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Volumn 88, Issue 8, 1996, Pages 2951-2958

Quantitative analysis of von Willebrand factor propeptide release in vivo: Effect of experimental endotoxemia and administration of 1-deamino-8- D-arginine vasopressin in humans

Author keywords

[No Author keywords available]

Indexed keywords

DESMOPRESSIN; ENDOTOXIN; PROTEIN PRECURSOR; VON WILLEBRAND FACTOR;

EID: 10244266470     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v88.8.2951.bloodjournal8882951     Document Type: Article
Times cited : (191)

References (37)
  • 1
    • 0025243601 scopus 로고
    • Cell biology of von Willebrand factor
    • Wagner DD: Cell biology of von Willebrand factor. Annu Rev Cell Biol 6:217, 1990
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 217
    • Wagner, D.D.1
  • 2
    • 0026323664 scopus 로고
    • Von Willebrand factor
    • Sadler JE: von Willebrand factor. J Biol Chem 266:22777, 1991
    • (1991) J Biol Chem , vol.266 , pp. 22777
    • Sadler, J.E.1
  • 5
    • 0019945329 scopus 로고
    • Thrombin-mediated release of factor VIII-related antigen from human umbilical vein endothelial cells in culture
    • Levine JD, Harlan JM, Harker LA, Joseph ML, Counts RB: Thrombin-mediated release of factor VIII-related antigen from human umbilical vein endothelial cells in culture. Blood 60:531, 1982
    • (1982) Blood , vol.60 , pp. 531
    • Levine, J.D.1    Harlan, J.M.2    Harker, L.A.3    Joseph, M.L.4    Counts, R.B.5
  • 7
    • 0021683006 scopus 로고
    • Biosynthesis of von Willebrand protein by human endothelial cells: Processing steps and their intracellular localization
    • Wagner DD, Marder VJ: Biosynthesis of von Willebrand protein by human endothelial cells: Processing steps and their intracellular localization. J Cell Biol 99:2123, 1984
    • (1984) J Cell Biol , vol.99 , pp. 2123
    • Wagner, D.D.1    Marder, V.J.2
  • 9
    • 0022504431 scopus 로고
    • Inducible secretion of large, biologically potent von Willebrand factor multimers
    • Sporn LA, Marder VJ. Wagner DD: Inducible secretion of large, biologically potent von Willebrand factor multimers. Cell 46:185, 1986
    • (1986) Cell , vol.46 , pp. 185
    • Sporn, L.A.1    Marder, V.J.2    Wagner, D.D.3
  • 10
    • 0024459008 scopus 로고
    • Binding of von Willebrand factor to glycoproteins Ib and IIIb/IIIa complex: Affinity is related to multimeric size
    • Federici AB, Pagani BS, Colibretti ML, DeMarco L, Manucci PM: Binding of von Willebrand factor to glycoproteins Ib and IIIb/IIIa complex: Affinity is related to multimeric size. Br J Haematol 73:93, 1989
    • (1989) Br J Haematol , vol.73 , pp. 93
    • Federici, A.B.1    Pagani, B.S.2    Colibretti, M.L.3    DeMarco, L.4    Manucci, P.M.5
  • 11
    • 0023091908 scopus 로고
    • Divergent fates of von Willebrand factor and its propolypeptide (von Willebrand antigen II) after secretion from endothelial cells
    • Wagner DD, Fay PJ, Sporn LA, Sinha S, Lawrence SO, Marder VJ: Divergent fates of von Willebrand factor and its propolypeptide (von Willebrand antigen II) after secretion from endothelial cells. Proc Natl Acad Sci USA 84:1955, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1955
    • Wagner, D.D.1    Fay, P.J.2    Sporn, L.A.3    Sinha, S.4    Lawrence, S.O.5    Marder, V.J.6
  • 13
    • 0026065681 scopus 로고
    • The propolypeptide of von Willebrand factor is required for the formation of a functional factor VIII binding site in mature von Willebrand factor
    • Leyte A, Voorberg J, van Schijndel HB, Duim B, Pannekoek H, van Mourik JA: The propolypeptide of von Willebrand factor is required for the formation of a functional factor VIII binding site in mature von Willebrand factor. Biochem J 274:257, 1991
    • (1991) Biochem J , vol.274 , pp. 257
    • Leyte, A.1    Voorberg, J.2    Van Schijndel, H.B.3    Duim, B.4    Pannekoek, H.5    Van Mourik, J.A.6
  • 14
    • 0015822275 scopus 로고
    • Culture of human cell derived from umbilical veins. Identification by morphologic criteria
    • Jaffe EA, Nachman NL, Becker CG, Minick CR: Culture of human cell derived from umbilical veins. Identification by morphologic criteria. J Clin Invest 52:2745, 1973
