메뉴 건너뛰기




Volumn 87, Issue 10, 1996, Pages 4223-4234

Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

BARIUM; CADMIUM; CALCIUM; COBALT; COPPER; IODOACETAMIDE; LEUPEPTIN; MAGNESIUM; MANGANESE; NICKEL; PROTEINASE; SERINE PROTEINASE INHIBITOR; STRONTIUM; VON WILLEBRAND FACTOR; ZINC;

EID: 0029925856     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.10.4223.bloodjournal87104223     Document Type: Article
Times cited : (827)

References (45)
  • 1
    • 0024356269 scopus 로고
    • Multimeric composition of endothelial cell-derived von Willebrand factor
    • Tsai H-M, 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
  • 2
    • 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 (types 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 (types 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
  • 7
    • 0023116024 scopus 로고
    • Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type IIA von Willebrand disease from those generated by plasmin
    • Berkowitz SD, Dent J, 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 IIA 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.2    Roberts, J.3    Fujimura, Y.4    Plow, E.F.5    Titani, K.6    Ruggeri, Z.M.7    Zimmerman, T.S.8
  • 8
    • 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
  • 9
    • 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
  • 11
    • 0022862698 scopus 로고
    • Subunit composition of plasma von Willebrand factor in patients with myeloproliferative syndrome
    • Budde U, Dent JA, Berkowitz SD, Ruggeri ZM, Zimmerman TS: Subunit composition of plasma von Willebrand factor in patients with myeloproliferative syndrome. Blood 68:1213, 1986
    • (1986) Blood , vol.68 , pp. 1213
    • Budde, U.1    Dent, J.A.2    Berkowitz, S.D.3    Ruggeri, Z.M.4    Zimmerman, T.S.5
  • 13
    • 0021959985 scopus 로고
    • Effects of fresh-frozen plasma and its cryosupernalant fraction on von Willebrand factor multimeric forms in chronic relapsing thrombotic thrombocytopenic purpura
    • Moake JL, Byrnes JJ, Troll JH, Rudy CK, Hong SL, Weinstein MJ, Colannino NM: Effects of fresh-frozen plasma and its cryosupernalant fraction on von Willebrand factor multimeric forms in chronic relapsing thrombotic thrombocytopenic purpura. Blood 65:1232, 1985
    • (1985) Blood , vol.65 , pp. 1232
    • Moake, J.L.1    Byrnes, J.J.2    Troll, J.H.3    Rudy, C.K.4    Hong, S.L.5    Weinstein, M.J.6    Colannino, N.M.7
  • 14
    • 0018913227 scopus 로고
    • Support of ristocetin-induced platelet aggregation by procoagulant-inactive and plasmin-cleaved forms of human factor VIII/von Willebrand factor
    • Andersen JC, Switzer ME, McKee PA: Support of ristocetin-induced platelet aggregation by procoagulant-inactive and plasmin-cleaved forms of human factor VIII/von Willebrand factor. Blood 55:101, 1980
    • (1980) Blood , vol.55 , pp. 101
    • Andersen, J.C.1    Switzer, M.E.2    McKee, P.A.3
  • 15
    • 0021984526 scopus 로고
    • Effects of plasmin on von Willebrand factor multimers. Degradation in vitro and stimulation of release in vivo
    • Hamilton KK, Fretto LJ, Grierson DS, McKee PA: Effects of plasmin on von Willebrand factor multimers. Degradation in vitro and stimulation of release in vivo. J Clin Invest 76:261, 1985
    • (1985) J Clin Invest , vol.76 , pp. 261
    • Hamilton, K.K.1    Fretto, L.J.2    Grierson, D.S.3    McKee, P.A.4
  • 16
    • 0024320111 scopus 로고
    • Cleavage of human von Willebrand factor by porcine pancreatic elastase
    • Howard MA, Greco T, Coghlan M: Cleavage of human von Willebrand factor by porcine pancreatic elastase. Blood 74:673, 1989
    • (1989) Blood , vol.74 , pp. 673
    • Howard, M.A.1    Greco, T.2    Coghlan, M.3
  • 17
    • 0022537998 scopus 로고
    • Proteolytic cleavage of human von Willebrand factor induced by enzyme(s) released from polymorphonuclear cells
