메뉴 건너뛰기




Volumn 87, Issue 10, 1996, Pages 4235-4244

Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; CALCIUM ION; EDETIC ACID; EGTAZIC ACID; GUANIDINE; METALLOPROTEINASE; PLASMIN; PROTEINASE; VON WILLEBRAND FACTOR;

EID: 0029878123     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.10.4235.bloodjournal87104235     Document Type: Article
Times cited : (721)

References (34)
  • 3
    • 0028909230 scopus 로고
    • Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group
    • Thompson SG, Kienast J, Pyke SD, Haverkate F, van de Loo JC: Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group. N Engl J Med 332:635, 1995
    • (1995) N Engl J Med , vol.332 , pp. 635
    • Thompson, S.G.1    Kienast, J.2    Pyke, S.D.3    Haverkate, F.4    Van De Loo, J.C.5
  • 4
    • 0025948224 scopus 로고
    • Von Willebrand factor in plasma: A novel risk factor for recurrent myocardial infarction and death
    • Jansson JH, Nilsson TK, Johnson O: von Willebrand factor in plasma: A novel risk factor for recurrent myocardial infarction and death. Br Heart J 66:351, 1991
    • (1991) Br Heart J , vol.66 , pp. 351
    • Jansson, J.H.1    Nilsson, T.K.2    Johnson, O.3
  • 5
    • 0023491311 scopus 로고
    • Unusually large von Willebrand factor multimers increase adhesion of sickle erytnrocytes to human endothelial cells under controlled flow
    • Wick TM, Moake JL, Udden MM, Eskin SG, Sears DA, McIntire LV: Unusually large von Willebrand factor multimers increase adhesion of sickle erytnrocytes to human endothelial cells under controlled flow. J Clin Invest 80:905, 1987
    • (1987) J Clin Invest , vol.80 , pp. 905
    • Wick, T.M.1    Moake, J.L.2    Udden, M.M.3    Eskin, S.G.4    Sears, D.A.5    McIntire, L.V.6
  • 6
    • 0027252053 scopus 로고
    • Sickle erythrocyte-endothelial interaction in microcirculation: The role of von Willebrand factor and implications for vasoocclusion
    • Kaul DK, Nagel RL, Chen D, Tsai HM: Sickle erythrocyte-endothelial interaction in microcirculation: The role of von Willebrand factor and implications for vasoocclusion. Blood 81:2429, 1993
    • (1993) Blood , vol.81 , pp. 2429
    • Kaul, D.K.1    Nagel, R.L.2    Chen, D.3    Tsai, H.M.4
  • 7
    • 0024356269 scopus 로고
    • Multimeric composition of endothelial cell-derived von Willebrand factor
    • Tsai HM, Nagel RL, Hatcher VB, Sussman II: Multimeric composition of endothelial cell-derived von Willebrand factor. Blood 73:2074, 1989
    • (1989) Blood , vol.73 , pp. 2074
    • Tsai, H.M.1    Nagel, R.L.2    Hatcher, V.B.3    Sussman, I.I.4
  • 8
    • 0026001694 scopus 로고
    • The high molecular weight form of endothelial cell von Willebrand factor is released by the regulated pathway
    • Tsai HM, Nagel RL, Hatcher VB, Seaton AC, Sussman II: The high molecular weight form of endothelial cell von Willebrand factor is released by the regulated pathway. Br J Haematol 79:239, 1991
    • (1991) Br J Haematol , vol.79 , pp. 239
    • Tsai, H.M.1    Nagel, R.L.2    Hatcher, V.B.3    Seaton, A.C.4    Sussman, I.I.5
  • 9
    • 0024531101 scopus 로고
    • Molecular and cellular biology of von Willebrand factor
    • Handin RI, Wagner DD: Molecular and cellular biology of von Willebrand factor. Prog Hemostas Thromb 9:233, 1989
    • (1989) Prog Hemostas Thromb , vol.9 , pp. 233
    • Handin, R.I.1    Wagner, D.D.2
  • 10
    • 0022517442 scopus 로고
    • Subunit composition of plasma von Willebrand factor. Cleavage is present in normal individuals, increased in IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individual oligomers (type IIC, IID, and IIE)
    • Zimmerman TS, Dent JA, Ruggeri ZM, Nannini LH: Subunit composition of plasma von Willebrand factor. Cleavage is present in normal individuals, increased in IIA and IIB von Willebrand disease, but minimal in variants with aberrant structure of individual oligomers (type IIC, IID, and IIE). J Clin Invest 77:947, 1986
    • (1986) J Clin Invest , vol.77 , pp. 947
    • Zimmerman, T.S.1    Dent, J.A.2    Ruggeri, Z.M.3    Nannini, L.H.4
  • 11
    • 0025895660 scopus 로고
    • Subunit composition of plasma von Willebrand factor multimers: Evidence for a non-proteolytic mechanism resulting in apparent increase in proteolytic fragments
