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Volumn 100, Issue 2, 2011, Pages 304-312

GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease

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EID: 78751685657     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.11.084     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 51349164922 scopus 로고    scopus 로고
    • Function of von Willebrand factor in haemostasis and thrombosis
    • Reininger, A. J. 2008. Function of von Willebrand factor in haemostasis and thrombosis. Haemophilia. 14 (Suppl 5):11-26.
    • (2008) Haemophilia , vol.14 , Issue.5 SUPPL. , pp. 11-26
    • Reininger, A.J.1
  • 2
    • 33748802581 scopus 로고    scopus 로고
    • Update on the pathophysiology and classification of von Willebrand disease: A report of the Subcommittee on von Willebrand factor
    • Working Party on von Willebrand Disease Classification
    • Sadler, J. E., U. Budde,..., Working Party on von Willebrand Disease Classification. 2006. Update on the pathophysiology and classification of von Willebrand disease: a report of the Subcommittee on von Willebrand Factor. J. Thromb. Haemost. 4:2103-2114.
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 2103-2114
    • Sadler, J.E.1    Budde, U.2
  • 3
    • 0036183554 scopus 로고    scopus 로고
    • Thrombotic thrombocytopenic purpura: The systemic clumping "plague"
    • Moake, J. L. 2002. Thrombotic thrombocytopenic purpura: the systemic clumping "plague". Annu. Rev. Med. 53:75-88.
    • (2002) Annu. Rev. Med. , vol.53 , pp. 75-88
    • Moake, J.L.1
  • 4
    • 0032483550 scopus 로고    scopus 로고
    • Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • Savage, B., F. Almus-Jacobs, and Z. M. Ruggeri. 1998. Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell. 94:657-666.
    • (1998) Cell. , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 6
    • 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., R. I. Handin, and R. J. Wise. 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
  • 7
    • 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., C. Martin, and M. A. Cruz. 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
  • 8
    • 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., R. A. Romijn,..., M. F. Hoylaerts. 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    Hoylaerts, M.F.3
  • 9
    • 0030970681 scopus 로고    scopus 로고
    • Von Willebrand factor binds to native collagen VI primarily via its A1 domain
    • Hoylaerts, M. F., H. Yamamoto,..., J. Vermylen. 1997. von Willebrand factor binds to native collagen VI primarily via its A1 domain. Biochem. J. 324:185-191.
    • (1997) Biochem. J. , vol.324 , pp. 185-191
    • Hoylaerts, M.F.1    Yamamoto, H.2    Vermylen, J.3
  • 10
    • 0023547037 scopus 로고
    • Localization of a collagen-interactive domain of human von Willebrand factor between amino acid residues Gly 911 and Glu 1, 365
    • Kalafatis, M., Y. Takahashi,..., D. Meyer. 1987. Localization of a collagen-interactive domain of human von Willebrand factor between amino acid residues Gly 911 and Glu 1, 365. Blood. 70:1577-1583.
    • (1987) Blood , vol.70 , pp. 1577-1583
    • Kalafatis, M.1    Takahashi, Y.2    Meyer, D.3
  • 11
    • 0029647484 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., H. Yuan,..., R. I. Handin. 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    Handin, R.I.3
  • 12
    • 0029960408 scopus 로고    scopus 로고
    • A3 domain is essential for interaction of von Willebrand factor with collagen type III
    • Lankhof, H., M. van Hoeij,..., J. J. Sixma. 1996. A3 domain is essential for interaction of von Willebrand factor with collagen type III. Thromb. Haemost. 75:950-958.
    • (1996) Thromb. Haemost. , vol.75 , pp. 950-958
    • Lankhof, H.1    Van Hoeij, M.2    Sixma, J.J.3
  • 13
    • 0036893186 scopus 로고    scopus 로고
    • ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
    • Dong, J. F., J. L. Moake,..., J. A. López. 2002. ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood. 100:4033-4039.
    • (2002) Blood , vol.100 , pp. 4033-4039
    • Dong, J.F.1    Moake, J.L.2    López, J.A.3
  • 14
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Iba and its complex with von Willebrand factor A1 domain
    • Huizinga, E. G., S. Tsuji,..., P. Gros. 2002. Structures of glycoprotein Iba and its complex with von Willebrand factor A1 domain. Science. 297:1176-1179.
    • (2002) Science , vol.297 , pp. 1176-1179
    • Huizinga, E.G.1    Tsuji, S.2    Gros, P.3
  • 15
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib
    • Emsley, J., M. Cruz,..., R. Liddington. 1998. Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib. J. Biol. Chem. 273:10396-10401.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Liddington, R.3
  • 16
    • 51349154185 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibα forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF
    • Yago, T., J. Lou,..., C. Zhu. 2008. Platelet glycoprotein Ibα forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF. J. Clin. Invest. 118:3195-3207.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3195-3207
    • Yago, T.1    Lou, J.2    Zhu, C.3
  • 17
    • 0026756331 scopus 로고
    • Von Willebrand disease type B: A missense mutation selectively abolishes ristocetininduced von Willebrand factor binding to platelet glycoprotein Ib
    • Rabinowitz, I., E. A. Tuley,..., J. E. Sadler. 1992. von Willebrand disease type B: a missense mutation selectively abolishes ristocetininduced von Willebrand factor binding to platelet glycoprotein Ib. Proc. Natl. Acad. Sci. USA. 89:9846-9849.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9846-9849
    • Rabinowitz, I.1    Tuley, E.A.2    Sadler, J.E.3
  • 18
    • 68949119686 scopus 로고    scopus 로고
    • Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbα
    • Auton, M., E. Sedlák,..., M. A. Cruz. 2009. Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbα. Biophys. J. 97:618-627.
