메뉴 건너뛰기




Volumn 8, Issue C, 2008, Pages 243-273

Chapter 8 Interactions of Phospholipid Binding Proteins with Negatively Charged Membranes. β2-Glycoprotein I as a Model Mechanism

Author keywords

[No Author keywords available]

Indexed keywords


EID: 69649085452     PISSN: 15544516     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1554-4516(08)00208-1     Document Type: Review
Times cited : (9)

References (104)
  • 1
    • 33746075254 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins
    • Lu J.Y., and Hofmann S.L. Thematic review series: Lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins. J. Lipid Res. 47 (2006) 1352-1357
    • (2006) J. Lipid Res. , vol.47 , pp. 1352-1357
    • Lu, J.Y.1    Hofmann, S.L.2
  • 2
    • 34548497139 scopus 로고    scopus 로고
    • Beta2-glycoprotein I and its clinical significance: From gene sequence to protein levels
    • Sodin-Semrl S., and Rozman B. Beta2-glycoprotein I and its clinical significance: From gene sequence to protein levels. Autoimmun. Rev. 6 (2007) 547-552
    • (2007) Autoimmun. Rev. , vol.6 , pp. 547-552
    • Sodin-Semrl, S.1    Rozman, B.2
  • 3
    • 0023805835 scopus 로고
    • Genetic variations of human serum beta2-glycoprotein I demonstrated by isoelectric focusing
    • Richter A., and Cleve H. Genetic variations of human serum beta2-glycoprotein I demonstrated by isoelectric focusing. Electrophoresis 9 (1988) 317-322
    • (1988) Electrophoresis , vol.9 , pp. 317-322
    • Richter, A.1    Cleve, H.2
  • 4
    • 0032531992 scopus 로고    scopus 로고
    • The insertion of human apolipoprotein H into phospholipid membranes: A monolayer study
    • Wang S.X., Cai G.P., and Sui S.F. The insertion of human apolipoprotein H into phospholipid membranes: A monolayer study. Biochem. J. 335 Pt 2 (1998) 225-232
    • (1998) Biochem. J. , vol.335 , Issue.PART 2 , pp. 225-232
    • Wang, S.X.1    Cai, G.P.2    Sui, S.F.3
  • 5
    • 0028860731 scopus 로고
    • Interactions and molecular structure of cardiolipin and beta 2-glycoprotein 1 (beta 2-GP1)
    • Borchman D., Harris E.N., Pierangeli S.S., and Lamba O.P. Interactions and molecular structure of cardiolipin and beta 2-glycoprotein 1 (beta 2-GP1). Clin. Exp. Immunol. 102 (1995) 373-378
    • (1995) Clin. Exp. Immunol. , vol.102 , pp. 373-378
    • Borchman, D.1    Harris, E.N.2    Pierangeli, S.S.3    Lamba, O.P.4
  • 6
    • 0021265066 scopus 로고
    • Beta 2-glycoprotein I (apolipoprotein H) interactions with phospholipid vesicles
    • Wurm H. Beta 2-glycoprotein I (apolipoprotein H) interactions with phospholipid vesicles. Int. J. Biochem. 16 (1984) 511-515
    • (1984) Int. J. Biochem. , vol.16 , pp. 511-515
    • Wurm, H.1
  • 7
    • 0027522834 scopus 로고
    • Identification of a Region of beta2-Glycoprotein I Critical for Lipid Binding and Anti-Cardiolipin Antibody Cofactor Activity
    • Hunt J.E., Simpson R.J., and Krilis S.A. Identification of a Region of beta2-Glycoprotein I Critical for Lipid Binding and Anti-Cardiolipin Antibody Cofactor Activity. Proc. Natl. Acad. Sci. USA. 90 (1993) 2141-2145
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 2141-2145
    • Hunt, J.E.1    Simpson, R.J.2    Krilis, S.A.3
  • 8
    • 0025833658 scopus 로고
    • Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I
    • Steinkasserer A., Estaller C., Weiss E.H., Sim R.B., and Day A.J. Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I. Biochem. J. 277 Pt 2 (1991) 387-391
    • (1991) Biochem. J. , vol.277 , Issue.PART 2 , pp. 387-391
    • Steinkasserer, A.1    Estaller, C.2    Weiss, E.H.3    Sim, R.B.4    Day, A.J.5
  • 10
    • 0000189838 scopus 로고    scopus 로고
    • A hydrophobic sequence at position 313-316 (Leu-Ala-Phe-Trp) in the fifth domain of apolipoprotein H (beta2-glycoprotein I) is crucial for cardiolipin binding
    • Mehdi H., Naqvi A., and Kamboh M.I. A hydrophobic sequence at position 313-316 (Leu-Ala-Phe-Trp) in the fifth domain of apolipoprotein H (beta2-glycoprotein I) is crucial for cardiolipin binding. Eur. J. Biochem. 267 (2000) 1770-1776
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1770-1776
    • Mehdi, H.1    Naqvi, A.2    Kamboh, M.I.3
  • 11
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins and as modulators of bilayer physical properties