    • Tsai HM, Nagel RL, Sussman II: Subunit composition of plasma von Willebrand factor multimers: Evidence for a non-proteolytic mechanism resulting in apparent increase in proteolytic fragments. Thromb Res 63:179, 1991
    • (1991) Thromb Res , vol.63 , pp. 179
    • Tsai, H.M.1    Nagel, R.L.2    Sussman, I.I.3
  • 12
    • 0026069774 scopus 로고
    • Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit
    • Dent JA, Galbusera M, Ruggeri ZM: Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit. J Clin Invest 88:774, 1991
    • (1991) J Clin Invest , vol.88 , pp. 774
    • Dent, J.A.1    Galbusera, M.2    Ruggeri, Z.M.3
  • 13
    • 0024552878 scopus 로고
    • Endothelial cell-derived high molecular weight von Willebrand factor is converted into the plasma multimer pattern by granulocyte proteases
    • Tsai HM, Nagel RL, Hatcher VB Sussman II: Endothelial cell-derived high molecular weight von Willebrand factor is converted into the plasma multimer pattern by granulocyte proteases. Biochem Biophys Res Commun 158:980, 1989
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 980
    • Tsai, H.M.1    Nagel, R.L.2    Hatcher, V.B.3    Sussman, I.I.4
  • 15
    • 0025831444 scopus 로고
    • Granulocyte proteases do not process endothelial cell-derived unusually large von Willebrand factor multimers to plasma vWF in vivo
    • Phillips MD, Vu C, Nolasco L, Moake JL: Granulocyte proteases do not process endothelial cell-derived unusually large von Willebrand factor multimers to plasma vWF in vivo. Am J Hematol 37:80, 1991
    • (1991) Am J Hematol , vol.37 , pp. 80
    • Phillips, M.D.1    Vu, C.2    Nolasco, L.3    Moake, J.L.4
  • 16
    • 0028266474 scopus 로고
    • Shear stress enhances the proteolysis of von Willebrand factor in normal plasma
    • Tsai HM, Sussman II, Nagel RL: Shear stress enhances the proteolysis of von Willebrand factor in normal plasma. Blood 83:2171, 1994
    • (1994) Blood , vol.83 , pp. 2171
    • Tsai, H.M.1    Sussman, I.I.2    Nagel, R.L.3
  • 17
    • 0017615909 scopus 로고
    • Binding of factor VIII to platelets in the presence of ristocetin
    • Zucker MB, Kim S-J, McPherson J, Grant RA: Binding of factor VIII to platelets in the presence of ristocetin. Br J Haematol 35:535, 1977
    • (1977) Br J Haematol , vol.35 , pp. 535
    • Zucker, M.B.1    Kim, S.-J.2    McPherson, J.3    Grant, R.A.4
  • 18
    • 0027496217 scopus 로고
    • Conformational flexibility of enzyme active sites
    • Tsou C-L: Conformational flexibility of enzyme active sites. Science 262:380, 1993
    • (1993) Science , vol.262 , pp. 380
    • Tsou, C.-L.1
  • 19
    • 0027536915 scopus 로고
    • Von Willebrand factor
    • Ruggeri ZM, Ware J: von Willebrand factor. FASEB J 7:308, 1993
    • (1993) FASEB J , vol.7 , pp. 308
    • Ruggeri, Z.M.1    Ware, J.2
  • 20
    • 0020407701 scopus 로고
    • Electron microscopy of human factor VIII/von Willebrand glycoprotein: Effect of reducing reagents on structure and function
    • Ohmori K, Fretto LJ, Harrison RL, Sw EP, Erickson HP, McKee PA: Electron microscopy of human factor VIII/von Willebrand glycoprotein: Effect of reducing reagents on structure and function. J Cell Biol 95:632, 1982
    • (1982) J Cell Biol , vol.95 , pp. 632
    • Ohmori, K.1    Fretto, L.J.2    Harrison, R.L.3    Sw, E.P.4    Erickson, H.P.5    McKee, P.A.6
  • 21
    • 0021162314 scopus 로고
    • Conformational domains and structural transitions of human von Willebrand protein
    • Loscalzo J, Handin RI: Conformational domains and structural transitions of human von Willebrand protein. Biochemistry 23:3880, 1984
    • (1984) Biochemistry , vol.23 , pp. 3880
    • Loscalzo, J.1    Handin, R.I.2
  • 22
    • 0023116024 scopus 로고
    • Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type UA von Willebrand disease from those generated by plasmin
    • Berkowitz SD, Dent JD, Roberts J, Fujimura Y, Plow EF, Titani K, Ruggeri ZM, Zimmerman TS: Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type UA von Willebrand disease from those generated by plasmin. J Clin Invest 79:524, 1987
    • (1987) J Clin Invest , vol.79 , pp. 524
    • Berkowitz, S.D.1    Dent, J.D.2    Roberts, J.3    Fujimura, Y.4    Plow, E.F.5    Titani, K.6    Ruggeri, Z.M.7    Zimmerman, T.S.8
  • 24
    • 0027994031 scopus 로고
