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Volumn 241, Issue 2, 1996, Pages 557-563

Structural and functional characterization of vitronectin-derived RGD-containing peptides from human hemofiltrate

Author keywords

Hemofiltrate; Integrin; Plasminogen activator inhibitor 1; Somatomedin B peptide; Vitronectin

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; INTEGRIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; VITRONECTIN;

EID: 0029858628     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00557.x     Document Type: Article
Times cited : (23)

References (37)
  • 2
    • 0019527376 scopus 로고
    • The structural basis for anuphylutoxin and chemotatic functions of C3a, C4a and C5a
    • Hugli, T. E. (1981) The structural basis for anuphylutoxin and chemotatic functions of C3a, C4a and C5a, CRC. Crit. Rev. Immunol. 2, 321-351.
    • (1981) CRC. Crit. Rev. Immunol. , vol.2 , pp. 321-351
    • Hugli, T.E.1
  • 8
    • 0030597577 scopus 로고    scopus 로고
    • Systematic isolation of circulating human peptides: The concept of peptide trapping
    • Schulz-Knappe, P., Raida, M., Meyer, M. & Forssmann, W. G. (1996) Systematic isolation of circulating human peptides: the concept of peptide trapping, Eur. J. Med. Res. 1, 223-236.
    • (1996) Eur. J. Med. Res. , vol.1 , pp. 223-236
    • Schulz-Knappe, P.1    Raida, M.2    Meyer, M.3    Forssmann, W.G.4
  • 9
    • 0025812551 scopus 로고
    • Structure of vitronectin and its biological role in haemostasis
    • Preissner, K. T. & Jenne, D. (1991) Structure of vitronectin and its biological role in haemostasis, Thromb. Haemostasis 66, 123-130.
    • (1991) Thromb. Haemostasis , vol.66 , pp. 123-130
    • Preissner, K.T.1    Jenne, D.2
  • 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
  • 12
    • 0025774971 scopus 로고
    • Evidence that type-1 plasminogen activator inhibitor binds to the somatomedin-B domain of vitronectin
    • Seiffert, D. & 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.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2824-2830
    • Seiffert, D.1    Loskutoff, D.J.2
  • 13
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor I binding protein from human plasma. Identification as a nultimeric form of S protein (vitronectin)
    • Declerck, P. J., De Mol, M., Alessi, M.-C., Baudner, S., Paques, E.-P., Preissner, K. T., Muller-Berghaus, G. & Collen, D. (1988) Purification and characterization of a plasminogen activator inhibitor I binding protein from human plasma. Identification as a nultimeric 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    Preissner, K.T.6    Muller-Berghaus, G.7    Collen, D.8
  • 14
    • 0024561807 scopus 로고
    • Binding of type 1 plasminogen activator inhibitor to the extracellular matrix of cultured bovine endothelial cells
    • Mimuro, J. & Loskutoff, D. J. (1989) Binding of type 1 plasminogen activator inhibitor to the extracellular matrix of cultured bovine endothelial cells. J. Biol. Chem. 264, 5058-5063.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5058-5063
    • Mimuro, J.1    Loskutoff, D.J.2
  • 15
    • 0025134891 scopus 로고
    • Structural requirements for the extracellular interaction of plasminogen activator inhibitor I with endothelial cell matrix-associated vitronectin
    • Preissner, K. T., Grulich-Henn, J., Ehrlich, H. J., Declerck, P., Justus, C., Collen, D., Pannekoek, H. & Müller-Berghaus, G. (1990) Structural requirements for the extracellular interaction of plasminogen activator inhibitor I with endothelial cell matrix-associated vitronectin, J. Biol. Chem. 265, 18490-18498.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18490-18498
    • Preissner, K.T.1    Grulich-Henn, J.2    Ehrlich, H.J.3    Declerck, P.4    Justus, C.5    Collen, D.6    Pannekoek, H.7    Müller-Berghaus, G.8
  • 16
    • 0023840967 scopus 로고
    • Measurement of plasminogen activator inhibitor 1 in biologic fluids with a murine monoclonal antibody-based enzyme-linked immunosorbent assay
    • Declerck, P. J., Alessi, M.-C., Verstreken, M., Kruithof, E. K. O., Juhan-Vague, I. & Collen, D. (1988) Measurement of plasminogen activator inhibitor 1 in biologic fluids with a murine monoclonal antibody-based enzyme-linked immunosorbent assay, Blood 71, 220-225.
    • (1988) Blood , vol.71 , pp. 220-225
    • Declerck, P.J.1    Alessi, M.-C.2    Verstreken, M.3    Kruithof, E.K.O.4    Juhan-Vague, I.5    Collen, D.6
