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Volumn 100, Issue 8, 2002, Pages 2832-2838

The von Willebrand factor-reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE; THIOL; THROMBOSPONDIN 1; VON WILLEBRAND FACTOR;

EID: 0037108554     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-03-0770     Document Type: Article
Times cited : (32)

References (39)
  • 1
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler JE. Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem. 1998;67:395-424.
    • (1998) Annu Rev Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 2
    • 0033168347 scopus 로고    scopus 로고
    • Contribution of distinct adhesive interactions to platelet aggregation in flowing blood
    • Ruggeri ZM, Dent JA, Saldivar E. Contribution of distinct adhesive interactions to platelet aggregation in flowing blood. Blood. 1999;94:172-178.
    • (1999) Blood , vol.94 , pp. 172-178
    • Ruggeri, Z.M.1    Dent, J.A.2    Saldivar, E.3
  • 3
    • 0037039439 scopus 로고    scopus 로고
    • Functional self-association of von Willebrand factor during platelet adhesion under flow
    • Savage B, Sixma JJ, Ruggeri ZM. Functional self-association of von Willebrand factor during platelet adhesion under flow. Proc Natl Acad Sci U S A. 2002;99:425-430.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 425-430
    • Savage, B.1    Sixma, J.J.2    Ruggeri, Z.M.3
  • 4
    • 0018123566 scopus 로고
    • Disulfide bonds and the quaternary structure of factor VIII/von Willebrand factor
    • Counts RB, Paskell SL, Elgee SK. Disulfide bonds and the quaternary structure of factor VIII/von Willebrand factor. J Clin Invest. 1978;62:702-709.
    • (1978) J Clin Invest , vol.62 , pp. 702-709
    • Counts, R.B.1    Paskell, S.L.2    Elgee, S.K.3
  • 5
    • 0034682789 scopus 로고    scopus 로고
    • Localization of disulfide bonds in the cysteine knot domain of human von Willebrand factor
    • Katsumi A, Tuley EA, Bodó I, Sadler JE. Localization of disulfide bonds in the cysteine knot domain of human von Willebrand factor. J Biol Chem. 2000;275:25585-25594.
    • (2000) J Biol Chem , vol.275 , pp. 25585-25594
    • Katsumi, A.1    Tuley, E.A.2    Bodó, I.3    Sadler, J.E.4
  • 6
    • 0023149024 scopus 로고
    • Topology and order of formation of interchain disulfide bonds in von Willebrand factor
    • Wagner DD, Lawrence SO, Ohlsson-Wilhelm BM, Fay PJ, Marder VJ. Topology and order of formation of interchain disulfide bonds in von Willebrand factor. Blood. 1987;69:27-32.
    • (1987) Blood , vol.69 , pp. 27-32
    • Wagner, D.D.1    Lawrence, S.O.2    Ohlsson-Wilhelm, B.M.3    Fay, P.J.4    Marder, V.J.5
  • 8
    • 0029907370 scopus 로고    scopus 로고
    • Von Willebrand factor: Molecular size and functional activity
    • Furlan M. von Willebrand factor: molecular size and functional activity. Ann Hematol. 1996;72: 341-348.
    • (1996) Ann Hematol , vol.72 , pp. 341-348
    • Furlan, M.1
  • 9
    • 0022852282 scopus 로고
    • Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation
    • Moake JL, Turner NA, Stathopoulos NA, Nolasco LH, Hellums JD. Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation. J Clin Invest. 1989;78:1456-1461.
    • (1989) J Clin Invest , vol.78 , pp. 1456-1461
    • Moake, J.L.1    Turner, N.A.2    Stathopoulos, N.A.3    Nolasco, L.H.4    Hellums, J.D.5
  • 10
    • 0020428664 scopus 로고
    • Unusually large plasma factor VIII: Von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura
    • Moake JL, Rudy CK, Troll JH, et al. Unusually large plasma factor VIII: von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura. N Engl J Med. 1982;307: 1432-1435.
    • (1982) N Engl J Med , vol.307 , pp. 1432-1435
    • Moake, J.L.1    Rudy, C.K.2    Troll, J.H.3
  • 11
    • 0031002345 scopus 로고    scopus 로고
    • Studies on the pathophysiology of thrombotic thrombocytopenic purpura
    • Moake JL. Studies on the pathophysiology of thrombotic thrombocytopenic purpura. Semin Hematol. 1997;34:83-89.