    • Thompson EA, Howard MA: Proteolytic cleavage of human von Willebrand factor induced by enzyme(s) released from polymorphonuclear cells. Blood 67:1281, 1986
    • (1986) Blood , vol.67 , pp. 1281
    • Thompson, E.A.1    Howard, M.A.2
  • 18
    • 0024552878 scopus 로고
    • Endothelial cell-derived high molecular weight von Willebrand factor is converted into the plasma multimer patterns by granulocyte proteases
    • Tsai H-M, Nagel RL, Hatcher VB, Sussman II: Endothelial cell-derived high molecular weight von Willebrand factor is converted into the plasma multimer patterns 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
  • 19
    • 0023765832 scopus 로고
    • Evidence that calpains and elastase do not produce the von Willebrand factor fragments present in normal plasma and IIA von Willebrand disease
    • Berkowitz SD, Nozaki H, Titani K, Murachi T, Plow EF, Zimmerman TS: Evidence that calpains and elastase do not produce the von Willebrand factor fragments present in normal plasma and IIA von Willebrand disease. Blood 72:721, 1988
    • (1988) Blood , vol.72 , pp. 721
    • Berkowitz, S.D.1    Nozaki, H.2    Titani, K.3    Murachi, T.4    Plow, E.F.5    Zimmerman, T.S.6
  • 20
    • 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
  • 21
    • 0021959235 scopus 로고
    • Cleavage of human von Willebrand factor by platelet calcium-activated protease
    • Kunicki TJ, Montgomery RR, Schullek J: Cleavage of human von Willebrand factor by platelet calcium-activated protease. Blood 65:352, 1985
    • (1985) Blood , vol.65 , pp. 352
    • Kunicki, T.J.1    Montgomery, R.R.2    Schullek, J.3
  • 22
    • 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
  • 23
    • 49149148296 scopus 로고
    • A simple method for dialysis of small-volume samples
    • Marusyk R, Sergeant A: A simple method for dialysis of small-volume samples. Anal Biochem 105:403, 1980
    • (1980) Anal Biochem , vol.105 , pp. 403
    • Marusyk, R.1    Sergeant, A.2
  • 24
    • 0019442145 scopus 로고
    • The complex multimeric composition of factor VIII/von Willebrand factor
    • Ruggeri ZM, Zimmerman TS: The complex multimeric composition of factor VIII/von Willebrand factor. Blood 57:1140, 1981
    • (1981) Blood , vol.57 , pp. 1140
    • Ruggeri, Z.M.1    Zimmerman, T.S.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage G4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage G4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 26
    • 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, Heliums 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 78:1456, 1986
    • (1986) J Clin Invest , vol.78 , pp. 1456
    • Moake, J.L.1    Turner, N.A.2    Stathopoulos, N.A.3    Nolasco, L.H.4    Heliums, J.D.5
  • 27
    • 0028266474 scopus 로고
    • Shear stress enhances the proteolysis of von Willebrand factor in normal plasma
    • Tsai H-M, 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
  • 29
    • 0017285840 scopus 로고
    • Immunologic studies on human factor VIII (anti-nemophilic factor A, AHF) components produced by low-ionic-strength dialysis
    • Bouma BN, van Mourik JA, de Graaf S, Hordijk-Hos JM, Sixma JJ: Immunologic studies on human factor VIII (anti-nemophilic factor A, AHF) components produced by low-ionic-strength dialysis. Blood 47:253, 1976
    • (1976) Blood , vol.47 , pp. 253
    • Bouma, B.N.1    Van Mourik, J.A.2    De Graaf, S.3    Hordijk-Hos, J.M.4    Sixma, J.J.5
  • 30
    • 0017619809 scopus 로고
    • Degradation of purified factor VIII by endogenous contaminating enzymes
    • Furlan M, Beck EA: Degradation of purified factor VIII by endogenous contaminating enzymes. Thromb Res 10:153, 1977
    • (1977) Thromb Res , vol.10 , pp. 153
    • Furlan, M.1    Beck, E.A.2
  • 31
    • 0018238910 scopus 로고
    • Divergent denaturation of proteases by urea and dodecylsulfate in the absence of substrate
