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Volumn 288, Issue 1, 2013, Pages 393-400

Distinct roles of ser-764 and lys-773 at the N terminus of von Willebrand factor in complex assembly with coagulation factor VIII

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; AMINO GROUP; BINDING MECHANISMS; CHEMICALLY MODIFIED; COAGULATION FACTOR; COMPLEX ASSEMBLY; COMPLEX FORMATIONS; FOOTPRINTING; IN-VIVO; LIGHT CHAIN; LYSINE RESIDUES; N-TERMINALS; NANO-LC-MS; SURFACE PLASMONS; VON WILLEBRAND FACTOR;

EID: 84872088575     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.400572     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 79960628104 scopus 로고    scopus 로고
    • Von Willebrand factor: The complex molecular genetics of a multidomain and multifunctional protein
    • Schneppenheim, R., and Budde, U. (2011) von Willebrand factor: the complex molecular genetics of a multidomain and multifunctional protein. J. Thromb. Haemost. 9, 209-215
    • (2011) J. Thromb. Haemost. , vol.9 , pp. 209-215
    • Schneppenheim, R.1    Budde, U.2
  • 2
    • 33646839132 scopus 로고    scopus 로고
    • Factor VIII structure and function
    • Fay, P. J. (2006) Factor VIII structure and function. Int. J. Hematol. 83, 103-108
    • (2006) Int. J. Hematol. , vol.83 , pp. 103-108
    • Fay, P.J.1
  • 4
    • 0028239173 scopus 로고
    • Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII
    • Lenting, P. J., Donath, M. J., van Mourik, J. A., and Mertens, K. (1994) Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII. J. Biol. Chem. 269, 7150-7155 (Pubitemid 24217900)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7150-7155
    • Lenting, P.J.1    Donath, M.-J.S.H.2    Van Mourik, J.A.3    Mertens, K.4
  • 5
    • 67649651890 scopus 로고    scopus 로고
    • Factor VIII-von Willebrand factor binding defects in autosomal recessive von Willebrand disease type Normandy and in mild hemophilia A. New insights into factor VIII-von Willebrand factor interactions
    • Jacquemin, M. (2009) Factor VIII-von Willebrand factor binding defects in autosomal recessive von Willebrand disease type Normandy and in mild hemophilia A. New insights into factor VIII-von Willebrand factor interactions. Acta Haematol. 121, 102-105
    • (2009) Acta Haematol. , vol.121 , pp. 102-105
    • Jacquemin, M.1
  • 6
    • 0022296676 scopus 로고
    • Purified human factor VIII procoagulant protein: Comparative hemostatic response after infusions into hemophilic and von Willebrand disease dogs
    • Brinkhous, K. M., Sandberg, H., Garris, J. B., Mattsson, C., Palm, M., Griggs, T., and Read, M. S. (1985) Purified human factor VIII procoagulant protein: comparative hemostatic response after infusions into hemophilic and von Willebrand disease dogs. Proc. Natl. Acad. Sci. U.S.A. 82, 8752-8756 (Pubitemid 16101122)
    • (1985) Proceedings of the National Academy of Sciences of the United States of America , vol.82 , Issue.24 , pp. 8752-8756
    • Brinkhous, K.M.1    Sandberg, H.2    Garris, J.B.3
  • 8
    • 0023677854 scopus 로고
    • Association of the factor VIII light chain with von Willebrand factor
    • Lollar, P., Hill-Eubanks, D. C., and Parker, C. G. (1988) Association of the factor VIII light chain with von Willebrand factor. J. Biol. Chem. 263, 10451-10455
    • (1988) J. Biol. Chem. , vol.263 , pp. 10451-10455
    • Lollar, P.1    Hill-Eubanks, D.C.2    Parker, C.G.3
  • 9
    • 0030800963 scopus 로고    scopus 로고
    • The acidic region of the factor VIII light chain and the C2 domain together form the high affinity binding site for von Willebrand factor
    • DOI 10.1074/jbc.272.29.18007
