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Volumn 287, Issue 18, 2012, Pages 14579-14585

N-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING PLATELETS; AMINO ACID SEQUENCE; BINDING CAPACITIES; COATED SURFACE; CONFORMATIONAL CHANGE; DOMAIN COMPLEXES; FLANKING REGIONS; GLYCOPROTEIN (GP); HIGH SHEAR; HIGH SHEAR RATE; N-TERMINALS; PLATELET ACTIVATION; PLATELET ADHESION; STRUCTURAL CONFORMATIONS; STRUCTURAL STABILIZATION; SURFACE AREA; THROMBUS FORMATION; VON WILLEBRAND FACTOR; WHOLE BLOOD;

EID: 84860376548     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.348573     Document Type: Article
Times cited : (41)

References (33)
  • 1
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage, B., Saldívar, E., and Ruggeri, Z. M. (1996) Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell 84, 289-297
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Saldívar, E.2    Ruggeri, Z.M.3
  • 3
    • 0029919411 scopus 로고    scopus 로고
    • Adhesion of platelets to surface-bound fibrinogen under flow
    • Zaidi, T. N., McIntire, L. V., Farrell, D. H., and Thiagarajan, P. (1996) Adhesion of platelets to surface-bound fibrinogen under flow. Blood 88, 2967-2972
    • (1996) Blood , vol.88 , pp. 2967-2972
    • Zaidi, T.N.1    McIntire, L.V.2    Farrell, D.H.3    Thiagarajan, P.4
  • 4
    • 77954921247 scopus 로고    scopus 로고
    • Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibß and platelet activation under shear stress
    • Auton, M., Sowa, K. E., Smith, S. M., Sedlák, E., Vijayan, K. V., and Cruz, M. A. (2010) Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibß and platelet activation under shear stress. J. Biol. Chem. 285, 22831-22839
    • (2010) J. Biol. Chem. , vol.285 , pp. 22831-22839
    • Auton, M.1    Sowa, K.E.2    Smith, S.M.3    Sedlák, E.4    Vijayan, K.V.5    Cruz, M.A.6
  • 5
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler, J. E. (1998) Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 67, 395-424
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 7
    • 0022764677 scopus 로고
    • Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit
    • Verweij, C. L., Diergaarde, P. J., Hart, M., and Pannekoek, H. (1986) Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit. EMBO J. 5, 1839-1847
    • (1986) EMBO J. , vol.5 , pp. 1839-1847
    • Verweij, C.L.1    Diergaarde, P.J.2    Hart, M.3    Pannekoek, H.4
  • 8
    • 0027427962 scopus 로고
    • The interaction of the von Willebrand factor-A1 domain with platelet glycoprotein Ib/IX: The role of glycosylation and disulfide bonding in a monomeric recombinant A1 domain protein
    • Cruz, M. A., Handin, R. I., and Wise, R. J. (1993) The interaction of the von Willebrand factor-A1 domain with platelet glycoprotein Ib/IX: the role of glycosylation and disulfide bonding in a monomeric recombinant A1 domain protein. J. Biol. Chem. 268, 21238-21245
    • (1993) J. Biol. Chem. , vol.268 , pp. 21238-21245
    • Cruz, M.A.1    Handin, R.I.2    Wise, R.J.3
  • 9
    • 33645565906 scopus 로고    scopus 로고
    • The interaction of von Willebrand factor-A1 domain with collagen: Mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen
    • Morales, L. D., Martin, C., and Cruz, M. A. (2006) The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen. J. Thromb. Haemost. 4, 417-425
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 417-425
    • Morales, L.D.1    Martin, C.2    Cruz, M.A.3
  • 10
    • 0026066834 scopus 로고