    • Cornell R.B., and Taneva S.G. Amphipathic helices as mediators of the membrane interaction of amphitropic proteins and as modulators of bilayer physical properties. Curr. Protein Pept. Sci. 7 (2006) 539-552
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 12
    • 0033570889 scopus 로고    scopus 로고
    • Crystal structure of human beta2-glycoprotein I: Implications for phospholipid binding and the antiphospholipid syndrome
    • Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M., Laggner P., and Prassl R. Crystal structure of human beta2-glycoprotein I: Implications for phospholipid binding and the antiphospholipid syndrome. EMBO J 18 (1999) 6228-6239
    • (1999) EMBO J , vol.18 , pp. 6228-6239
    • Schwarzenbacher, R.1    Zeth, K.2    Diederichs, K.3    Gries, A.4    Kostner, G.M.5    Laggner, P.6    Prassl, R.7
  • 14
    • 0020633363 scopus 로고
    • Beta 2-Glycoprotein I. Molecular properties of an unusual apolipoprotein H
    • Lee N.S., Brewer Jr. H.B., and Osborne Jr. J.C. Beta 2-Glycoprotein I. Molecular properties of an unusual apolipoprotein H. J. Biol. Chem. 258 (1983) 4765-4770
    • (1983) J. Biol. Chem. , vol.258 , pp. 4765-4770
    • Lee, N.S.1    Brewer Jr., H.B.2    Osborne Jr., J.C.3
  • 15
    • 0027987114 scopus 로고
    • Autoantibodies to phospholipid-binding plasma proteins: A new view of lupus anticoagulants and other "antiphospholipid" autoantibodies
    • Roubey R.A. Autoantibodies to phospholipid-binding plasma proteins: A new view of lupus anticoagulants and other "antiphospholipid" autoantibodies. Blood 84 (1994) 2854-2867
    • (1994) Blood , vol.84 , pp. 2854-2867
    • Roubey, R.A.1
  • 16
    • 0022412337 scopus 로고
    • Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system
    • Chung L.P., Bentley D.R., and Reid K.B. Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system. Biochem. J. 230 (1985) 133-141
    • (1985) Biochem. J. , vol.230 , pp. 133-141
    • Chung, L.P.1    Bentley, D.R.2    Reid, K.B.3
  • 17
    • 0030870312 scopus 로고    scopus 로고
    • NMR studies of a viral protein that mimics the regulators of complement activation
    • Wiles A.P., Shaw G., Bright J., Perczel A., Campbell I.D., and Barlow P.N. NMR studies of a viral protein that mimics the regulators of complement activation. J. Mol. Biol. 272 (1997) 253-265
    • (1997) J. Mol. Biol. , vol.272 , pp. 253-265
    • Wiles, A.P.1    Shaw, G.2    Bright, J.3    Perczel, A.4    Campbell, I.D.5    Barlow, P.N.6
  • 18
    • 0033151839 scopus 로고    scopus 로고
    • Crystal structure of two CD46 domains reveals an extended measles virus-binding surface
    • Casasnovas J.M., Larvie M., and Stehle T. Crystal structure of two CD46 domains reveals an extended measles virus-binding surface. EMBO. J 18 (1999) 2911-2922
    • (1999) EMBO. J , vol.18 , pp. 2911-2922
    • Casasnovas, J.M.1    Larvie, M.2    Stehle, T.3
  • 20
    • 0031731613 scopus 로고    scopus 로고
    • Beta2-glycoprotein I: Target antigen for "antiphospholipid" antibodies. Immunological and molecular aspects
    • Sheng Y., Kandiah D.A., and Krilis S.A. Beta2-glycoprotein I: Target antigen for "antiphospholipid" antibodies. Immunological and molecular aspects. Lupus 7 Suppl. 2 (1998) S5-S9
    • (1998) Lupus , vol.7 , Issue.SUPPL. 2
    • Sheng, Y.1    Kandiah, D.A.2    Krilis, S.A.3
  • 21
    • 0031054567 scopus 로고    scopus 로고
    • Identification of structural mutations in the fifth domain of apolipoprotein H (beta 2-glycoprotein I) which affect phospholipid binding
    • Sanghera D.K., Wagenknecht D.R., McIntyre J.A., and Kamboh M.I. Identification of structural mutations in the fifth domain of apolipoprotein H (beta 2-glycoprotein I) which affect phospholipid binding. Hum. Mol. Genet. 6 (1997) 311-316
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 311-316
    • Sanghera, D.K.1    Wagenknecht, D.R.2    McIntyre, J.A.3    Kamboh, M.I.4
  • 22
    • 0011030357 scopus 로고
    • Complete amino acid sequence of human plasma beta 2-glycoprotein I
    • Lozier J., Takahashi N., and Putnam F.W. Complete amino acid sequence of human plasma beta 2-glycoprotein I. Proc. Natl. Acad. Sci. USA 81 (1984) 3640-3644
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3640-3644
    • Lozier, J.1    Takahashi, N.2    Putnam, F.W.3
  • 23
    • 0020421219 scopus 로고
    • Evidence of normal functional levels of activated protein C inhibitor in combined Factor V/VIII deficiency disease