    • Saenko, E. L., and Scandella, D. (1997) The acidic region of the factor VIII light chain and the C2 domain together form the high affinity binding site for von Willebrand factor. J. Biol. Chem. 272, 18007-18014 (Pubitemid 27306379)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18007-18014
    • Saenko, E.L.1    Scandella, D.2
  • 10
    • 0023922071 scopus 로고
    • 1684of the factor VIII light chain induces antibodies which inhibit binding of factor VIII to von Willebrand factor
    • 1684 of the factor VIII light chain induces antibodies which inhibit binding of factor VIII to von Willebrand factor. J. Biol. Chem. 263, 5230-5234
    • (1988) J. Biol. Chem. , vol.263 , pp. 5230-5234
    • Foster, P.A.1    Fulcher, C.A.2    Houghten, R.A.3    Zimmerman, T.S.4
  • 12
    • 79953084961 scopus 로고    scopus 로고
    • A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function
    • Lü, J., Pipe, S. W., Miao, H., Jacquemin, M., and Gilbert, G. E. (2011) A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function. Blood 117, 3181-3189
    • (2011) Blood , vol.117 , pp. 3181-3189
    • Lü, J.1    Pipe, S.W.2    Miao, H.3    Jacquemin, M.4    Gilbert, G.E.5
  • 13
    • 70449709337 scopus 로고    scopus 로고
    • Factor VIII C1 domain residues Lys2092 and Phe2093 contribute to membrane binding and cofactor activity
    • Meems, H., Meijer, A. B., Cullinan, D. B., Mertens, K., and Gilbert, G. E. (2009) Factor VIII C1 domain residues Lys2092 and Phe2093 contribute to membrane binding and cofactor activity. Blood 114, 3938-3946
    • (2009) Blood , vol.114 , pp. 3938-3946
    • Meems, H.1    Meijer, A.B.2    Cullinan, D.B.3    Mertens, K.4    Gilbert, G.E.5
  • 14
    • 67849097380 scopus 로고    scopus 로고
    • Von Willebrand factor assembly and secretion
    • Sadler, J. E. (2009) von Willebrand factor assembly and secretion. J. Thromb. Haemost. 7, 24-27
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 24-27
    • Sadler, J.E.1
  • 15
    • 84864055963 scopus 로고    scopus 로고
    • Sequence and structure relationships within von Willebrand factor
    • Zhou, Y. F., Eng, E. T., Zhu, J., Lu, C., Walz, T., and Springer, T. A. (2012) Sequence and structure relationships within von Willebrand factor. Blood 120, 449-458
    • (2012) Blood , vol.120 , pp. 449-458
    • Zhou, Y.F.1    Eng, E.T.2    Zhu, J.3    Lu, C.4    Walz, T.5    Springer, T.A.6
  • 16
    • 0023217139 scopus 로고
    • A major factor VIII binding domain resides within the amino-terminal 272 amino acid residues of von Willebrand factor
    • Foster, P. A., Fulcher, C. A., Marti, T., Titani, K., and Zimmerman, T. S. (1987) A major factor VIII binding domain resides within the amino-terminal 272 amino acid residues of von Willebrand factor. J. Biol. Chem. 262, 8443-8446
    • (1987) J. Biol. Chem. , vol.262 , pp. 8443-8446
    • Foster, P.A.1    Fulcher, C.A.2    Marti, T.3    Titani, K.4    Zimmerman, T.S.5
  • 17
    • 0023553491 scopus 로고
    • Localization of a factor VIII binding domain on a 34 kilodalton fragment of the N-terminal portion of von Willebrand factor
    • Takahashi, Y., Kalafatis, M., Girma, J. P., Sewerin, K., Andersson, L. O., and Meyer, D. (1987) Localization of a factor VIII binding domain on a 34 kilodalton fragment of the N-terminal portion of von Willebrand factor. Blood 70, 1679-1682 (Pubitemid 18026187)
    • (1987) Blood , vol.70 , Issue.5 , pp. 1679-1682
    • Takahashi, Y.1    Kalafatis, M.2    Girma, J.-P.3    Sewerin, K.4    Andersson, L.-O.5    Meyer, D.6
  • 18
    • 38949168866 scopus 로고    scopus 로고
    • The tertiary structure and domain organization of coagulation factor VIII
    • DOI 10.1182/blood-2007-08-109918