  • 17
    • 0022289172 scopus 로고
    • Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion
    • Jenne, D. & Stanley, K. K. (1985) Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion. EMBO J. 4, 3153-3157.
    • (1985) EMBO J. , vol.4 , pp. 3153-3157
    • Jenne, D.1    Stanley, K.K.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the protein-dye binding. Anal. Biochem. 72, 234-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 234-254
    • Bradford, M.M.1
  • 19
    • 0027965876 scopus 로고
    • Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Escherichia coli
    • Sancho, E., Tonge, D. W., Hockney, R. C. & Booth, N. A. (1994) Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Escherichia coli, Eur. J. Biochem. 224, 125-134.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 125-134
    • Sancho, E.1    Tonge, D.W.2    Hockney, R.C.3    Booth, N.A.4
  • 20
    • 0026664184 scopus 로고
    • Mapping of binding sites for heparin, plasminogen-activator inhibitor-1 and plasminogen to vitronectin's heparin binding region reveals a novel vitronectin-dependent feedback mechanism for the control of plasmin formation
    • Kost, C., Stüber, W., Ehrlich, H., Pannekoek, H. & Preissner, K. T. (1992) Mapping of binding sites for heparin, plasminogen-activator inhibitor-1 and plasminogen to vitronectin's heparin binding region reveals a novel vitronectin-dependent feedback mechanism for the control of plasmin formation, J. Biol. Chem. 267, 12098-12105.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12098-12105
    • Kost, C.1    Stüber, W.2    Ehrlich, H.3    Pannekoek, H.4    Preissner, K.T.5
  • 21
    • 0022004305 scopus 로고
    • Physicochemical characterization of human S-protein and its function in the blood coagulation system
    • Preissner, K. T., Wassmuth, R. & Müller-Berghaus, G. (1985) Physicochemical characterization of human S-protein and its function in the blood coagulation system, Biochem. J. 231, 349-355.
    • (1985) Biochem. J. , vol.231 , pp. 349-355
    • Preissner, K.T.1    Wassmuth, R.2    Müller-Berghaus, G.3
  • 23
    • 0029873910 scopus 로고    scopus 로고
    • The urokinase receptor is a major vitronectin binding protein on endothelial cells
    • Kanse, S. M., Kost, C., Wilhelm, O. G., Andreasen, P. A. & Preissner, K. T. (1996) The urokinase receptor is a major vitronectin binding protein on endothelial cells, Exp. Cell Res. 224, 344-353.
    • (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
  • 24
    • 0016354646 scopus 로고
    • Isolation and characterization of polypeptides from human plasma enhancing the growth of human normal cells in culture
    • Fryklund, L., Uthne, K. & Sievertsson, H. (1974) Isolation and characterization of polypeptides from human plasma enhancing the growth of human normal cells in culture, Biochem. Biophys. Res. Commun. 61, 950-956.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 950-956
    • Fryklund, L.1    Uthne, K.2    Sievertsson, H.3
  • 25
    • 0017880606 scopus 로고
    • Primary structure of somatomedin B. A growth hormone-dependent serum factor with protease inhibiting activity
    • Fryklund, L. & Sievertsson, H. (1978) Primary structure of somatomedin B. A growth hormone-dependent serum factor with protease inhibiting activity, FEBS Lett. 87, 55-60.
    • (1978) FEBS Lett. , vol.87 , pp. 55-60
    • Fryklund, L.1    Sievertsson, H.2
  • 26
    • 0019830475 scopus 로고
    • Somatomedin B: Mitogenic activity derived from contaminant epidermal growth factor
    • Heldin, C.-H., Wasteson, A., Fryklund, L. & Westermark, B. (1981) Somatomedin B: mitogenic activity derived from contaminant epidermal growth factor. Science 213, 1122-1123.
    • (1981) Science , vol.213 , pp. 1122-1123
    • Heldin, C.-H.1    Wasteson, A.2    Fryklund, L.3    Westermark, B.4
  • 28
    • 0028074531 scopus 로고
    • The somatomedin B domain of vitronectin. Structural requirements for the binding and stabilization of active type 1 plasminogen activator inhibitor
    • Seiffert, D., Ciambrone, G., Wagner, N. V., Binder, B. R. & Loskutoff, D. J. (1994) The somatomedin B domain of vitronectin. Structural requirements for the binding and stabilization of active type 1 plasminogen activator inhibitor, J. Biol. Chem. 269, 2659-2666.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2659-2666