    • (1997) Semin Hematol , vol.34 , pp. 83-89
    • Moake, J.L.1
  • 12
    • 0033818794 scopus 로고    scopus 로고
    • The functions of thrombospondin-1 and -2
    • Lawler, J. The functions of thrombospondin-1 and -2. Curr Opin Cell Biol. 2000;12:634-640.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 634-640
    • Lawler, J.1
  • 13
    • 0033828950 scopus 로고    scopus 로고
    • Reduction of von Willebrand factor by endothelial cells
    • Xie L, Chesterman CN, Hogg PJ. Reduction of von Willebrand factor by endothelial cells. Thromb Haemost. 2000;84:506-513.
    • (2000) Thromb Haemost , vol.84 , pp. 506-513
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 14
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1
    • Xie L, Chesterman CN, Hogg PJ. Control of von Willebrand factor multimer size by thrombospondin-1. J Exp Med. 2001;193:1341-1349.
    • (2001) J Exp Med , vol.193 , pp. 1341-1349
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 15
    • 0022237879 scopus 로고
    • Localization of thrombospondin in clots formed in situ
    • Murphy-Ullrich JE, Mosher DF. Localization of thrombospondin in clots formed in situ. Blood. 1985;66:1098-1104.
    • (1985) Blood , vol.66 , pp. 1098-1104
    • Murphy-Ullrich, J.E.1    Mosher, D.F.2
  • 16
    • 0030771752 scopus 로고    scopus 로고
    • Interaction of platelet-derived growth factor with thrombospondin 1: Dependence on the disulfide-bond arrangement in thrombospondin 1
    • Hogg PJ, Hotchkiss KA, Jiménez BM, Stathakis P, Chesterman CN. Interaction of platelet-derived growth factor with thrombospondin 1: dependence on the disulfide-bond arrangement in thrombospondin 1. Biochem J. 1997;326:709-716.
    • (1997) Biochem J , vol.326 , pp. 709-716
    • Hogg, P.J.1    Hotchkiss, K.A.2    Jiménez, B.M.3    Stathakis, P.4    Chesterman, C.N.5
  • 17
    • 0035824607 scopus 로고    scopus 로고
    • Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2
    • Misenheimer TM, Hahr AJ, Harms AC, Annis DS, Mosher DF. Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2. J Biol Chem. 2001;276:45882-45887.
    • (2001) J Biol Chem , vol.276 , pp. 45882-45887
    • Misenheimer, T.M.1    Hahr, A.J.2    Harms, A.C.3    Annis, D.S.4    Mosher, D.F.5
  • 18
    • 0034731490 scopus 로고    scopus 로고
    • Physical characterization of the procollagen module of human thrombospondin 1 expressed in insect cells
    • Misenheimer TM, Huwiler KG, Annis DS, Mosher DF. Physical characterization of the procollagen module of human thrombospondin 1 expressed in insect cells. J Biol Chem. 2000;275:40938-40945.
    • (2000) J Biol Chem , vol.275 , pp. 40938-40945
    • Misenheimer, T.M.1    Huwiler, K.G.2    Annis, D.S.3    Mosher, D.F.4
  • 19
    • 0036368536 scopus 로고    scopus 로고
    • Expression of recombinant matrix components using baculoviruses
    • Adams JC, ed. San Diego, CA: Academic Press
    • Mosher DF, Huwiler KG, Misenheimer TM, Annis DS. Expression of recombinant matrix components using baculoviruses. In: Adams JC, ed. Methods in Cell-Matrix Adhesion. San Diego, CA: Academic Press; 2002:69-81.
    • (2002) Methods in Cell-Matrix Adhesion , pp. 69-81
    • Mosher, D.F.1    Huwiler, K.G.2    Misenheimer, T.M.3    Annis, D.S.4
  • 20
    • 0026149117 scopus 로고
    • Development of a simple collagen based ELISA assay aids in the diagnosis of, and permits sensitive discrimination between type I and type II, von Willebrand's disease
    • Favaloro EJ, Grispo L, Exner T, Koutts J. Development of a simple collagen based ELISA assay aids in the diagnosis of, and permits sensitive discrimination between type I and type II, von Willebrand's disease. Blood Coagul Fibrinolysis. 1991;2:285-291.