    • Shen, B. W., Spiegel, P. C., Chang, C. H., Huh, J. W., Lee, J. S., Kim, J., Kim, Y. H., and Stoddard, B. L. (2008) The tertiary structure and domain organization of coagulation factor VIII. Blood 111, 1240-1247 (Pubitemid 351213406)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1240-1247
    • Shen, B.W.1    Spiegel, P.C.2    Chang, C.-H.3    Huh, J.-W.4    Lee, J.-S.5    Kim, J.6    Kim, Y.-H.7    Stoddard, B.L.8
  • 19
    • 84857287653 scopus 로고    scopus 로고
    • Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII
    • Bloem, E., Meems, H., van den Biggelaar, M., van der Zwaan, C., Mertens, K., and Meijer, A. B. (2012) Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII. J. Biol. Chem. 287, 5775-5783
    • (2012) J. Biol. Chem. , vol.287 , pp. 5775-5783
    • Bloem, E.1    Meems, H.2    Van Den Biggelaar, M.3    Van Der Zwaan, C.4    Mertens, K.5    Meijer, A.B.6
  • 20
    • 80052332355 scopus 로고    scopus 로고
    • Storage of factor VIII variants with impaired von Willebrand factor binding in Weibel-Palade bodies in endothelial cells
    • van den Biggelaar, M., Bouwens, E. A., Voorberg, J., and Mertens, K. (2011) Storage of factor VIII variants with impaired von Willebrand factor binding in Weibel-Palade bodies in endothelial cells. PLoS ONE 6, e24163
    • (2011) PLoS ONE , vol.6
    • Van Den Biggelaar, M.1    Bouwens, E.A.2    Voorberg, J.3    Mertens, K.4
  • 21
    • 0022354412 scopus 로고
    • The role of factor VIII in the activation of human blood coagulation factor X by activated factor IX
    • Mertens, K., van Wijngaarden, A., and Bertina, R. M. (1985) The role of factor VIII in the activation of human blood coagulation factor X by activated factor IX. Thromb. Haemost. 54, 654-660 (Pubitemid 16195312)
    • (1985) Thrombosis and Haemostasis , vol.54 , Issue.3 , pp. 654-660
    • Mertens, K.1    Van Wijngaarden, A.2    Bertina, R.M.3
  • 22
    • 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, H. V., Sakariassen, K. S., Scholte, B. J., Veerman, E. C., van der Kwast, T. H., de Groot, P. G., Sixma, J. J., and van Mourik, J. A. (1984) Characterization of 25 monoclonal antibodies to factor VIII-von Willebrand factor: relationship between ristocetin-induced platelet aggregation and platelet adherence to subendothelium. Blood 63, 1408-1415 (Pubitemid 14120388)
    • (1984) Blood , vol.63 , Issue.6 , pp. 1408-1415
    • Stel, H.V.1    Sakariassen, K.S.2    Scholte, B.J.3
  • 23
    • 79957975266 scopus 로고    scopus 로고
    • HLA-DR-presented peptide repertoires derived from human monocyte-derived dendritic cells pulsed with blood coagulation factor VIII
    • van Haren, S. D., Herczenik, E., ten Brinke, A., Mertens, K., Voorberg, J., and Meijer, A. B. (2011) HLA-DR-presented peptide repertoires derived from human monocyte-derived dendritic cells pulsed with blood coagulation factor VIII. Mol. Cell Proteomics 10, M110.002246
    • (2011) Mol. Cell Proteomics , vol.10
    • Van Haren, S.D.1    Herczenik, E.2    Ten Brinke, A.3    Mertens, K.4    Voorberg, J.5    Meijer, A.B.6
  • 24
    • 74849138649 scopus 로고    scopus 로고
    • Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags
    • Dayon, L., Pasquarello, C., Hoogland, C., Sanchez, J. C., and Scherl, A. (2010) Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags. J. Proteomics 73, 769-777
    • (2010) J. Proteomics , vol.73 , pp. 769-777
    • Dayon, L.1    Pasquarello, C.2    Hoogland, C.3    Sanchez, J.C.4    Scherl, A.5
  • 26
    • 63849281084 scopus 로고    scopus 로고
    • Intracellular cotrafficking of factor VIII and von Willebrand factor type 2N variants to storage organelles
