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Volumn 8, Issue 12, 2010, Pages 2778-2788

Disulfide bond reduction of von Willebrand factor by ADAMTS-13

Author keywords

(ultra large) von Willebrand factor; ADAMTS 13; Redox regulation; Shear stress; Thiol disulfide exchange

Indexed keywords

THIOL; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

EID: 78649995651     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2010.04094.x     Document Type: Article
Times cited : (46)

References (39)
  • 1
    • 0025906758 scopus 로고
    • Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids
    • Voorberg J, Fontijn R, Calafat J, Janssen H, Van Mourik JA, Pannekoek H. Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids. J Cell Biol 1991; 113: 195-205.
    • (1991) J Cell Biol , vol.113 , pp. 195-205
    • Voorberg, J.1    Fontijn, R.2    Calafat, J.3    Janssen, H.4    Van Mourik, J.A.5    Pannekoek, H.6
  • 3
    • 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
  • 4
    • 0023547917 scopus 로고
    • Identification of disulfide-bridged substructures within human von Willebrand factor
    • Marti T, Rosselet SJ, Titani K, Walsh KA. Identification of disulfide-bridged substructures within human von Willebrand factor. Biochemistry 1987; 26: 8099-109.
    • (1987) Biochemistry , vol.26 , pp. 8099-8109
    • Marti, T.1    Rosselet, S.J.2    Titani, K.3    Walsh, K.A.4
  • 5
    • 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 1991; 79: 239-45.
    • (1991) Br J Haematol , vol.79 , pp. 239-245
    • Tsai, H.M.1    Nagel, R.L.2    Hatcher, V.B.3    Seaton, A.C.4    Sussman, I.I.5
  • 6
    • 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 1986; 46: 185-90.
    • (1986) Cell , vol.46 , pp. 185-190
    • Sporn, L.A.1    Marder, V.J.2    Wagner, D.D.3
  • 7
    • 0033386647 scopus 로고    scopus 로고
    • In vivo regulation of von willebrand factor synthesis: von Willebrand factor production in endothelial cells after lung transplantation between normal pigs and von Willebrand factor-deficient pigs
    • Brouland JP, Egan T, Roussi J, Bonneau M, Pignaud G, Bal C, Vaiman M, Andre P, Herve P, Mazmanian GM, Drouet L. In vivo regulation of von willebrand factor synthesis: von Willebrand factor production in endothelial cells after lung transplantation between normal pigs and von Willebrand factor-deficient pigs. Arterioscler Thromb Vasc Biol 1999; 19: 3055-62.
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 3055-3062
    • Brouland, J.P.1    Egan, T.2    Roussi, J.3    Bonneau, M.4    Pignaud, G.5    Bal, C.6    Vaiman, M.7    Andre, P.8    Herve, P.9    Mazmanian, G.M.10    Drouet, L.11
  • 8
    • 0036624844 scopus 로고    scopus 로고
    • Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers
    • Arya M, Anvari B, Romo GM, Cruz MA, Dong JF, McIntire LV, Moake JL, Lopez JA. Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers. Blood 2002; 99: 3971-7.
    • (2002) Blood , vol.99 , pp. 3971-3977
    • Arya, M.1    Anvari, B.2    Romo, G.M.3    Cruz, M.A.4    Dong, J.F.5    McIntire, L.V.6    Moake, J.L.7    Lopez, J.A.8
  • 9
    • 0031733409 scopus 로고    scopus 로고
    • Increased von Willebrand factor (vWf) binding to platelets associated with impaired vWf breakdown in thrombotic thrombocytopenic purpura
    • Moake JL, Chow TW. Increased von Willebrand factor (vWf) binding to platelets associated with impaired vWf breakdown in thrombotic thrombocytopenic purpura. J Clin Apher 1998; 13: 126-32.
    • (1998) J Clin Apher , vol.13 , pp. 126-132
    • Moake, J.L.1    Chow, T.W.2
  • 10
