angiogenesis: insights into potential mechanisms of action and clinical development. J. Clin. Invest. 103, 1227-1230. (Pubitemid 29218291)
    • (1999) Journal of Clinical Investigation , vol.103 , Issue.9 , pp. 1227-1230
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 98
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding, A. S., and, Hancock, J. F., (2008) Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol. 18, 364-371.
    • (2008) Trends Cell Biol. , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 100
    • 0034130708 scopus 로고    scopus 로고
    • Vitronectin deficiency is associated with increased wound fibrinolysis and decreased microvascular angiogenesis in mice
    • Jang, Y. C., Tsou, R., Gibran, N. S., and, Isik, F. F., (2000). Vitronectin deficiency is associated with increased wound fibrinolysis and decreased microvascular angiogenesis in mice. Surgery 127, 696-704. (Pubitemid 30399062)
    • (2000) Surgery , vol.127 , Issue.6 , pp. 696-704
    • Jang, Y.-C.1    Tsou, R.2    Gibran, N.S.3    Isik, F.F.4
  • 101
    • 84861013031 scopus 로고    scopus 로고
    • Vitronectin increases vascular permeability by promoting VE-cadherin internalization at cell junctions
    • Li, R., Ren, M., Chen, N., Luo, M., Zhang, Z., et al. (2012) Vitronectin increases vascular permeability by promoting VE-cadherin internalization at cell junctions. PLoS One 7, e37195.
    • (2012) PLoS One , vol.7
    • Li, R.1    Ren, M.2    Chen, N.3    Luo, M.4    Zhang, Z.5
  • 102
    • 0022891340 scopus 로고
    • Tumors: Wounds that do not heal: Similarities between tumor stroma generation and wound healing
    • Dvorak, H. F., (1986) Tumors: wounds that do not heal. Similarities between tumor stroma generation and wound healing. N Engl. J. Med. 315, 1650-1659. (Pubitemid 17052899)
    • (1986) New England Journal of Medicine , vol.315 , Issue.26 , pp. 1650-1659
    • Dvorak, H.F.1
  • 103
    • 17844367105 scopus 로고    scopus 로고
    • Alpha(v)beta3 and alpha(v)beta5 integrin expression in glioma periphery
    • discussion, 390
    • Bello, L., Francolini, M., Marthyn, P., Zhang, J., Carroll, R. S., et al. (2001) Alpha(v)beta3 and alpha(v)beta5 integrin expression in glioma periphery. Neurosurgery 49, 380-389; discussion, 390.
    • (2001) Neurosurgery , vol.49 , pp. 380-389
    • Bello, L.1    Francolini, M.2    Marthyn, P.3    Zhang, J.4    Carroll, R.S.5
  • 104
    • 0037357315 scopus 로고    scopus 로고
    • Adhesion and migration of extracellular matrix-stimulated breast cancer
    • DOI 10.1016/S0022-4804(03)00004-0
    • Bartsch, J. E., Staren, E. D., and, Appert, H. E., (2003). Adhesion and migration of extracellular matrix-stimulated breast cancer. J. Surg. Res. 110, 287-294. (Pubitemid 36403720)
    • (2003) Journal of Surgical Research , vol.110 , Issue.1 , pp. 287-294
    • Bartsch, J.E.1    Staren, E.D.2    Appert, H.E.3
  • 105
    • 0029686918 scopus 로고    scopus 로고
    • Tumor angiogenesis and the role of vascular cell integrin alphavbeta3
    • Varner, J. A., and, Cheresh, D. A., (1996) Tumor angiogenesis and the role of vascular cell integrin alphavbeta3. Important Adv. Oncol. 69-87.
    • (1996) Important Adv. Oncol. , pp. 69-87
    • Varner, J.A.1    Cheresh, D.A.2
  • 106
    • 33745918670 scopus 로고    scopus 로고
    • Mathematical modelling of dynamic adaptive tumour-induced angiogenesis: Clinical implications and therapeutic targeting strategies
    • DOI 10.1016/j.jtbi.2005.12.022, PII S0022519305005564
    • McDougall, S. R., Anderson, A. R. A., and, Chaplain, M. A. J., (2006). Mathematical modelling of dynamic adaptive tumour-induced angiogenesis: clinical implications and therapeutic targeting strategies. J. Theor. Biol. 241, 564-589. (Pubitemid 44041121)
    • (2006) Journal of Theoretical Biology , vol.241 , Issue.3 , pp. 564-589
    • McDougall, S.R.1    Anderson, A.R.A.2    Chaplain, M.A.J.3
  • 107
    • 0036984640 scopus 로고    scopus 로고
    • Role of angiogenesis in tumour growth and metastasis
    • Folkman, J., (2002) Role of angiogenesis in tumour growth and metastasis. Semin. Oncol. 29, 15-18.