    • van den Biggelaar, M., Meijer, A. B., Voorberg, J., and Mertens, K. (2009) Intracellular cotrafficking of factor VIII and von Willebrand factor type 2N variants to storage organelles. Blood 113, 3102-3109
    • (2009) Blood , vol.113 , pp. 3102-3109
    • Van Den Biggelaar, M.1    Meijer, A.B.2    Voorberg, J.3    Mertens, K.4
  • 27
    • 0028241067 scopus 로고
    • The activation of human blood coagulation factor X on the surface of endothelial cells: A comparison with various vascular cells, platelets and monocytes
    • Brinkman, H. J., Mertens, K., Holthuis, J., Zwart-Huinink, L. A., Grijm, K., and van Mourik, J. A. (1994) The activation of human blood coagulation factor X on the surface of endothelial cells: a comparison with various vascular cells, platelets and monocytes. Br. J. Haematol. 87, 332-342 (Pubitemid 24204736)
    • (1994) British Journal of Haematology , vol.87 , Issue.2 , pp. 332-342
    • Brinkman, H.-J.M.1    Mertens, K.2    Holthuis, J.3    Zwart-Huinink, L.A.4    Grijm, K.5    Van Mourik, J.A.6
  • 28
    • 0032528532 scopus 로고    scopus 로고
    • Binding of factor VIII to von Willebrand factor is enabled by cleavage of the von Willebrand factor propeptide and enhanced by formation of disulfide-linked multimers
    • Bendetowicz, A. V., Morris, J. A., Wise, R. J., Gilbert, G. E., and Kaufman, R. J. (1998) Binding of factor VIII to von Willebrand factor is enabled by cleavage of the von Willebrand factor propeptide and enhanced by formation of disulfide-linked multimers. Blood 92, 529-538 (Pubitemid 28323716)
    • (1998) Blood , vol.92 , Issue.2 , pp. 529-538
    • Bendetowicz, A.V.1    Morris, J.A.2    Wise, R.J.3    Gilbert, G.E.4    Kaufman, R.J.5
  • 29
    • 0025123702 scopus 로고
    • Von Willebrand factor is a cofactor for thrombin-catalyzed cleavage of the factor VIII light chain
    • Hill-Eubanks, D. C., and Lollar, P. (1990) von Willebrand factor is a cofactor for thrombin-catalyzed cleavage of the factor VIII light chain. J. Biol. Chem. 265, 17854-17858
    • (1990) J. Biol. Chem. , vol.265 , pp. 17854-17858
    • Hill-Eubanks, D.C.1    Lollar, P.2
  • 32
    • 0034129479 scopus 로고    scopus 로고
    • NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): Structural similarity with ascaris protease inhibitors
    • Cierpicki, T., Bania, J., and Otlewski, J. (2000) NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors. Protein Sci. 9, 976-984 (Pubitemid 30353339)
    • (2000) Protein Science , vol.9 , Issue.5 , pp. 976-984
    • Cierpicki, T.1    Bania, J.2    Otlewski, J.3
  • 35
    • 0026065681 scopus 로고
    • The pro-polypeptide of von Willebrand factor is required for the formation of a functional factor VIII-binding site on mature von Willebrand factor
    • Leyte, A., Voorberg, J., Van Schijndel, H. B., Duim, B., Pannekoek, H., and Van Mourik, J. A. (1991) The pro-polypeptide of von Willebrand factor is required for the formation of a functional factor VIII-binding site on mature von Willebrand factor. Biochem. J. 274, 257-261
    • (1991) Biochem. J. , vol.274 , pp. 257-261
    • Leyte, A.1    Voorberg, J.2    Van Schijndel, H.B.3    Duim, B.4    Pannekoek, H.5    Van Mourik, J.A.6
  • 36
    • 41449117525 scopus 로고    scopus 로고
    • Crystal Structure of Human Factor VIII: Implications for the Formation of the Factor IXa-Factor VIIIa Complex
    • DOI 10.1016/j.str.2008.03.001, PII S0969212608000968
    • Ngo, J. C., Huang, M., Roth, D. A., Furie, B. C., and Furie, B. (2008) Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex. Structure 16, 597-606 (Pubitemid 351458707)
    • (2008) Structure , vol.16 , Issue.4 , pp. 597-606
    • Ngo, J.C.K.1    Huang, M.2    Roth, D.A.3    Furie, B.C.4    Furie, B.5


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