    • The binding domain of von Willebrand factor to sulfatides is distinct from those interacting with glycoprotein Ib, heparin, and collagen and resides between amino acid residues Leu-512 and Lys-673
    • Christophe, O., Obert, B., Meyer, D., and Girma, J. P. (1991) The binding domain of von Willebrand factor to sulfatides is distinct from those interacting with glycoprotein Ib, heparin, and collagen and resides between amino acid residues Leu-512 and Lys-673. Blood 78, 2310-2317
    • (1991) Blood , vol.78 , pp. 2310-2317
    • Christophe, O.1    Obert, B.2    Meyer, D.3    Girma, J.P.4
  • 11
    • 33748747136 scopus 로고    scopus 로고
    • Von Willebrand factor A1 domain can adequately substitute for A3 domain in recruitment of flowing platelets to collagen
    • Bonnefoy, A., Romijn, R. A., Vandervoort, P. A., Van Rompaey, I, Vermylen, J., and Hoylaerts, M. F. (2006) von Willebrand factor A1 domain can adequately substitute for A3 domain in recruitment of flowing platelets to collagen. J. Thromb. Haemost. 4, 2151-2161
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 2151-2161
    • Bonnefoy, A.1    Romijn, R.A.2    Vandervoort, P.A.3    Van Rompaey, I.4    Vermylen, J.5    Hoylaerts, M.F.6
  • 12
    • 0028914676 scopus 로고
    • Interaction of the von Willebrand factor (vWF) with collagen: Localization of the primary collagen-binding site by analysis of recombinant vWF A domain polypeptides
    • Cruz, M. A., Yuan, H., Lee, J. R., Wise, R. J., and Handin, R. I. (1995) Interaction of the von Willebrand factor (vWF) with collagen: localization of the primary collagen-binding site by analysis of recombinant vWF A domain polypeptides. J. Biol. Chem. 270, 10822-10827
    • (1995) J. Biol. Chem. , vol.270 , pp. 10822-10827
    • Cruz, M.A.1    Yuan, H.2    Lee, J.R.3    Wise, R.J.4    Handin, R.I.5
  • 14
    • 0025044664 scopus 로고
    • Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor
    • Dent, J. A., Berkowitz, S. D., Ware, J., Kasper, C. K., and Ruggeri, Z. M. (1990) Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor. Proc. Natl. Acad. Sci. U.S.A. 87, 6306-6310
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6306-6310
    • Dent, J.A.1    Berkowitz, S.D.2    Ware, J.3    Kasper, C.K.4    Ruggeri, Z.M.5
  • 15
    • 6944244008 scopus 로고    scopus 로고
    • ADAMTS-13 activity in plasma is rapidly measured by a new ELISA method that uses recombinant VWF-A2 domain as substrate
    • Whitelock, J. L., Nolasco, L., Bernardo, A., Moake, J., Dong, J. F., and Cruz, M. A. (2004) ADAMTS-13 activity in plasma is rapidly measured by a new ELISA method that uses recombinant VWF-A2 domain as substrate. J. Thromb. Haemost. 2, 485-491
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 485-491
    • Whitelock, J.L.1    Nolasco, L.2    Bernardo, A.3    Moake, J.4    Dong, J.F.5    Cruz, M.A.6
  • 16
    • 0034705544 scopus 로고    scopus 로고
    • Mapping the glycoprotein Ib-binding site in the von Willebrand factor A1 domain
    • Cruz, M. A., Diacovo, T. G., Emsley, J., Liddington, R., and Handin, R. I. (2000) Mapping the glycoprotein Ib-binding site in the von Willebrand factor A1 domain. J. Biol. Chem. 275, 19098-19105
    • (2000) J. Biol. Chem. , vol.275 , pp. 19098-19105
    • Cruz, M.A.1    Diacovo, T.G.2    Emsley, J.3    Liddington, R.4    Handin, R.I.5
  • 17
    • 0347533937 scopus 로고    scopus 로고
    • Evaluation of ADAMTS- 13 activity in plasma using recombinant von Willebrand factor A2 domain polypeptide as substrate
    • Cruz, M. A., Whitelock, J., and Dong, J. F. (2003) Evaluation of ADAMTS- 13 activity in plasma using recombinant von Willebrand factor A2 domain polypeptide as substrate. Thromb. Haemost. 90, 1204-1209