    • Canfield W.M., and Kisiel W. Evidence of normal functional levels of activated protein C inhibitor in combined Factor V/VIII deficiency disease. J. Clin. Invest. 70 (1982) 1260-1272
    • (1982) J. Clin. Invest. , vol.70 , pp. 1260-1272
    • Canfield, W.M.1    Kisiel, W.2
  • 24
    • 0018977210 scopus 로고
    • Chemistry and function of human plasma proteins
    • Schwick H.G., and Haupt H. Chemistry and function of human plasma proteins. Angew. Chem. Int. Ed. Engl. 19 (1980) 87-99
    • (1980) Angew. Chem. Int. Ed. Engl. , vol.19 , pp. 87-99
    • Schwick, H.G.1    Haupt, H.2
  • 25
    • 0042763102 scopus 로고    scopus 로고
    • 2-glycoprotein I antibodies and the antiphospholipid syndrome
    • 2-glycoprotein I antibodies and the antiphospholipid syndrome. Autoimmun. Rev. 2 (2003) 229-234
    • (2003) Autoimmun. Rev. , vol.2 , pp. 229-234
    • Li, Z.1    Krilis, S.A.2
  • 27
    • 0032817911 scopus 로고    scopus 로고
    • The binding of apolipoprotein H (beta2-Glycoprotein I) to lipoproteins
    • Gambino R., Ruiu G., Pagano G., and Cassader M. The binding of apolipoprotein H (beta2-Glycoprotein I) to lipoproteins. Prostag. Oth. Lipid M. 57 (1999) 351-359
    • (1999) Prostag. Oth. Lipid M. , vol.57 , pp. 351-359
    • Gambino, R.1    Ruiu, G.2    Pagano, G.3    Cassader, M.4
  • 28
    • 0024338069 scopus 로고
    • Characterization of isoelectric subspecies of asialo-beta 2-glycoprotein I
    • Gries A., Nimpf J., Wurm H., Kostner G.M., and Kenner T. Characterization of isoelectric subspecies of asialo-beta 2-glycoprotein I. Biochem. J. 260 (1989) 531-534
    • (1989) Biochem. J. , vol.260 , pp. 531-534
    • Gries, A.1    Nimpf, J.2    Wurm, H.3    Kostner, G.M.4    Kenner, T.5
  • 29
    • 0023880969 scopus 로고
    • Genetic studies of human apolipoproteins. IV. Structural heterogeneity of apolipoprotein H (beta 2-glycoprotein I)
    • Kamboh M.I., Ferrell R.E., and Sepehrnia B. Genetic studies of human apolipoproteins. IV. Structural heterogeneity of apolipoprotein H (beta 2-glycoprotein I). Am. J. Hum. Genet. 42 (1988) 452-457
    • (1988) Am. J. Hum. Genet. , vol.42 , pp. 452-457
    • Kamboh, M.I.1    Ferrell, R.E.2    Sepehrnia, B.3
  • 30
    • 0030912446 scopus 로고    scopus 로고
    • Qualitative analysis of the carbohydrate composition of apolipoprotein H
    • Gambino R., Ruiu G., Pagano G., and Cassader M. Qualitative analysis of the carbohydrate composition of apolipoprotein H. J. Protein Chem. 16 (1997) 205-212
    • (1997) J. Protein Chem. , vol.16 , pp. 205-212
    • Gambino, R.1    Ruiu, G.2    Pagano, G.3    Cassader, M.4
  • 31
    • 0017114288 scopus 로고
    • Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct
    • Kiely M.L., McKnight G.S., and Schimke R.T. Studies on the attachment of carbohydrate to ovalbumin nascent chains in hen oviduct. J. Biol. Chem. 251 (1976) 5490-5495
    • (1976) J. Biol. Chem. , vol.251 , pp. 5490-5495
    • Kiely, M.L.1    McKnight, G.S.2    Schimke, R.T.3
  • 32
    • 0025369545 scopus 로고
    • Effect of the carbohydrate moiety on the secondary structure of beta 2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins
    • Walsh M.T., Watzlawick H., Putnam F.W., Schmid K., and Brossmer R. Effect of the carbohydrate moiety on the secondary structure of beta 2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins. Biochemistry 29 (1990) 6250-6257
    • (1990) Biochemistry , vol.29 , pp. 6250-6257
    • Walsh, M.T.1    Watzlawick, H.2    Putnam, F.W.3    Schmid, K.4    Brossmer, R.5
  • 33
    • 0031149078 scopus 로고    scopus 로고
    • Characterization of the carbohydrate structures of apolipoprotein H through concanavalin A affinity chromatography
    • Gambino R., Ruiu G., Pagano G., and Cassader M. Characterization of the carbohydrate structures of apolipoprotein H through concanavalin A affinity chromatography. J. Lipid Mediat. Cell Signal. 16 (1997) 11-21
    • (1997) J. Lipid Mediat. Cell Signal. , vol.16 , pp. 11-21
    • Gambino, R.1    Ruiu, G.2    Pagano, G.3    Cassader, M.4
  • 34
    • 0029855586 scopus 로고    scopus 로고
    • Role of divalency in the high-affinity binding of anticardiolipin antibody-beta 2-glycoprotein I complexes to lipid membranes
    • Willems G.M., Janssen M.P., Pelsers M.M., Comfurius P., Galli M., Zwaal R.F., and Bevers E.M. Role of divalency in the high-affinity binding of anticardiolipin antibody-beta 2-glycoprotein I complexes to lipid membranes. Biochemistry 35 (1996) 13833-13842