    • 0029925856 scopus 로고    scopus 로고
    • Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis
    • Furlan M, Robles R, Lammle B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood 1996; 87: 4223-34.
    • (1996) Blood , vol.87 , pp. 4223-4234
    • Furlan, M.1    Robles, R.2    Lammle, B.3
  • 11
    • 0029878123 scopus 로고    scopus 로고
    • Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion
    • Tsai HM. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. Blood 1996; 87: 4235-44.
    • (1996) Blood , vol.87 , pp. 4235-4244
    • Tsai, H.M.1
  • 13
    • 0035798582 scopus 로고    scopus 로고
    • Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura
    • Zheng X, Chung D, Takayama TK, Majerus EM, Sadler JE, Fujikawa K. Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura. J Biol Chem 2001; 276: 41059-63.
    • (2001) J Biol Chem , vol.276 , pp. 41059-41063
    • Zheng, X.1    Chung, D.2    Takayama, T.K.3    Majerus, E.M.4    Sadler, J.E.5    Fujikawa, K.6
  • 14
    • 0347533937 scopus 로고    scopus 로고
    • Evaluation of ADAMTS-13 activity in plasma using recombinant von Willebrand Factor A2 domain polypeptide as substrate
    • Cruz MA, Whitelock J, Dong JF. Evaluation of ADAMTS-13 activity in plasma using recombinant von Willebrand Factor A2 domain polypeptide as substrate. Thromb Haemost 2003; 90: 1204-9.
    • (2003) Thromb Haemost , vol.90 , pp. 1204-1209
    • Cruz, M.A.1    Whitelock, J.2    Dong, J.F.3
  • 15
    • 17144408687 scopus 로고    scopus 로고
    • FRETS-VWF73, a first fluorogenic substrate for ADAMTS13 assay
    • Kokame K, Nobe Y, Kokubo Y, Okayama A, Miyata T. FRETS-VWF73, a first fluorogenic substrate for ADAMTS13 assay. Br J Haematol 2005; 129: 93-100.
    • (2005) Br J Haematol , vol.129 , pp. 93-100
    • Kokame, K.1    Nobe, Y.2    Kokubo, Y.3    Okayama, A.4    Miyata, T.5
  • 17
    • 28344435221 scopus 로고    scopus 로고
    • Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions
    • Dong JF. Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions. J Thromb Haemost 2005; 3: 1710-6.
    • (2005) J Thromb Haemost , vol.3 , pp. 1710-1716
    • Dong, J.F.1
  • 18
    • 37249000281 scopus 로고    scopus 로고
    • Shear-induced disulfide bond formation regulates adhesion activity of von willebrand factor
    • Choi H, Aboulfatova K, Pownall HJ, Cook R, Dong JF. Shear-induced disulfide bond formation regulates adhesion activity of von willebrand factor. J Biol Chem 2007; 282: 35604-11.
    • (2007) J Biol Chem , vol.282 , pp. 35604-35611
    • Choi, H.1    Aboulfatova, K.2    Pownall, H.J.3    Cook, R.4    Dong, J.F.5
  • 21
    • 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: 1341-9.
    • (2001) J Exp Med , vol.193 , pp. 1341-1349
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 23
    • 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 1989; 256: H1635-44.
    • (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
  • 24
    • 28844490990 scopus 로고    scopus 로고
    • Recombinant CUB-1 domain polypeptide inhibits the cleavage of ULVWF strings by ADAMTS13 under flow conditions
    • Tao Z, Peng Y, Nolasco L, Cal S, Lopez-Otin C, Li R, Moake JL, Lopez JA, Dong JF. Recombinant CUB-1 domain polypeptide inhibits the cleavage of ULVWF strings by ADAMTS13 under flow conditions. Blood 2005; 106: 4139-45.
    • (2005) Blood , vol.106 , pp. 4139-4145
    • Tao, Z.1    Peng, Y.2    Nolasco, L.3    Cal, S.4    Lopez-Otin, C.5    Li, R.6    Moake, J.L.7    Lopez, J.A.8    Dong, J.F.9
  • 25
    • 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 1986; 78: 1456-61.