    • Hilz H, Fanick W: Divergent denaturation of proteases by urea and dodecylsulfate in the absence of substrate. Hoppe-Seyler Z Physiol Chem 359:1447, 1978
    • (1978) Hoppe-Seyler Z Physiol Chem , vol.359 , pp. 1447
    • Hilz, H.1    Fanick, W.2
  • 32
    • 0017284797 scopus 로고
    • Some properties of proteolysis by polymorphonuclear leukocyte-granule extracts
    • Asghar SS, Cormane RH: Some properties of proteolysis by polymorphonuclear leukocyte-granule extracts. J Invest Dermatol 66:93, 1976
    • (1976) J Invest Dermatol , vol.66 , pp. 93
    • Asghar, S.S.1    Cormane, R.H.2
  • 33
    • 0027996812 scopus 로고
    • Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol
    • Hojima Y, Behta B, Romanic AM, Prockop DJ: Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol. Anal Biochem 223:173, 1994
    • (1994) Anal Biochem , vol.223 , pp. 173
    • Hojima, Y.1    Behta, B.2    Romanic, A.M.3    Prockop, D.J.4
  • 34
    • 0028314508 scopus 로고
    • Proteolysis of von Willebrand factor in therapeutic plasma concentrates
    • Mannucci PM, Lattuada A, Ruggeri ZM: Proteolysis of von Willebrand factor in therapeutic plasma concentrates. Blood 83:3018, 1994
    • (1994) Blood , vol.83 , pp. 3018
    • Mannucci, P.M.1    Lattuada, A.2    Ruggeri, Z.M.3
  • 36
    • 0025834586 scopus 로고
    • Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin
    • Lambert Vidmar S, Lottspeich F, Emod I, Planchenault T, Keil-Dlouha V: Latent fibronectin-degrading serine proteinase activity in N-terminal heparin-binding domain of human plasma fibronectin. Eur J Biochem 201:71, 1991
    • (1991) Eur J Biochem , vol.201 , pp. 71
    • Lambert Vidmar, S.1    Lottspeich, F.2    Emod, I.3    Planchenault, T.4    Keil-Dlouha, V.5
  • 38
    • 0023784467 scopus 로고
    • The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B
    • Crawford C, Mason RW, Wikstrom P, Shaw E: The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B. Biochem J 253:751, 1988
    • (1988) Biochem J , vol.253 , pp. 751
    • Crawford, C.1    Mason, R.W.2    Wikstrom, P.3    Shaw, E.4
  • 40
    • 0020615908 scopus 로고
    • 2-macroglobuHn-enzyme complexes toward human factor VIII/von Willebrand factor
    • 2-macroglobuHn-enzyme complexes toward human factor VIII/von Willebrand factor. Biochemistry 22:1437, 1983
    • (1983) Biochemistry , vol.22 , pp. 1437
    • Switzer, M.E.P.1    Gordon, H.J.2    McKee, P.A.3
  • 41
    • 0021101203 scopus 로고
    • 2-macroglobulin half-molecules with plasmin as a probe of protease binding site structure
    • 2-macroglobulin half-molecules with plasmin as a probe of protease binding site structure. Biochemistry 22:4933, 1983
    • (1983) Biochemistry , vol.22 , pp. 4933
    • Gonias, S.L.1    Pizzo, S.V.2
  • 43
    • 0028020715 scopus 로고
    • Amino acid analysis and protein database composition search as a fast and inexpensive method to identify proteins
    • Hobohm U, Houthaeve T, Sander C: Amino acid analysis and protein database composition search as a fast and inexpensive method to identify proteins. Anal Biochem 222:202, 1994
    • (1994) Anal Biochem , vol.222 , pp. 202
    • Hobohm, U.1    Houthaeve, T.2    Sander, C.3
  • 44
    • 0018189401 scopus 로고
    • Human fibrinogen heterogeneities: Distribution and charge characteristics of chains of Aa origin
    • Galanakis DK, Mosesson MW, Stathakis NE: Human fibrinogen heterogeneities: Distribution and charge characteristics of chains of Aa origin. J Lab Clin Med 92:376, 1987
    • (1987) J Lab Clin Med , vol.92 , pp. 376
    • Galanakis, D.K.1    Mosesson, M.W.2    Stathakis, N.E.3
  • 45
    • 0021265740 scopus 로고
    • Cleavage of fibrinogen by human platelet calcium-activated protease
    • Kunicki TJ, Mosesson MW, Pidard D: Cleavage of fibrinogen by human platelet calcium-activated protease. Thromb Res 35:169, 1984
    • (1984) Thromb Res , vol.35 , pp. 169
    • Kunicki, T.J.1    Mosesson, M.W.2    Pidard, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.