    • (1996) Biochemistry , vol.35 , pp. 13833-13842
    • Willems, G.M.1    Janssen, M.P.2    Pelsers, M.M.3    Comfurius, P.4    Galli, M.5    Zwaal, R.F.6    Bevers, E.M.7
  • 35
    • 0035652560 scopus 로고    scopus 로고
    • Effect of cardiolipin oxidation on solid-phase immunoassay for antiphospholipid antibodies
    • Schlame M., Haller I., Sammaritano L.R., and Blanck T.J. Effect of cardiolipin oxidation on solid-phase immunoassay for antiphospholipid antibodies. Thromb. Haemost. 86 (2001) 1475-1482
    • (2001) Thromb. Haemost. , vol.86 , pp. 1475-1482
    • Schlame, M.1    Haller, I.2    Sammaritano, L.R.3    Blanck, T.J.4
  • 36
    • 0034740526 scopus 로고    scopus 로고
    • Oxidation of beta2-glycoprotein I (beta2GPI) by the hydroxyl radical alters phospholipid binding and modulates recognition by anti-beta2GPI autoantibodies
    • Arvieux J., Regnault V., Hachulla E., Darnige L., Berthou F., and Youinou P. Oxidation of beta2-glycoprotein I (beta2GPI) by the hydroxyl radical alters phospholipid binding and modulates recognition by anti-beta2GPI autoantibodies. Thromb. Haemost. 86 (2001) 1070-1076
    • (2001) Thromb. Haemost. , vol.86 , pp. 1070-1076
    • Arvieux, J.1    Regnault, V.2    Hachulla, E.3    Darnige, L.4    Berthou, F.5    Youinou, P.6
  • 37
  • 38
    • 20444420860 scopus 로고    scopus 로고
    • Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an increase in its affinity for anionic phospholipids similar to that obtained by the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies
    • d'Angeac A.D., Stefas I., Duperray C., Rucheton M., Graafland H., Montero J.L., and Chicheportiche R. Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an increase in its affinity for anionic phospholipids similar to that obtained by the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies. J. Immunol. Methods 300 (2005) 160-178
    • (2005) J. Immunol. Methods , vol.300 , pp. 160-178
    • d'Angeac, A.D.1    Stefas, I.2    Duperray, C.3    Rucheton, M.4    Graafland, H.5    Montero, J.L.6    Chicheportiche, R.7
  • 39
    • 30044451650 scopus 로고    scopus 로고
    • Biotinylation of glycan chains in beta2 glycoprotein I induces dimerization of the molecule and its detection by the human autoimmune anti-cardiolipin antibody EY2C9
    • d'Angeac A.D., Stefas I., Graafland H., De Lamotte F., Rucheton M., Palais C., Eriksson A.K., Bosc P., Rose C., and Chicheportiche R. Biotinylation of glycan chains in beta2 glycoprotein I induces dimerization of the molecule and its detection by the human autoimmune anti-cardiolipin antibody EY2C9. Biochem. J. 393 (2006) 117-127
    • (2006) Biochem. J. , vol.393 , pp. 117-127
    • d'Angeac, A.D.1    Stefas, I.2    Graafland, H.3    De Lamotte, F.4    Rucheton, M.5    Palais, C.6    Eriksson, A.K.7    Bosc, P.8    Rose, C.9    Chicheportiche, R.10
  • 40
    • 0028983571 scopus 로고
    • "Anticardiolipin" autoantibodies recognize beta 2-glycoprotein I in the absence of phospholipid. Importance of Ag density and bivalent binding
    • Roubey R.A., Eisenberg R.A., Harper M.F., and Winfield J.B. "Anticardiolipin" autoantibodies recognize beta 2-glycoprotein I in the absence of phospholipid. Importance of Ag density and bivalent binding. J. Immunol. 154 (1995) 954-960
    • (1995) J. Immunol. , vol.154 , pp. 954-960
    • Roubey, R.A.1    Eisenberg, R.A.2    Harper, M.F.3    Winfield, J.B.4
  • 41
    • 8344238269 scopus 로고    scopus 로고
    • Binding of high-avidity anti-beta2-glycoprotein I antibodies
    • Cucnik S., Kveder T., Rozman B., and Bozic B. Binding of high-avidity anti-beta2-glycoprotein I antibodies. Rheumatology (Oxford) 43 (2004) 1353-1356
    • (2004) Rheumatology (Oxford) , vol.43 , pp. 1353-1356
    • Cucnik, S.1    Kveder, T.2    Rozman, B.3    Bozic, B.4
  • 42
    • 0032529194 scopus 로고    scopus 로고
    • Anti-beta 2-glycoprotein I autoantibodies from patients with the "antiphospholipid" syndrome bind to beta 2-glycoprotein I with low affinity: Dimerization of beta 2-glycoprotein I induces a significant increase in anti-beta 2-glycoprotein I antibody affinity
    • Sheng Y., Kandiah D.A., and Krilis S.A. Anti-beta 2-glycoprotein I autoantibodies from patients with the "antiphospholipid" syndrome bind to beta 2-glycoprotein I with low affinity: Dimerization of beta 2-glycoprotein I induces a significant increase in anti-beta 2-glycoprotein I antibody affinity. J. Immunol. 161 (1998) 2038-2043