    • (2009) Biophys. J. , vol.97 , pp. 618-627
    • Auton, M.1    Sedlák, E.2    Cruz, M.A.3
  • 19
    • 0030884913 scopus 로고    scopus 로고
    • The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling
    • Alon, R., S. Chen,..., T. A. Springer. 1997. The kinetics of L-selectin tethers and the mechanics of selectin-mediated rolling. J. Cell Biol. 138:1169-1180.
    • (1997) J. Cell. Biol. , vol.138 , pp. 1169-1180
    • Alon, R.1    Chen, S.2    Springer, T.A.3
  • 20
    • 4544238275 scopus 로고    scopus 로고
    • Catch bonds govern adhesion through L-selectin at threshold shear
    • Yago, T., J. Wu,..., R. P. McEver. 2004. Catch bonds govern adhesion through L-selectin at threshold shear. J. Cell Biol. 166:913-923.
    • (2004) J. Cell. Biol. , vol.166 , pp. 913-923
    • Yago, T.1    Wu, J.2    McEver, R.P.3
  • 21
    • 0036286198 scopus 로고    scopus 로고
    • Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: The GPIb (α)-vWF tether bond
    • Doggett, T. A., G. Girdhar,..., T. G. Diacovo. 2002. Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb (α)-vWF tether bond. Biophys. J. 83:194-205.
    • (2002) Biophys. J. , vol.83 , pp. 194-205
    • Doggett, T.A.1    Girdhar, G.2    Diacovo, T.G.3
  • 22
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • Marshall, B. T., M. Long,..., C. Zhu. 2003. Direct observation of catch bonds involving cell-adhesion molecules. Nature. 423:190-193.
    • (2003) Nature , vol.423 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Zhu, C.3
  • 23
    • 0346457092 scopus 로고    scopus 로고
    • Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan
    • Sarangapani, K. K., T. Yago,..., C. Zhu. 2004. Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan. J. Biol. Chem. 279:2291-2298.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2291-2298
    • Sarangapani, K.K.1    Yago, T.2    Zhu, C.3
  • 24
    • 0023917132 scopus 로고
    • The reaction-limited kinetics of membrane-to-surface adhesion and detachment
    • Dembo, M., D. C. Torney,..., D. Hammer. 1988. The reaction-limited kinetics of membrane-to-surface adhesion and detachment. Proc. R. Soc. Lond. B Biol. Sci. 234:55-83.
    • (1988) Proc. R. Soc. Lond. B. Biol. Sci. , vol.234 , pp. 55-83
    • Dembo, M.1    Torney, D.C.2    Hammer, D.3
  • 25
    • 33846805698 scopus 로고    scopus 로고
    • Adhesive dynamics simulations of the shear threshold effect for leukocytes
    • Caputo, K. E., D. Lee,..., D. A. Hammer. 2007. Adhesive dynamics simulations of the shear threshold effect for leukocytes. Biophys. J. 92:787-797.
    • (2007) Biophys. J. , vol.92 , pp. 787-797
    • Caputo, K.E.1    Lee, D.2    Hammer, D.A.3
  • 26
    • 0034705544 scopus 로고    scopus 로고
    • Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain
    • Cruz, M. A., T. G. Diacovo,..., R. I. Handin. 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    Handin, R.I.3
  • 27
    • 33846592202 scopus 로고    scopus 로고
    • Conformational stability and domain unfolding of the Von Willebrand factor A domains
    • Auton, M., M. A. Cruz, and J. Moake. 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
  • 28
    • 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 J. E. Sadler. 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
  • 29
    • 0031974270 scopus 로고    scopus 로고
    • Platelet activation and aggregation induced by recombinant von Willebrand factors reproducing four type 2B von Willebrand disease missense mutations
    • de Romeuf, C., L. Hilbert, and C. Mazurier. 1998. Platelet activation and aggregation induced by recombinant von Willebrand factors reproducing four type 2B von Willebrand disease missense mutations. Thromb. Haemost. 79:211-216.
    • (1998) Thromb. Haemost. , vol.79 , pp. 211-216
    • De Romeuf, C.1    Hilbert, L.2    Mazurier, C.3
  • 30
    • 0345412698 scopus 로고    scopus 로고
    • Kinetics of GPIbα-vWF-A1 tether bond under flow: Effect of GPIbα mutations on the association and dissociation rates
    • Kumar, R. A., J. F. Dong,..., L. V. McIntire. 2003. Kinetics of GPIbα-vWF-A1 tether bond under flow: effect of GPIbα mutations on the association and dissociation rates. Biophys. J. 85:4099-4109.
    • (2003) Biophys. J. , vol.85 , pp. 4099-4109
    • Kumar, R.A.1    Dong, J.F.2    McIntire, L.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.