    • (2002) Semin. Oncol. , vol.29 , pp. 15-18
    • Folkman, J.1
  • 109
    • 0028670833 scopus 로고
    • Integrin avb3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • Brooks, P. C., Montgomery, A. M. P., Rosenfeld, M., Reisfeld, R. A., Hu, T., et al. (1994). Integrin avb3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 79, 1157-1164.
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.P.2    Rosenfeld, M.3    Reisfeld, R.A.4    Hu, T.5
  • 111
    • 0037064589 scopus 로고    scopus 로고
    • ECM regulates MT1-MMP localization with β1 or αvβ3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells
    • DOI 10.1083/jcb.200205026
    • Gálvez, B. G., Matías-Román, S., Yáñez-Mõ, M., Sánchez-Madrid, F., Arroyo, A. G., (2002) ECM regulates MT1-MMP localization with beta1 or alphavbeta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells. J. Cell Biol. 159, 509-521. (Pubitemid 35332837)
    • (2002) Journal of Cell Biology , vol.159 , Issue.3 , pp. 509-521
    • Galvez, B.G.1    Matias-Roman, S.2    Yanez-Mo, M.3    Sanchez-Madrid, F.4    Arroyo, A.G.5
  • 112
    • 84855412217 scopus 로고    scopus 로고
    • Concise review: Cancer stem cells and minimal residual disease
    • Guiaur, G., Gerber, J., and, Jones, R. J., (2012) Concise review: cancer stem cells and minimal residual disease. Stem Cells 30, 89-93.
    • (2012) Stem Cells , vol.30 , pp. 89-93
    • Guiaur, G.1    Gerber, J.2    Jones, R.J.3
  • 113
    • 25844459154 scopus 로고    scopus 로고
    • NF-κB: Linking inflammation and immunity to cancer development and progression
    • DOI 10.1038/nri1703
    • Karin, M., and, Greten, F. R., (2005) NF-kB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol. 5, 749-759. (Pubitemid 41400849)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.10 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 114
    • 0021647086 scopus 로고
    • Kinetics of cell spreading in the presence of different concentrations of serum or fibronectin-depleted serum
    • Knox, P., (1984) Kinetics of cell spreading in the presence of different concentrations of serum or fibronectin-depleted serum. J. Cell Sci. 71, 51-59. (Pubitemid 15214576)
    • (1984) Journal of Cell Science , vol.VOL. 71 , pp. 51-59
    • Knox, P.1
  • 115
    • 0025744067 scopus 로고
    • Adhesion and growth of cultured human endothelial cells on perfluorosulphonate: Role of vitronectin and fibronectin in cell attachment
    • Steele, J. G., Johnson, G., Norris, W. D., and, Underwood, P. A., (1991) Adhesion and growth of cultured human endothelial cells on perfluorosulphonate: role of vitronectin and fibronectin in cell attachment. Biomaterials 12, 531-539.
    • (1991) Biomaterials , vol.12 , pp. 531-539
    • Steele, J.G.1    Johnson, G.2    Norris, W.D.3    Underwood, P.A.4
  • 116
    • 0027624239 scopus 로고
    • Polystyrene chemistry affects vitronectin activity: An explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene
    • Steele, J. G., Dalton, B. A., Johnson, G., and, Underwood, P. A., (1993) Polystyrene chemistry affects vitronectin activity: an explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene. J. Biomed. Mater. Res. 27, 927-940. (Pubitemid 23178669)
    • (1993) Journal of Biomedical Materials Research , vol.27 , Issue.7 , pp. 927-940
    • Steele, J.G.1    Dalton, B.A.2    Johnson, G.3    Underwood, P.A.4
  • 117
    • 0021647085 scopus 로고
    • The competitive effects of serum proteins on cell adhesion
    • Curtis, A. S., and, Forrester, J. V., (1984) The competitive effects of serum proteins on cell adhesion. J. Cell Sci. 71, 17-35. (Pubitemid 15214574)
    • (1984) Journal of Cell Science , vol.VOL. 71 , pp. 17-35
    • Curtis, A.S.G.1    Forrester, J.V.2
  • 118
    • 0026898451 scopus 로고
    • Role of serum vitronectin and fibronectin in adhesion of fibroblasts following seeding onto tissue culture polystyrene
    • Steele, J. G., Johnson, G., and, Underwood, P. A., (1992) Role of serum vitronectin and fibronectin in adhesion of fibroblasts following seeding onto tissue culture polystyrene. J. Biomed. Mater. Res. 26, 861-884.