    • (1998) J. Immunol. , vol.161 , pp. 2038-2043
    • Sheng, Y.1    Kandiah, D.A.2    Krilis, S.A.3
  • 43
    • 0035793644 scopus 로고    scopus 로고
    • Dimers of beta 2-glycoprotein I mimic the in vitro effects of beta 2-glycoprotein I-anti-beta 2-glycoprotein I antibody complexes
    • Lutters B.C., Meijers J.C., Derksen R.H., Arnout J., and de Groot P.G. Dimers of beta 2-glycoprotein I mimic the in vitro effects of beta 2-glycoprotein I-anti-beta 2-glycoprotein I antibody complexes. J. Biol. Chem. 276 (2001) 3060-3067
    • (2001) J. Biol. Chem. , vol.276 , pp. 3060-3067
    • Lutters, B.C.1    Meijers, J.C.2    Derksen, R.H.3    Arnout, J.4    de Groot, P.G.5
  • 46
    • 14444274552 scopus 로고    scopus 로고
    • Structure and function of the recombinant fifth domain of human beta 2-glycoprotein I: Effects of specific cleavage between Lys77 and Thr78
    • Hagihara Y., Enjyoji K., Omasa T., Katakura Y., Suga K., Igarashi M., Matsuura E., Kato H., Yoshimura T., and Goto Y. Structure and function of the recombinant fifth domain of human beta 2-glycoprotein I: Effects of specific cleavage between Lys77 and Thr78. J. Biochem. 121 (1997) 128-137
    • (1997) J. Biochem. , vol.121 , pp. 128-137
    • Hagihara, Y.1    Enjyoji, K.2    Omasa, T.3    Katakura, Y.4    Suga, K.5    Igarashi, M.6    Matsuura, E.7    Kato, H.8    Yoshimura, T.9    Goto, Y.10
  • 47
    • 0032101032 scopus 로고    scopus 로고
    • Plasmin can reduce the function of human beta2 glycoprotein I by cleaving domain V into a nicked form
    • Ohkura N., Hagihara Y., Yoshimura T., Goto Y., and Kato H. Plasmin can reduce the function of human beta2 glycoprotein I by cleaving domain V into a nicked form. Blood 91 (1998) 4173-4179
    • (1998) Blood , vol.91 , pp. 4173-4179
    • Ohkura, N.1    Hagihara, Y.2    Yoshimura, T.3    Goto, Y.4    Kato, H.5
  • 51
    • 0034530038 scopus 로고    scopus 로고
    • 2 glycoprotein I in patients with leukemia and with lupus anticoagulant: Measurement with a monoclonal antibody specific for a nicked form of domain V
    • 2 glycoprotein I in patients with leukemia and with lupus anticoagulant: Measurement with a monoclonal antibody specific for a nicked form of domain V. J. Biochem. 128 (2000) 1017-1024
    • (2000) J. Biochem. , vol.128 , pp. 1017-1024
    • Itoh, Y.1    Inuzuka, K.2    Kohno, I.3    Wada, H.4    Shiku, H.5    Ohkura, N.6    Kato, H.7
  • 52
    • 0033562968 scopus 로고    scopus 로고
    • Microheterogeneity of beta-2 glycoprotein I: Implications for binding to anionic phospholipids
    • Brighton T.A., Dai Y.P., Hogg P.J., and Chesterman C.N. Microheterogeneity of beta-2 glycoprotein I: Implications for binding to anionic phospholipids. Biochem. J. 340 Pt 1 (1999) 59-67
    • (1999) Biochem. J. , vol.340 , Issue.PART 1 , pp. 59-67
    • Brighton, T.A.1    Dai, Y.P.2    Hogg, P.J.3    Chesterman, C.N.4
  • 54
    • 0037169563 scopus 로고    scopus 로고
    • Heparin inhibits the binding of beta 2-glycoprotein I to phospholipids and promotes the plasmin-mediated inactivation of this blood protein. Elucidation of the consequences of the two biological events in patients with the anti-phospholipid syndrome
    • Guerin J., Sheng Y., Reddel S., Iverson G.M., Chapman M.G., and Krilis S.A. Heparin inhibits the binding of beta 2-glycoprotein I to phospholipids and promotes the plasmin-mediated inactivation of this blood protein. Elucidation of the consequences of the two biological events in patients with the anti-phospholipid syndrome. J. Biol. Chem. 277 (2002) 2644-2649
    • (2002) J. Biol. Chem. , vol.277 , pp. 2644-2649
    • Guerin, J.1    Sheng, Y.2    Reddel, S.3    Iverson, G.M.4    Chapman, M.G.5    Krilis, S.A.6
  • 55
    • 0033587625 scopus 로고    scopus 로고
    • Intrinsic fluorescence study of the interaction of human apolipoprotein H with phospholipid vesicles
    • Wang S.X., Cai G., and Sui S. Intrinsic fluorescence study of the interaction of human apolipoprotein H with phospholipid vesicles. Biochemistry 38 (1999) 9477-9484
    • (1999) Biochemistry , vol.38 , pp. 9477-9484
    • Wang, S.X.1    Cai, G.2    Sui, S.3
  • 57
    • 23644439970 scopus 로고    scopus 로고
    • Membrane binding of beta2-glycoprotein I can be described by a two-state reaction model: An atomic force microscopy and surface plasmon resonance study