    • (1991) Blood Coagul Fibrinolysis , vol.2 , pp. 285-291
    • Favaloro, E.J.1    Grispo, L.2    Exner, T.3    Koutts, J.4
  • 21
    • 0018855952 scopus 로고
    • Variant von Willebrand's disease: Characterization of two subtypes by analysis of multimer composition of factor VIII/von Willebrand factor in plasma and platelets
    • Ruggeri ZM, Zimmerman TS. Variant von Willebrand's disease: characterization of two subtypes by analysis of multimer composition of factor VIII/von Willebrand factor in plasma and platelets. J Clin Invest. 1980;65:1318-1325.
    • (1980) J Clin Invest , vol.65 , pp. 1318-1325
    • Ruggeri, Z.M.1    Zimmerman, T.S.2
  • 23
    • 0015895285 scopus 로고
    • Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystine residues
    • Jacobson GR, Schaffer MH, Stark GR, Vanaman TC. Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystine residues. J Biol Chem. 1973;248:6583-6591.
    • (1973) J Biol Chem , vol.248 , pp. 6583-6591
    • Jacobson, G.R.1    Schaffer, M.H.2    Stark, G.R.3    Vanaman, T.C.4
  • 24
    • 0029918575 scopus 로고    scopus 로고
    • A strategy to locate cysteine residues in proteins by specific chemical cleavage followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Wu J, Gage DA, Watson JT. A strategy to locate cysteine residues in proteins by specific chemical cleavage followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Biochem. 1996;235:161-174.
    • (1996) Anal Biochem , vol.235 , pp. 161-174
    • Wu, J.1    Gage, D.A.2    Watson, J.T.3
  • 25
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra- and inter-molecular sulfonamide bonds in S100A8 produced by hypochlorite oxidation
    • Raftery MJ, Yang Z, Valenzuela SM, Geczy CL. Novel intra- and inter-molecular sulfonamide bonds in S100A8 produced by hypochlorite oxidation. J Biol Chem. 2001;276:33393-33401.
    • (2001) J Biol Chem , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 26
    • 0025109879 scopus 로고
    • Free thiols of platelet thrombospondin
    • Speziale MV, Detwiler TC. Free thiols of platelet thrombospondin. J Biol Chem. 1990;265:17859-17867.
    • (1990) J Biol Chem , vol.265 , pp. 17859-17867
    • Speziale, M.V.1    Detwiler, T.C.2
  • 27
    • 0026667093 scopus 로고
    • Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin
    • Sun X, Skorstengaard K, Mosher DF. Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin. J Cell Biol. 1992;118:693-701.
    • (1992) J Cell Biol , vol.118 , pp. 693-701
    • Sun, X.1    Skorstengaard, K.2    Mosher, D.F.3
  • 28
    • 0023035074 scopus 로고
    • The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins
    • Lawler J, Hynes RO. The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J Cell Biol. 1986; 103:1635-1648.
    • (1986) J Cell Biol , vol.103 , pp. 1635-1648
    • Lawler, J.1    Hynes, R.O.2
  • 29
    • 0025816414 scopus 로고
    • A second, expressed thrombospondin gene (Thbs2) exists in the mouse genome
    • Bornstein P, O'Rourke K, Wikstrom K, et al. A second, expressed thrombospondin gene (Thbs2) exists in the mouse genome. J Biol Chem. 1991; 266:12821-12824.
    • (1991) J Biol Chem , vol.266 , pp. 12821-12824
    • Bornstein, P.1    O'Rourke, K.2    Wikstrom, K.3
  • 30
    • 0026606259 scopus 로고
    • Thrombospondin II: Partial cDNA sequence, chromosome location, and expression of a second member of the thrombospondin gene family in humans
    • LaBelI TL, Milewicz DJ, Disteche CM, Byers PH. Thrombospondin II: partial cDNA sequence, chromosome location, and expression of a second member of the thrombospondin gene family in humans. Genomics. 1992;12:421-429.