    • (2003) Thromb. Haemost. , vol.90 , pp. 1204-1209
    • Cruz, M.A.1    Whitelock, J.2    Dong, J.F.3
  • 18
    • 33846592202 scopus 로고    scopus 로고
    • Conformational stability and domain unfolding of the von Willebrand factor A domains
    • Auton, M., Cruz, M. A., and Moake, J. (2007) Conformational stability and domain unfolding of the von Willebrand factor A domains. J. Mol. Biol. 366, 986-1000
    • (2007) J. Mol. Biol. , vol.366 , pp. 986-1000
    • Auton, M.1    Cruz, M.A.2    Moake, J.3
  • 19
    • 0038446690 scopus 로고    scopus 로고
    • Aspects of hydrodynamic shear regulating shear-induced platelet activation and self-association of von Willebrand factor in suspension
    • Shankaran, H., Alexandridis, P., and Neelamegham, S. (2003) Aspects of hydrodynamic shear regulating shear-induced platelet activation and self-association of von Willebrand factor in suspension. Blood 101, 2637-2645
    • (2003) Blood , vol.101 , pp. 2637-2645
    • Shankaran, H.1    Alexandridis, P.2    Neelamegham, S.3
  • 20
    • 60249092963 scopus 로고    scopus 로고
    • Clinical and molecular predictors of thrombocytopenia and risk of bleeding in patients with von Willebrand disease type 2B: A cohort study of 67 patients
    • Federici, A. B., Mannucci, P. M., Castaman, G., Baronciani, L., Bucciarelli, P., Canciani, M. T., Pecci, A., Lenting, P. J., and De Groot, P. G. (2009) Clinical and molecular predictors of thrombocytopenia and risk of bleeding in patients with von Willebrand disease type 2B: a cohort study of 67 patients. Blood 113, 526-534
    • (2009) Blood , vol.113 , pp. 526-534
    • Federici, A.B.1    Mannucci, P.M.2    Castaman, G.3    Baronciani, L.4    Bucciarelli, P.5    Canciani, M.T.6    Pecci, A.7    Lenting, P.J.8    De Groot, P.G.9
  • 21
    • 0027398579 scopus 로고
    • A role for von Willebrand factor proline residues 702-704 in ristocetin-mediated binding to platelet glycoprotein Ib
    • Azuma, H., Sugimoto, M., Ruggeri, Z. M., and Ware, J. (1993) A role for von Willebrand factor proline residues 702-704 in ristocetin-mediated binding to platelet glycoprotein Ib. Thromb. Haemost. 69, 192-196
    • (1993) Thromb. Haemost. , vol.69 , pp. 192-196
    • Azuma, H.1    Sugimoto, M.2    Ruggeri, Z.M.3    Ware, J.4
  • 22
    • 33646194222 scopus 로고    scopus 로고
    • Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V
    • Ulrichts, H., Udvardy, M., Lenting, P. J., Pareyn, I., Vandeputte, N., Vanhoorelbeke, K., and Deckmyn, H. (2006) Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V. J. Biol. Chem. 281, 4699-4707
    • (2006) J. Biol. Chem. , vol.281 , pp. 4699-4707
    • Ulrichts, H.1    Udvardy, M.2    Lenting, P.J.3    Pareyn, I.4    Vandeputte, N.5    Vanhoorelbeke, K.6    Deckmyn, H.7
  • 25
    • 34250692515 scopus 로고    scopus 로고
    • Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibα
    • Martin, C., Morales, L. D., and Cruz, M. A. (2007) Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibα. J. Thromb. Haemost. 5, 1363-1370
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1363-1370
    • Martin, C.1    Morales, L.D.2    Cruz, M.A.3
  • 26
    • 14944369328 scopus 로고    scopus 로고
    • The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor α2β1 to bind collagen: Activation-dependent conformational change of the α2-I domain
    • Cruz, M. A., Chen, J., Whitelock, J. L., Morales, L. D., and López, J. A. (2005) The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor α2β1 to bind collagen: activation-dependent conformational change of the α2-I domain. Blood 105, 1986-1991