    • Gamsjaeger R., Johs A., Gries A., Gruber H.J., Romanin C., Prassl R., and Hinterdorfer P. Membrane binding of beta2-glycoprotein I can be described by a two-state reaction model: An atomic force microscopy and surface plasmon resonance study. Biochem. J. 389 (2005) 665-673
    • (2005) Biochem. J. , vol.389 , pp. 665-673
    • Gamsjaeger, R.1    Johs, A.2    Gries, A.3    Gruber, H.J.4    Romanin, C.5    Prassl, R.6    Hinterdorfer, P.7
  • 58
    • 34548751157 scopus 로고    scopus 로고
    • Interaction of beta2-glycoprotein 1 with phosphatidylserine-containing membranes: Ligand-dependent conformational alterations initiate bivalent binding
    • Hamdan R., Maiti S.N., and Schroit A.J. Interaction of beta2-glycoprotein 1 with phosphatidylserine-containing membranes: Ligand-dependent conformational alterations initiate bivalent binding. Biochemistry 46 (2007) 10612-10620
    • (2007) Biochemistry , vol.46 , pp. 10612-10620
    • Hamdan, R.1    Maiti, S.N.2    Schroit, A.J.3
  • 59
    • 0034658321 scopus 로고    scopus 로고
    • Membrane-induced conformational change in human apolipoprotein H
    • Wang S.X., Sun Y.T., and Sui S.F. Membrane-induced conformational change in human apolipoprotein H. Biochem. J. 348 Pt 1 (2000) 103-106
    • (2000) Biochem. J. , vol.348 , Issue.PART 1 , pp. 103-106
    • Wang, S.X.1    Sun, Y.T.2    Sui, S.F.3
  • 61
    • 84970332058 scopus 로고
    • Structure and function of beta 2-glycoprotein I: With special reference to the interaction with phospholipid
    • Hagihara Y., Goto Y., Kato H., and Yoshimura T. Structure and function of beta 2-glycoprotein I: With special reference to the interaction with phospholipid. Lupus 4 Suppl. 1 (1995) S3-S5
    • (1995) Lupus , vol.4 , Issue.SUPPL. 1
    • Hagihara, Y.1    Goto, Y.2    Kato, H.3    Yoshimura, T.4
  • 62
    • 33751218588 scopus 로고    scopus 로고
    • Interaction of giant phospholipid vesicles containing cardiolipin and cholesterol with beta2-glycoprotein-I and anti-beta2-glycoprotein-I antibodies
    • Ambrožič A., Čučnik S., Tomšič N., Urbanija J., Lokar M., Babnik B., Rozman B., Iglič A., and Kralj-Iglič V. Interaction of giant phospholipid vesicles containing cardiolipin and cholesterol with beta2-glycoprotein-I and anti-beta2-glycoprotein-I antibodies. Autoimmun. Rev. 6 (2006) 10-15
    • (2006) Autoimmun. Rev. , vol.6 , pp. 10-15
    • Ambrožič, A.1    Čučnik, S.2    Tomšič, N.3    Urbanija, J.4    Lokar, M.5    Babnik, B.6    Rozman, B.7    Iglič, A.8    Kralj-Iglič, V.9
  • 65
    • 18844400656 scopus 로고    scopus 로고
    • Budding, vesiculation and permeabilization of phospholipid membranes-evidence for a feasible physiologic role of beta2-glycoprotein I and pathogenic actions of anti-beta2-glycoprotein I antibodies
    • Ambrožic A., Božič B., Kveder T., Majhenc J., Arrigler V., Svetina S., and Rozman B. Budding, vesiculation and permeabilization of phospholipid membranes-evidence for a feasible physiologic role of beta2-glycoprotein I and pathogenic actions of anti-beta2-glycoprotein I antibodies. Biochim. Biophys. Acta 1740 (2005) 38-44
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 38-44
    • Ambrožic, A.1    Božič, B.2    Kveder, T.3    Majhenc, J.4    Arrigler, V.5    Svetina, S.6    Rozman, B.7
  • 66
    • 37649004233 scopus 로고    scopus 로고
    • Prevention of microvesiculation by adhesion of buds to the mother cell membrane-a possible anticoagulant effect of healthy donor plasma
    • Frank M., Manček-Keber M., Kržan M., Sodin-Semrl S., Jerala R., Iglič A., Rozman B., and Kralj-Iglič V. Prevention of microvesiculation by adhesion of buds to the mother cell membrane-a possible anticoagulant effect of healthy donor plasma. Autoimmun. Rev. 7 (2008) 240-245
    • (2008) Autoimmun. Rev. , vol.7 , pp. 240-245
    • Frank, M.1    Manček-Keber, M.2    Kržan, M.3    Sodin-Semrl, S.4    Jerala, R.5    Iglič, A.6    Rozman, B.7    Kralj-Iglič, V.8
  • 67
    • 77956833559 scopus 로고    scopus 로고
    • M. Frank, J. Pavliover(c, -), K. Bohinc, B. Rozman, V. Kralj-Iglič, A. Iglič, Influence of ionic strength on agglutination of like-charged phospholipid membranes induced by beta2-GPI (in preparation).
    • M. Frank, J. Pavliover(c, -), K. Bohinc, B. Rozman, V. Kralj-Iglič, A. Iglič, Influence of ionic strength on agglutination of like-charged phospholipid membranes induced by beta2-GPI (in preparation).