    • Seiffert, D.1    Ciambrone, G.2    Wagner, N.V.3    Binder, B.R.4    Loskutoff, D.J.5
  • 29
    • 0016438674 scopus 로고
    • Radioimmunoassay of somatomedin B. Application to clinical and physiologic studies
    • Yalow, R. S., Hall, K. & Luft, R. (1975) Radioimmunoassay of somatomedin B. Application to clinical and physiologic studies, J. Clin. Invest. 55, 127-137.
    • (1975) J. Clin. Invest. , vol.55 , pp. 127-137
    • Yalow, R.S.1    Hall, K.2    Luft, R.3
  • 30
    • 0018973306 scopus 로고
    • Radio-immuno-assayable serum somatomedin B in normal subjects and in patients with acromegaly and pituitary dwarfism: Effects of human growth hormone therapy
    • Wajchenberg, B. L., Liberman, B., Gomes, E. N. D. S. & Pieroni, R. R. (1980) Radio-immuno-assayable serum somatomedin B in normal subjects and in patients with acromegaly and pituitary dwarfism: effects of human growth hormone therapy, Horm. Metab. Res. 12, 516-519.
    • (1980) Horm. Metab. Res. , vol.12 , pp. 516-519
    • Wajchenberg, B.L.1    Liberman, B.2    Gomes, E.N.D.S.3    Pieroni, R.R.4
  • 31
    • 0007767714 scopus 로고
    • Vitronectin and plasmin(ogen) in lesional skin of the bullous pemphigoid: Colocalisation suggests binding interactions
    • (Preissner. K. T., Rosenblatt, S., Kost, C., Wegerhoff, J. & Mosher, D. F., eds) Eisevier, Amsterdam
    • Kramer, M. D., Gissler, H. M., Weidenthaler-Barth, B. & Preissner, K. T. (1993) Vitronectin and plasmin(ogen) in lesional skin of the bullous pemphigoid: colocalisation suggests binding interactions, in Biology of vitronectins and their receptors (Preissner. K. T., Rosenblatt, S., Kost, C., Wegerhoff, J. & Mosher, D. F., eds) pp. 295-301, Eisevier, Amsterdam.
    • (1993) Biology of Vitronectins and Their Receptors , pp. 295-301
    • Kramer, M.D.1    Gissler, H.M.2    Weidenthaler-Barth, B.3    Preissner, K.T.4
  • 32
    • 0028968007 scopus 로고
    • Fibronectin, laminin, vitronectin and their receptors at newly-formed capillaries in proliferative diabetic retinopathy
    • Casaroli Marano, R. P., Preissner, K. T. & Vilaro, S. (1995) Fibronectin, laminin, vitronectin and their receptors at newly-formed capillaries in proliferative diabetic retinopathy, Exp. Eye Res. 60, 5-17.
    • (1995) Exp. Eye Res. , vol.60 , pp. 5-17
    • Casaroli Marano, R.P.1    Preissner, K.T.2    Vilaro, S.3
  • 33
    • 0025833050 scopus 로고
    • Limited proteolysis of vitronectin by plasmin destroys heparin binding activity
    • Sane, D. C., Moser, T. L. & Greenberg, C. S. (1991) Limited proteolysis of vitronectin by plasmin destroys heparin binding activity, Thromb. Haemostasis 66, 310-314.
    • (1991) Thromb. Haemostasis , vol.66 , pp. 310-314
    • Sane, D.C.1    Moser, T.L.2    Greenberg, C.S.3
  • 34
    • 0029920554 scopus 로고    scopus 로고
    • Limited plasmin proteolysis of vitronectin: Characterization of the adhesion protein as morpho-regulatory and angiostutin-binding factor
    • Kost, C., Benner, K., Stockmann, A., Linder, D. & Preissner, K. T. (1996) Limited plasmin proteolysis of vitronectin: characterization of the adhesion protein as morpho-regulatory and angiostutin-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
  • 35
    • 15844372375 scopus 로고    scopus 로고
    • Hydrolysis of platelet vitronectin by calpain
    • Seiffert, D. (1996) Hydrolysis of platelet vitronectin by calpain. J. Biol. Chem. 271, 11170- 11176.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11170-11176
    • Seiffert, D.1
  • 36
    • 0024444124 scopus 로고
    • Identification and partial characterization of platelet vitronectin: Evidence for complex formation with platelet-derived plasminogen-activator inhibitor-1
    • Preissner, K. T., Holzhüter, S., Justus, C. & Müller-Berghaus, G. (1989) Identification and partial characterization of platelet vitronectin: Evidence for complex formation with platelet-derived plasminogen-activator inhibitor-1. Blood 74, 1989-1996.
    • (1989) Blood , vol.74 , pp. 1989-1996
    • Preissner, K.T.1    Holzhüter, S.2    Justus, C.3    Müller-Berghaus, G.4
  • 37
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Wei, Y., Waltz, D. A., Rao, N., Drummond, R. J., Rosenberg, S. & Chapman, H. A. (1994) Identification of the urokinase receptor as an adhesion receptor for vitronectin, J. Biol. Chem. 269, 32380-32388.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6


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