    • (2005) Blood , vol.105 , pp. 1986-1991
    • Cruz, M.A.1    Chen, J.2    Whitelock, J.L.3    Morales, L.D.4    López, J.A.5
  • 27
    • 75649138819 scopus 로고    scopus 로고
    • Force-induced cleavage of single VWFA1A2A3 tri-domains by ADAMTS-13
    • Wu, T., Lin, J., Cruz, M. A., Dong, J. F., and Zhu, C. (2010) Force-induced cleavage of single VWFA1A2A3 tri-domains by ADAMTS-13. Blood 115, 370-378
    • (2010) Blood , vol.115 , pp. 370-378
    • Wu, T.1    Lin, J.2    Cruz, M.A.3    Dong, J.F.4    Zhu, C.5
  • 28
    • 77958168869 scopus 로고    scopus 로고
    • The mechanism of VWF-mediated platelet GPIbα binding
    • Auton, M., Zhu, C., and Cruz, M. A. (2010) The mechanism of VWF-mediated platelet GPIbα binding. Biophys. J. 99, 1192-1201
    • (2010) Biophys. J. , vol.99 , pp. 1192-1201
    • Auton, M.1    Zhu, C.2    Cruz, M.A.3
  • 29
    • 81055131933 scopus 로고    scopus 로고
    • Shear stress-induced unfolding of VWF accelerates oxidation of key methionine residues in the A1A2A3 region
    • Fu, X., Chen, J., Gallagher, R., Zheng, Y., Chung, D. W., and López, J. A. (2011) Shear stress-induced unfolding of VWF accelerates oxidation of key methionine residues in the A1A2A3 region. Blood 118, 5283-5291
    • (2011) Blood , vol.118 , pp. 5283-5291
    • Fu, X.1    Chen, J.2    Gallagher, R.3    Zheng, Y.4    Chung, D.W.5    López, J.A.6
  • 30
    • 0026098060 scopus 로고
    • Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin- and botrocetin-induced vWF binding to platelet glycoprotein Ib
    • Fujimura, Y., Usami, Y., Titani, K., Niinomi, K., Nishio, K., Takase, T., Yoshioka, A., and Fukui, H. (1991) Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin- and botrocetin-induced vWF binding to platelet glycoprotein Ib. Blood 77, 113-120
    • (1991) Blood , vol.77 , pp. 113-120
    • Fujimura, Y.1    Usami, Y.2    Titani, K.3    Niinomi, K.4    Nishio, K.5    Takase, T.6    Yoshioka, A.7    Fukui, H.8
  • 31
    • 0025119629 scopus 로고
    • Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib
    • Girma, J. P., Takahashi, Y., Yoshioka, A., Diaz, J., and Meyer, D. (1990) Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib. Thromb. Haemost. 64, 326-332
    • (1990) Thromb. Haemost. , vol.64 , pp. 326-332
    • Girma, J.P.1    Takahashi, Y.2    Yoshioka, A.3    Diaz, J.4    Meyer, D.5
  • 32
    • 0027314540 scopus 로고
    • Analysis of structure-function relationships in the platelet membrane glycoprotein Ib-binding domain of von Willebrand factor by expression of deletion mutants
    • Sugimoto, M., Dent, J., McClintock, R., Ware, J., and Ruggeri, Z. M. (1993) Analysis of structure-function relationships in the platelet membrane glycoprotein Ib-binding domain of von Willebrand factor by expression of deletion mutants. J. Biol. Chem. 268, 12185-12192
    • (1993) J. Biol. Chem. , vol.268 , pp. 12185-12192
    • Sugimoto, M.1    Dent, J.2    McClintock, R.3    Ware, J.4    Ruggeri, Z.M.5
  • 33
    • 0029042992 scopus 로고
    • Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib: Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor
    • Matsushita, T., and Sadler, J. E. (1995) Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib: charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor. J. Biol. Chem. 270, 13406-13414
    • (1995) J. Biol. Chem. , vol.270 , pp. 13406-13414
    • Matsushita, T.1    Sadler, J.E.2


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