  • 68
    • 0031593870 scopus 로고    scopus 로고
    • Characterization of beta2-glycoprotein I binding to phospholipid membranes
    • Harper M.F., Hayes P.M., Lentz B.R., and Roubey R.A. Characterization of beta2-glycoprotein I binding to phospholipid membranes. Thromb. Haemost. 80 (1998) 610-614
    • (1998) Thromb. Haemost. , vol.80 , pp. 610-614
    • Harper, M.F.1    Hayes, P.M.2    Lentz, B.R.3    Roubey, R.A.4
  • 69
    • 0035997048 scopus 로고    scopus 로고
    • Human apolipoprotein H may have various orientations when attached to lipid layer
    • Wang F., Xia X.F., and Sui S.F. Human apolipoprotein H may have various orientations when attached to lipid layer. Biophys. J. 83 (2002) 985-993
    • (2002) Biophys. J. , vol.83 , pp. 985-993
    • Wang, F.1    Xia, X.F.2    Sui, S.F.3
  • 70
    • 3042835297 scopus 로고    scopus 로고
    • The effect of phospholipids on the formation of immune complexes between autoantibodies and beta2-glycoprotein I or prothrombin
    • Bevers E.M., Zwaal R.F., and Willems G.M. The effect of phospholipids on the formation of immune complexes between autoantibodies and beta2-glycoprotein I or prothrombin. Clin. Immunol. 112 (2004) 150-160
    • (2004) Clin. Immunol. , vol.112 , pp. 150-160
    • Bevers, E.M.1    Zwaal, R.F.2    Willems, G.M.3
  • 71
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • Zwaal R.F., and Schroit A.J. Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89 (1997) 1121-1132
    • (1997) Blood , vol.89 , pp. 1121-1132
    • Zwaal, R.F.1    Schroit, A.J.2
  • 72
    • 3242667696 scopus 로고    scopus 로고
    • Cellular microparticles: A disseminated storage pool of bioactive vascular effectors
    • Morel O., Toti F., Hugel B., and Freyssinet J.M. Cellular microparticles: A disseminated storage pool of bioactive vascular effectors. Curr. Opin. Hematol. 11 (2004) 156-164
    • (2004) Curr. Opin. Hematol. , vol.11 , pp. 156-164
    • Morel, O.1    Toti, F.2    Hugel, B.3    Freyssinet, J.M.4
  • 74
    • 0025301753 scopus 로고
    • Loss of membrane phospholipid asymmetry in platelets and red cells may be associated with calcium-induced shedding of plasma membrane and inhibition of aminophospholipid translocase
    • Comfurius P., Senden J.M., Tilly R.H., Schroit A.J., Bevers E.M., and Zwaal R.F. Loss of membrane phospholipid asymmetry in platelets and red cells may be associated with calcium-induced shedding of plasma membrane and inhibition of aminophospholipid translocase. Biochim. Biophys. Acta 1026 (1990) 153-160
    • (1990) Biochim. Biophys. Acta , vol.1026 , pp. 153-160
    • Comfurius, P.1    Senden, J.M.2    Tilly, R.H.3    Schroit, A.J.4    Bevers, E.M.5    Zwaal, R.F.6
  • 75
    • 0024325249 scopus 로고
    • Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: An isolated defect in platelet procoagulant activity
    • Sims P.J., Wiedmer T., Esmon C.T., Weiss H.J., and Shattil S.J. Assembly of the platelet prothrombinase complex is linked to vesiculation of the platelet plasma membrane. Studies in Scott syndrome: An isolated defect in platelet procoagulant activity. J. Biol. Chem. 264 (1989) 17049-17057
    • (1989) J. Biol. Chem. , vol.264 , pp. 17049-17057
    • Sims, P.J.1    Wiedmer, T.2    Esmon, C.T.3    Weiss, H.J.4    Shattil, S.J.5
  • 76
    • 0025101650 scopus 로고
    • Role of calcium and calpain in complement-induced vesiculation of the platelet plasma membrane and in the exposure of the platelet factor Va receptor
    • Wiedmer T., Shattil S.J., Cunningham M., and Sims P.J. Role of calcium and calpain in complement-induced vesiculation of the platelet plasma membrane and in the exposure of the platelet factor Va receptor. Biochemistry 29 (1990) 623-632
    • (1990) Biochemistry , vol.29 , pp. 623-632
    • Wiedmer, T.1    Shattil, S.J.2    Cunningham, M.3    Sims, P.J.4
  • 77
    • 0026688548 scopus 로고
    • Platelet procoagulant activity and microvesicle formation. Its putative role in hemostasis and thrombosis
    • Zwaal R.F., Comfurius P., and Bevers E.M. Platelet procoagulant activity and microvesicle formation. Its putative role in hemostasis and thrombosis. Biochim. Biophys. Acta 1180 (1992) 1-8
    • (1992) Biochim. Biophys. Acta , vol.1180 , pp. 1-8
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 78
    • 0026651919 scopus 로고
    • Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids
    • Farge E., and Devaux P.F. Shape changes of giant liposomes induced by an asymmetric transmembrane distribution of phospholipids. Biophys. J. 61 (1992) 347-357
    • (1992) Biophys. J. , vol.61 , pp. 347-357