    • (1973) J Clin Invest , vol.52 , pp. 2745
    • Jaffe, E.A.1    Nachman, N.L.2    Becker, C.G.3    Minick, C.R.4
  • 16
    • 0025095281 scopus 로고
    • Domains involved in multimer assembly of von Willebrand factor (vWf): Multimerization is independent of dimerization
    • Voorberg J, Fontijn R, van Mourik JA, Pannekoek H: Domains involved in multimer assembly of von Willebrand factor (vWf): Multimerization is independent of dimerization. EMBO J 9:797, 1990
    • (1990) EMBO J , vol.9 , pp. 797
    • Voorberg, J.1    Fontijn, R.2    Van Mourik, J.A.3    Pannekoek, H.4
  • 18
    • 0026509891 scopus 로고
    • Monocytes enhance endothelial von Willebrand factor release and prostacyclin production with different kinetics and dependency on intercellular contact between these two cell types
    • Hakkert BC, Rentenaar JM, van Mourik JA: Monocytes enhance endothelial von Willebrand factor release and prostacyclin production with different kinetics and dependency on intercellular contact between these two cell types. Br J Haematol 80:495, 1992
    • (1992) Br J Haematol , vol.80 , pp. 495
    • Hakkert, B.C.1    Rentenaar, J.M.2    Van Mourik, J.A.3
  • 19
    • 0021249145 scopus 로고
    • Characterization of 25 monoclonal antibodies to factor VIII-von Willebrand factor: Relationship between ristocetin-induced platelet aggregation and platelet adherence to subendothelium
    • Stel HV, Sakariassen KS, Scholte BJ, Veerman ECI, van der Kwast TH, de Groot PG, Sixma JJ, van Mourik JA: Characterization of 25 monoclonal antibodies to factor VIII-von Willebrand factor: Relationship between ristocetin-induced platelet aggregation and platelet adherence to subendothelium. Blood 63:1408, 1984
    • (1984) Blood , vol.63 , pp. 1408
    • Stel, H.V.1    Sakariassen, K.S.2    Scholte, B.J.3    Veerman, E.C.I.4    Van Der Kwast, T.H.5    De Groot, P.G.6    Sixma, J.J.7    Van Mourik, J.A.8
  • 20
    • 0027209683 scopus 로고
    • Factor VIII structure and function
    • Fay PJ: Factor VIII structure and function. Thromb Haemost 70:63, 1993
    • (1993) Thromb Haemost , vol.70 , pp. 63
    • Fay, P.J.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248, 1989
    • (1989) Anal Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 24
    • 0016318820 scopus 로고
    • Peroxidase-labeled antibody: A new method of conjugation
    • Nakane PK, Kawaoi A: Peroxidase-labeled antibody: A new method of conjugation. J Histochem Cytochem 22:1084, 1974
    • (1974) J Histochem Cytochem , vol.22 , pp. 1084
    • Nakane, P.K.1    Kawaoi, A.2
  • 25
    • 0026062952 scopus 로고
    • Collagen-binding domain within bovine propolypeptide of von Willebrand factor
    • Takagi J, Fujisawa T, Sekiya F, Saito Y: Collagen-binding domain within bovine propolypeptide of von Willebrand factor. J Biol Chem 266:5575, 1991
    • (1991) J Biol Chem , vol.266 , pp. 5575
    • Takagi, J.1    Fujisawa, T.2    Sekiya, F.3    Saito, Y.4
  • 26
    • 0027254197 scopus 로고
    • Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin
    • Usui T, Takagi J, Saito Y: Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin. J Biol Chem 268:12311, 1993
    • (1993) J Biol Chem , vol.268 , pp. 12311
    • Usui, T.1    Takagi, J.2    Saito, Y.3
  • 27
    • 0029161613 scopus 로고
    • Identification of factor XIIIa-reactive glutamyl residues in the propolypeptide of bovine von Willebrand factor
    • Takagi J, Aoyama T, Ueki S, Ohba H, Saito Y, Lorand L: Identification of factor XIIIa-reactive glutamyl residues in the propolypeptide of bovine von Willebrand factor. Eur J Biochem 232:773, 1995
    • (1995) Eur J Biochem , vol.232 , pp. 773
    • Takagi, J.1    Aoyama, T.2    Ueki, S.3    Ohba, H.4    Saito, Y.5    Lorand, L.6
  • 28
    • 85068951418 scopus 로고
    • Von Willebrand antigen II (VWFAgII) links activation of coagulation and the inflammatory response
    • abstr
    • Kao J, Fan Y, Yan SD, Kisiel W, Tijburg P, van Mourik JA, Stern D: von Willebrand antigen II (VWFAgII) links activation of coagulation and the inflammatory response. Thromb Haemost 69:265, 1993 (abstr)
    • (1993) Thromb Haemost , vol.69 , pp. 265