    • (1992) J. Biomed. Mater. Res. , vol.26 , pp. 861-884
    • Steele, J.G.1    Johnson, G.2    Underwood, P.A.3
  • 119
    • 0024308771 scopus 로고
    • Identification of vitronectin as a major plasma protein adsorbed on polymer surfaces of different copolymer composition
    • Bale, M. D., Wohlfahrt, L. A., Mosher, D. F., Tomasini, B., and, Sutton, R. C., (1989) Identification of vitronectin as a major plasma protein adsorbed on polymer surfaces of different copolymer composition. Blood 74, 2698-2706. (Pubitemid 20007795)
    • (1989) Blood , vol.74 , Issue.8 , pp. 2698-2706
    • Bale, M.D.1    Wohlfahrt, L.A.2    Mosher, D.F.3    Tomasini, B.4    Sutton, R.C.5
  • 120
    • 69349091811 scopus 로고
    • Residence time effects on monoclonal antibody binding to adsorbed fibrinogen
    • Horbett, T. A., and, Lew, K. R., (1994) Residence time effects on monoclonal antibody binding to adsorbed fibrinogen. J. Biomater. Sci. Polym. Ed. 6, 15-33.
    • (1994) J. Biomater. Sci. Polym. Ed. , vol.6 , pp. 15-33
    • Horbett, T.A.1    Lew, K.R.2
  • 121
    • 0024440425 scopus 로고
    • A comparison of the biological activities of the cell-adhesive proteins vitronectin and fibronectin
    • Underwood, P. A., and, Bennett, F. A., (1989) A comparison of the biological activities of the cell-adhesive proteins vitronectin and fibronectin. J. Cell Sci. 93, 641-649. (Pubitemid 19222382)
    • (1989) Journal of Cell Science , vol.93 , Issue.4 , pp. 641-649
    • Underwood, P.A.1    Bennett, F.A.2
  • 122
    • 0038237587 scopus 로고    scopus 로고
    • Insulin-like growth factor-II bound to vitronectin enhances MCF-7 breast cancer cell migration
    • DOI 10.1210/en.2002-221138
    • Noble, A., Towne, C., Chopin, L., Leavesley, D., and, Upton, Z., (2003) Insulin-like growth factor-II bound to vitronectin enhances MCF-7 breast cancer cell migration. Endocrinology 144, 2417-2424. (Pubitemid 36629893)
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2417-2424
    • Noble, A.M.1    Towne, C.2    Chopin, L.3    Leavesley, D.4    Upton, Z.5
  • 123
    • 2442486433 scopus 로고    scopus 로고
    • Insulin-like growth factors (IGF) and IGF-binding proteins bound to vitronectin enhance keratinocyte protein synthesis and migration
    • DOI 10.1111/j.0022-202X.2004.22527.x
    • Hyde, C., Hollier, B., Anderson, A., Harkin, D., and, Upton, Z., (2004) Insulin-like growth factors (IGF) and IGF-binding proteins bound to vitronectin enhance keratinocyte protein synthesis and migration. J. Invest. Dermatol. 122, 1198-1206. (Pubitemid 38651095)
    • (2004) Journal of Investigative Dermatology , vol.122 , Issue.5 , pp. 1198-1206
    • Hyde, C.1    Hollier, B.2    Anderson, A.3    Harkin, D.4    Upton, Z.5
  • 124
    • 40849085396 scopus 로고    scopus 로고
    • Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by αv-integrins and the IGF-I receptor
    • DOI 10.1210/en.2007-0740
    • Hollier, B. G., Kricker, J. A., Van Lonkhuyzen, D. R., Leavesley, D. I., and, Upton, Z., (2008) Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by alphav-integrins and the IGF-I receptor. Endocrinology 149, 1075-1090. (Pubitemid 351397938)
    • (2008) Endocrinology , vol.149 , Issue.3 , pp. 1075-1090
    • Hollier, B.G.1    Kricker, J.A.2    Van Lonkhuyzen, D.R.3    Leavesley, D.I.4    Upton, Z.5
  • 125
    • 77957768371 scopus 로고    scopus 로고
    • Mechanistic investigations into interactions between IGF-I and IGFBPs and their impact on facilitating cell migration on vitronectin
    • Kricker, J. A., Hyde, C., Van Lonkhuyzen, D. R., Hollier, B., Shooter, G. K., et al. (2010) Mechanistic investigations into interactions between IGF-I and IGFBPs and their impact on facilitating cell migration on vitronectin. Growth Factors 28, 359-369.