    • (1992) Genomics , vol.12 , pp. 421-429
    • LaBell, T.L.1    Milewicz, D.J.2    Disteche, C.M.3    Byers, P.H.4
  • 31
    • 0026653809 scopus 로고
    • Thrombospondin 3 (Thbs3), a new member of the thrombospondin gene family
    • Vos HL, Devarayalu S, de Vries Y, Bornstein P. Thrombospondin 3 (Thbs3), a new member of the thrombospondin gene family. J Biol Chem. 1992; 267:12192-12196.
    • (1992) J Biol Chem , vol.267 , pp. 12192-12196
    • Vos, H.L.1    Devarayalu, S.2    De Vries, Y.3    Bornstein, P.4
  • 32
    • 0027393902 scopus 로고
    • Identification and characterization of thrombospondin-4, a new member of the thrombospondin gene family
    • Lawler J, Duquette M, Whittaker CA, Adams JC, McHenry K, DeSimone DW, Identification and characterization of thrombospondin-4, a new member of the thrombospondin gene family. J Cell Biol. 1993;120:1059-1067.
    • (1993) J Cell Biol , vol.120 , pp. 1059-1067
    • Lawler, J.1    Duquette, M.2    Whittaker, C.A.3    Adams, J.C.4    McHenry, K.5    DeSimone, D.W.6
  • 33
    • 0026499722 scopus 로고
    • COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins
    • Oldberg A, Antonsson P, Lindblom K, Heinegard D. COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. J Biol Chem. 1992;267:22346-22350.
    • (1992) J Biol Chem , vol.267 , pp. 22346-22350
    • Oldberg, A.1    Antonsson, P.2    Lindblom, K.3    Heinegard, D.4
  • 34
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams MD, Celniker SE, Holt RA, et al. The genome sequence of Drosophila melanogaster. Science. 2000;287:2185-2195.
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1    Celniker, S.E.2    Holt, R.A.3
  • 35
    • 0035897654 scopus 로고    scopus 로고
    • A thrombospondin homologue in Drosophila melanogastec cDNA and protein structure
    • Adolph KW. A thrombospondin homologue in Drosophila melanogastec cDNA and protein structure. Gene. 2001;269:177-184.
    • (2001) Gene , vol.269 , pp. 177-184
    • Adolph, K.W.1
  • 36
    • 0035178990 scopus 로고    scopus 로고
    • Thrombospondins: Multifunctional regulators of cell interactions
    • Adams JC. Thrombospondins: multifunctional regulators of cell interactions. Annu Rev Cell Dev Biol. 2001;17:25-51.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 25-51
    • Adams, J.C.1
  • 37
    • 0031833609 scopus 로고    scopus 로고
    • Restricted localization of thrombospondin-2 protein during mouse embryogenesis: A comparison to thrombospondin-1
    • Tooney PA, Sakai T, Sakai K, Aeschlimann D, Mosher DF. Restricted localization of thrombospondin-2 protein during mouse embryogenesis: a comparison to thrombospondin-1. Matrix Biol. 1998;17:131-143.
    • (1998) Matrix Biol , vol.17 , pp. 131-143
    • Tooney, P.A.1    Sakai, T.2    Sakai, K.3    Aeschlimann, D.4    Mosher, D.F.5
  • 38
    • 0027199292 scopus 로고
    • Differential expression of thrombospondin 1,2, and 3 during murine development
    • Iruela-Arispe ML, Liska DJ, Sage EH, Bornstein P. Differential expression of thrombospondin 1,2, and 3 during murine development. Dev Dyn. 1993;197:40-56.
    • (1993) Dev Dyn , vol.197 , pp. 40-56
    • Iruela-Arispe, M.L.1    Liska, D.J.2    Sage, E.H.3    Bornstein, P.4
  • 39
    • 0029081659 scopus 로고
    • Thrombospondin-4 is expressed by early osteogenic tissues in the chick embryo
    • Tucker RP, Adams JC, Lawler J. Thrombospondin-4 is expressed by early osteogenic tissues in the chick embryo. Dev Dyn. 1995;203: 477-490.
    • (1995) Dev Dyn , vol.203 , pp. 477-490
    • Tucker, R.P.1    Adams, J.C.2    Lawler, J.3


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