    • Kao, J.1    Fan, Y.2    Yan, S.D.3    Kisiel, W.4    Tijburg, P.5    Van Mourik, J.A.6    Stern, D.7
  • 29
    • 85068945689 scopus 로고
    • Vascular permeability/vascular endothelial growth factor (VPF/VEGF) and histamin induction of tissue factor (TF) on endothelial cells is linked to the release and action of von Willebrand factor propolypeptide (provWF)
    • Heidelberg, Germany, August 30-September 4, (abstr)
    • Clauss M, Knies U, Risau W, Pötschz B: Vascular permeability/vascular endothelial growth factor (VPF/VEGF) and histamin induction of tissue factor (TF) on endothelial cells is linked to the release and action of von Willebrand factor propolypeptide (provWF). VIIIth International Symposium on the Biology of Vascular Cells. Heidelberg, Germany, August 30-September 4, 1994 (abstr)
    • (1994) VIIIth International Symposium on the Biology of Vascular Cells
    • Clauss, M.1    Knies, U.2    Risau, W.3    Pötschz, B.4
  • 30
    • 0023279138 scopus 로고
    • Composition of the von Willebrand factor storage organelle (Weibel-Palade body) isolated from cultured human umbilical vein endothelial cells
    • Ewenstein BM, Warhol MJ, Handin RI, Pober JS: Composition of the von Willebrand factor storage organelle (Weibel-Palade body) isolated from cultured human umbilical vein endothelial cells. J Cell Biol 104:1423, 1987
    • (1987) J Cell Biol , vol.104 , pp. 1423
    • Ewenstein, B.M.1    Warhol, M.J.2    Handin, R.I.3    Pober, J.S.4
  • 31
    • 0021344581 scopus 로고
    • The effect of DDAVP on plasma levels of von Willebrand antigen II in normal individuals and patients with von Willebrand's disease
    • McCarroll DR, Ruggeri ZM, Montgomery RR: The effect of DDAVP on plasma levels of von Willebrand antigen II in normal individuals and patients with von Willebrand's disease. Blood 63:532, 1984
    • (1984) Blood , vol.63 , pp. 532
    • McCarroll, D.R.1    Ruggeri, Z.M.2    Montgomery, R.R.3
  • 32
    • 0021354080 scopus 로고
    • Correlation between circulating levels of von Willebrand's antigen II and von Willebrand factor: Discrimination between type I and type II von Willebrand's disease
    • McCarroll DR, Ruggeri ZM, Montgomery RR: Correlation between circulating levels of von Willebrand's antigen II and von Willebrand factor: Discrimination between type I and type II von Willebrand's disease. J Lab Clin Med 103:704, 1984
    • (1984) J Lab Clin Med , vol.103 , pp. 704
    • McCarroll, D.R.1    Ruggeri, Z.M.2    Montgomery, R.R.3
  • 33
    • 0029112839 scopus 로고
    • Desmopressin induces endothelial P-Selectin expression and leukocyte rolling in postcapillary venules
    • Kanwar S, Woodman RC, Poon MC, Murohara T, Lefer AM, Davenpeck KL, Kubus P: Desmopressin induces endothelial P-Selectin expression and leukocyte rolling in postcapillary venules. Blood 86:2760, 1995
    • (1995) Blood , vol.86 , pp. 2760
    • Kanwar, S.1    Woodman, R.C.2    Poon, M.C.3    Murohara, T.4    Lefer, A.M.5    Davenpeck, K.L.6    Kubus, P.7
  • 35
    • 0028242239 scopus 로고
    • Von Willebrand Factor proteolytic processing and multimerization precede the formation of Weibel-Palade bodies
    • Vischer VM, Wagner DD: von Willebrand Factor proteolytic processing and multimerization precede the formation of Weibel-Palade bodies. Blood 83:3536, 1994
    • (1994) Blood , vol.83 , pp. 3536
    • Vischer, V.M.1    Wagner, D.D.2
  • 36
    • 0027468518 scopus 로고
    • Post-translational processing of proenkephalins and chromogranins/secretogranins
    • Dillen L, Miserez B, Claeys M, Aunis D, De Potter W: Post-translational processing of proenkephalins and chromogranins/secretogranins. Neurochem Int 22:315, 1993
    • (1993) Neurochem Int , vol.22 , pp. 315
    • Dillen, L.1    Miserez, B.2    Claeys, M.3    Aunis, D.4    De Potter, W.5
  • 37
    • 0028569521 scopus 로고
    • Proteases and the emerging role of protease inhibitors in prohormone processing
    • Hook VYH, Azaryan AV, Hwang SR, Tezapsidis N: Proteases and the emerging role of protease inhibitors in prohormone processing. FASEB J 8:1269, 1994
    • (1994) FASEB J , vol.8 , pp. 1269
    • Hook, V.Y.H.1    Azaryan, A.V.2    Hwang, S.R.3    Tezapsidis, N.4


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