    • (2010) Growth Factors , vol.28 , pp. 359-369
    • Kricker, J.A.1    Hyde, C.2    Van Lonkhuyzen, D.R.3    Hollier, B.4    Shooter, G.K.5
  • 126
    • 79953182314 scopus 로고    scopus 로고
    • Insulin-like growth factor-I: Vitronectin complex-induced changes in gene expression effect breast cell survival and migration
    • Kashyap, A. S., Hollier, B. G., Manton, K. J., Satyamoorthy, K., Leavesley, D. I., et al. (2011) Insulin-like growth factor-I:vitronectin complex-induced changes in gene expression effect breast cell survival and migration. Endocrinology 152, 1388-1401.
    • (2011) Endocrinology , vol.152 , pp. 1388-1401
    • Kashyap, A.S.1    Hollier, B.G.2    Manton, K.J.3    Satyamoorthy, K.4    Leavesley, D.I.5
  • 127
    • 33845190403 scopus 로고    scopus 로고
    • Surfaces and interfacial water: Evidence that hydrophilic surfaces have long-range impact
    • DOI 10.1016/j.cis.2006.07.002, PII S0001868606000972
    • Zheng, J.-M., Chin, W. -C., Khijniak, E., Khijniak, E. Jr., Pollack, G. H., (2006) Surfaces and interfacial water: evidence that hydrophilic surfaces have long-range impact. Adv. Colloid Interface Sci. 127, 19-27. (Pubitemid 44854784)
    • (2006) Advances in Colloid and Interface Science , vol.127 , Issue.1 , pp. 19-27
    • Zheng, J.-m.1    Chin, W.-C.2    Khijniak, E.3    Khijniak Jr., E.4    Pollack, G.H.5
  • 128
    • 0035815743 scopus 로고    scopus 로고
    • The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media
    • DOI 10.1074/jbc.R100005200
    • Minton, A. P., (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276, 10577-10580. (Pubitemid 38089223)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10577-10580
    • Minton, A.P.1
  • 129
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons, K., and, Gerl, M. J., (2010) Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 11, 688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 130
    • 0024391951 scopus 로고
    • Adsorption of vitronectin in human serum onto plastics is augmented by sodium dodecyl sulfate
    • Miyamoto, Y., Izumi, M., Ishizaka, S., and, Hayashi, M., (1989) Adsorption of vitronectin in human serum onto plastics is augmented by sodium dodecyl sulfate. Cell Struct. Funct. 14, 151-162. (Pubitemid 19147943)
    • (1989) Cell Structure and Function , vol.14 , Issue.2 , pp. 151-162
    • Miyamoto, Y.1    Izumi, M.2    Ishizaka, S.3    Hayashi, M.4
  • 131
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: Integrins, signaling and cell survival
    • DOI 10.1242/jcs.00071
    • Stupack, D. G., and, Cheresh, D. A., (2002) Get a ligand, get a life: integrins, signaling and cell survival. J. Cell Sci. 115, 3729-3738. (Pubitemid 35203599)
    • (2002) Journal of Cell Science , vol.115 , Issue.19 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 132
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram, C. L., and, Lowell, C. A., (2009) The ins and outs of leukocyte integrin signaling. Annu. Rev. Immunol. 27, 339-362.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 133
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger, D. S., and, Calderwood, D. A., (2009) Integrin signalling at a glance. J. Cell Sci. 122, 159-163.
    • (2009) J. Cell Sci. , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 134
    • 0034142057 scopus 로고    scopus 로고
    • 3 regulates cell adhesion and migration to bone sialoprotein
    • DOI 10.1006/excr.1999.4765
    • Byzova, T. V., Kim, W., Midura, R. J., and, Plow, E. F., (2000) Activation of integrin alpha(V)beta(3) regulates cell adhesion and migration to bone sialoprotein. Exp. Cell Res. 254, 299-308. (Pubitemid 30080586)
    • (2000) Experimental Cell Research , vol.254 , Issue.2 , pp. 299-308
    • Byzova, T.V.1    Kim, W.2    Midura, R.J.3    Plow, E.F.4
  • 135
    • 0035824920 scopus 로고    scopus 로고
    • Integrin and growth factor receptor crosstalk
    • Eliceiri, B.P., (2001) Integrin and growth factor receptor crosstalk. Circ. Res. 89, 1104-1110. (Pubitemid 34627867)
    • (2001) Circulation Research , vol.89 , Issue.12 , pp. 1104-1110
    • Eliceiri, B.P.1
  • 136
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • DOI 10.1038/ncb0402-e65
    • Schwartz, M. A., and, Ginsberg, M. H., (2002) Networks and crosstalk: integrin signalling spreads. Nat. Cell Biol. 4, E65-E68. (Pubitemid 34308840)
    • (2002) Nature Cell Biology , vol.4 , Issue.4
    • Schwartz, M.A.1    Ginsberg, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.