    • Matrix metalloproteinase inhibitor BB-94 (batimastat) inhibits human colon tumor growth and spread in a patient-like orthotopic model in nude mice
    • Wang X, Fu X, Brown PD, Crimmin MJ, Hoffman RM: Matrix metalloproteinase inhibitor BB-94 (batimastat) inhibits human colon tumor growth and spread in a patient-like orthotopic model in nude mice. Cancer Res 54:4726, 1994
    • (1994) Cancer Res , vol.54 , pp. 4726
    • Wang, X.1    Fu, X.2    Brown, P.D.3    Crimmin, M.J.4    Hoffman, R.M.5
  • 25
    • 0025044664 scopus 로고
    • Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor
    • Dent JA, Berkowitz SD, Ware J, Kasper CK, Ruggeri ZM: Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor. Proc Natl Acad Sci USA 87:6306, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6306
    • Dent, J.A.1    Berkowitz, S.D.2    Ware, J.3    Kasper, C.K.4    Ruggeri, Z.M.5
  • 26
    • 0024369489 scopus 로고
    • Cryosupernatant regulates accumulation of unusually large vWF multimers from endothelial cells
    • Frangos JA, Moake JL, Nolasco L, Phillips MD, McIntire LV: Cryosupernatant regulates accumulation of unusually large vWF multimers from endothelial cells. Am J Physiol 256:H1635, 1989
    • (1989) Am J Physiol , vol.256
    • Frangos, J.A.1    Moake, J.L.2    Nolasco, L.3    Phillips, M.D.4    McIntire, L.V.5
  • 27
    • 0001601210 scopus 로고
    • Plasma von Willebrand factor processing activity functions like a disulfide bond reduclase: Reversible decrease of multimer size
    • Phillips MD, Moake JL, Nolasco L, Garcia R: Plasma von Willebrand factor processing activity functions like a disulfide bond reduclase: Reversible decrease of multimer size. Thromb Haemost 69:1199a, 1993
    • (1993) Thromb Haemost , vol.69
    • Phillips, M.D.1    Moake, J.L.2    Nolasco, L.3    Garcia, R.4
  • 28
    • 0027172201 scopus 로고
    • Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers
    • Furlan M, Robles R, Affolter D, Meyer D, Baillod P, Lämmle B: Triplet structure of von Willebrand factor reflects proteolytic degradation of high molecular weight multimers. Proc Natl Acad Sci USA 90:7503, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7503
    • Furlan, M.1    Robles, R.2    Affolter, D.3    Meyer, D.4    Baillod, P.5    Lämmle, B.6
  • 30
    • 0026716153 scopus 로고
    • Molecular genetics of von Willebrand disease
    • Ginsburg D, Bowie EJW: Molecular genetics of von Willebrand disease. Blood 79:2507, 1992
    • (1992) Blood , vol.79 , pp. 2507
    • Ginsburg, D.1    Bowie, E.J.W.2
  • 31
    • 0024734977 scopus 로고
    • Abnormalities of von Willebrand factor multimers in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome
    • Moake JL, McPherson PD: Abnormalities of von Willebrand factor multimers in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome. Am J Med 87:9N, 1989
    • (1989) Am J Med , vol.87
    • Moake, J.L.1    McPherson, P.D.2
  • 32
    • 0022597036 scopus 로고
    • Loss of the largest von Willebrand factor multimers from the plasma of patients with congenital cardiac defects
    • Gill JC, Wilson AD, Endres-Brooks J, Montgomery RR: Loss of the largest von Willebrand factor multimers from the plasma of patients with congenital cardiac defects. Blood 67:758, 1986
    • (1986) Blood , vol.67 , pp. 758
    • Gill, J.C.1    Wilson, A.D.2    Endres-Brooks, J.3    Montgomery, R.R.4
  • 33
    • 0023914138 scopus 로고
    • Changes in von Willebrand factor during cardiac surgery: Effect of desmopressin acetate
    • Weinstein M, Ware JA, Troll J, Salzman E: Changes in von Willebrand factor during cardiac surgery: Effect of desmopressin acetate. Blood 71:1648, 1988
    • (1988) Blood , vol.71 , pp. 1648
    • Weinstein, M.1    Ware, J.A.2    Troll, J.3    Salzman, E.4
  • 34
    • 0027500203 scopus 로고
    • Degradation of von Willebrand factor in patients with acquired clinical conditons in which there is heightened proteolysis
    • Federici AB, Berkowitz SD, Lattuada A, Mannucci PM: Degradation of von Willebrand factor in patients with acquired clinical conditons in which there is heightened proteolysis. Blood 81:720, 1993
    • (1993) Blood , vol.81 , pp. 720
    • Federici, A.B.1    Berkowitz, S.D.2    Lattuada, A.3    Mannucci, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.