    • (1986) 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
  • 27
    • 57749177100 scopus 로고    scopus 로고
    • ADAMTS-13 cleaves long von Willebrand factor multimeric strings anchored to endothelial cells in the absence of flow, platelets or conformation-altering chemicals
    • Turner N, Nolasco L, Dong JF, Moake J. ADAMTS-13 cleaves long von Willebrand factor multimeric strings anchored to endothelial cells in the absence of flow, platelets or conformation-altering chemicals. J Thromb Haemost 2009; 7: 229-32.
    • (2009) J Thromb Haemost , vol.7 , pp. 229-232
    • Turner, N.1    Nolasco, L.2    Dong, J.F.3    Moake, J.4
  • 28
    • 0014060675 scopus 로고
    • Determination of sulfhydryl groups with 2,2'- or 4,4'-dithiodipyridine
    • Grassetti DR, Murray JF Jr. Determination of sulfhydryl groups with 2, 2'- or 4, 4'-dithiodipyridine. Arch Biochem Biophys 1967; 119: 41-9.
    • (1967) Arch Biochem Biophys , vol.119 , pp. 41-49
    • Grassetti, D.R.1    Murray Jr, J.F.2
  • 29
    • 0014687501 scopus 로고
    • The use of 2,2'-dithiobis-(5-nitropyridine) as a selective reagent for the detection of thiols
    • Grassetti DR, Murray JF Jr. The use of 2, 2'-dithiobis-(5-nitropyridine) as a selective reagent for the detection of thiols. J Chromatogr 1969; 41: 121-3.
    • (1969) J Chromatogr , vol.41 , pp. 121-123
    • Grassetti, D.R.1    Murray Jr, J.F.2
  • 31
    • 34548834974 scopus 로고    scopus 로고
    • The cooperative activity between the carboxyl-terminal TSP1 repeats and the CUB domains of ADAMTS13 is crucial for recognition of von Willebrand factor under flow
    • Zhang P, Pan W, Rux AH, Sachais BS, Zheng XL. The cooperative activity between the carboxyl-terminal TSP1 repeats and the CUB domains of ADAMTS13 is crucial for recognition of von Willebrand factor under flow. Blood 2007; 110: 1887-94.
    • (2007) Blood , vol.110 , pp. 1887-1894
    • Zhang, P.1    Pan, W.2    Rux, A.H.3    Sachais, B.S.4    Zheng, X.L.5
  • 32
    • 22044446207 scopus 로고    scopus 로고
    • Cleavage of ultra-large multimers of Von Willebrand factor by C-terminal truncated mutants of ADAMTS-13 under flow
    • Tao Z, Wang Y, Choi H, Bernardo A, Nishio K, Sadler JE, Lopez JA, Dong JF. Cleavage of ultra-large multimers of Von Willebrand factor by C-terminal truncated mutants of ADAMTS-13 under flow. Blood 2005; 106: 141-3.
    • (2005) Blood , vol.106 , pp. 141-143
    • Tao, Z.1    Wang, Y.2    Choi, H.3    Bernardo, A.4    Nishio, K.5    Sadler, J.E.6    Lopez, J.A.7    Dong, J.F.8
  • 33
    • 0042530524 scopus 로고    scopus 로고
    • Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13
    • Zheng X, Nishio K, Majerus EM, Sadler JE. Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13. J Biol Chem 2003; 278: 30136-41.
    • (2003) J Biol Chem , vol.278 , pp. 30136-30141
    • Zheng, X.1    Nishio, K.2    Majerus, E.M.3    Sadler, J.E.4
  • 35
    • 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 USA 2002; 99: 425-30.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 425-430
    • Savage, B.1    Sixma, J.J.2    Ruggeri, Z.M.3
  • 37
    • 0026766487 scopus 로고
    • Shear stress-induced von Willebrand factor binding to platelet glycoprotein Ib initiates calcium influx associated with aggregation
    • Chow TW, Hellums JD, Moake JL, Kroll MH. Shear stress-induced von Willebrand factor binding to platelet glycoprotein Ib initiates calcium influx associated with aggregation. Blood 1992; 80: 113-20.
    • (1992) Blood , vol.80 , pp. 113-120
    • Chow, T.W.1    Hellums, J.D.2    Moake, J.L.3    Kroll, M.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.