    • Farge, E.1    Devaux, P.F.2
  • 81
    • 0036828837 scopus 로고    scopus 로고
    • Shape behavior of lipid vesicles as the basis of some cellular processes
    • Svetina S., and Žekš B. Shape behavior of lipid vesicles as the basis of some cellular processes. Anat. Rec. 268 (2002) 215-225
    • (2002) Anat. Rec. , vol.268 , pp. 215-225
    • Svetina, S.1    Žekš, B.2
  • 82
    • 0029866102 scopus 로고    scopus 로고
    • Surface blebs on apoptotic cells are sites of enhanced procoagulant activity: Implications for coagulation events and antigenic spread in systemic lupus erythematosus
    • Casciola-Rosen L., Rosen A., Petri M., and Schlissel M. Surface blebs on apoptotic cells are sites of enhanced procoagulant activity: Implications for coagulation events and antigenic spread in systemic lupus erythematosus. Proc. Natl. Acad. Sci. USA. 93 (1996) 1624-1629
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 1624-1629
    • Casciola-Rosen, L.1    Rosen, A.2    Petri, M.3    Schlissel, M.4
  • 83
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples - molecular mechanism of drug erythrocyte interaction
    • Sheetz M.P., and Singer S.J. Biological membranes as bilayer couples - molecular mechanism of drug erythrocyte interaction. Proc. Natl. Acad. Sci. USA. 71 (1974) 4457-4461
    • (1974) Proc. Natl. Acad. Sci. USA. , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 84
    • 0024324636 scopus 로고
    • Membrane bending energy and shape determination of phospholipid vesicles and red blood cels
    • Svetina S., and Žekš B. Membrane bending energy and shape determination of phospholipid vesicles and red blood cels. Eur. Biophys. J. 17 (1989) 101-111
    • (1989) Eur. Biophys. J. , vol.17 , pp. 101-111
    • Svetina, S.1    Žekš, B.2
  • 85
    • 84956215183 scopus 로고
    • Shape transformations of giant vesicles: Extreme sensitivity to bilayer asymmetry
    • Berndl K., Käs J., Lipowsky R., Sackmann E., and Seifert U. Shape transformations of giant vesicles: Extreme sensitivity to bilayer asymmetry. Europhys. Lett. 13 (1990) 659-664
    • (1990) Europhys. Lett. , vol.13 , pp. 659-664
    • Berndl, K.1    Käs, J.2    Lipowsky, R.3    Sackmann, E.4    Seifert, U.5
  • 86
    • 33846363469 scopus 로고
    • Budding transitions of fluid-bilayer vesicles: The effect of area-difference elasticity
    • Miao L., Seifert U., Wortis M., and Dobereiner H.G. Budding transitions of fluid-bilayer vesicles: The effect of area-difference elasticity. Phys. Rev. E. 49 (1994) 5389-5407
    • (1994) Phys. Rev. E. , vol.49 , pp. 5389-5407
    • Miao, L.1    Seifert, U.2    Wortis, M.3    Dobereiner, H.G.4
  • 87
    • 0021778449 scopus 로고
    • Bilayer couple as a possible mechanism of biological shape formation
    • Svetina S., and Žekš B. Bilayer couple as a possible mechanism of biological shape formation. Biomed. Biochim. Acta 44 (1985) 979-986
    • (1985) Biomed. Biochim. Acta , vol.44 , pp. 979-986
    • Svetina, S.1    Žekš, B.2
  • 88
    • 0034805912 scopus 로고    scopus 로고
    • Pathogenic mechanisms mediating antiphospholipid syndrome
    • Meroni P.L., and Riboldi P. Pathogenic mechanisms mediating antiphospholipid syndrome. Curr. Opin. Rheumatol. 13 (2001) 377-382
    • (2001) Curr. Opin. Rheumatol. , vol.13 , pp. 377-382
    • Meroni, P.L.1    Riboldi, P.2
  • 91
    • 0035885939 scopus 로고    scopus 로고
    • 2-glycoprotein I in patients with antiphospholipid syndrome: Preferential recognition of the major phospholipid-binding site
    • 2-glycoprotein I in patients with antiphospholipid syndrome: Preferential recognition of the major phospholipid-binding site. Blood 98 (2001) 1889-1896
    • (2001) Blood , vol.98 , pp. 1889-1896
    • Arai, T.1    Yoshida, K.2    Kaburaki, J.3    Inoko, H.4    Ikeda, Y.5    Kawakami, Y.6    Kuwana, M.7
  • 94
    • 0028181357 scopus 로고
    • The fifth domain of beta 2-glycoprotein I contains a phospholipid binding site (Cys281-Cys288) and a region recognized by anticardiolipin antibodies
    • Hunt J., and Krilis S. The fifth domain of beta 2-glycoprotein I contains a phospholipid binding site (Cys281-Cys288) and a region recognized by anticardiolipin antibodies. J. Immunol. 152 (1994) 653-659
    • (1994) J. Immunol. , vol.152 , pp. 653-659
    • Hunt, J.1    Krilis, S.2
  • 95
    • 0030587953 scopus 로고    scopus 로고
    • Site-directed mutagenesis of recombinant human beta 2-glycoprotein I identifies a cluster of lysine residues that are critical for phospholipid binding and anti-cardiolipin antibody activity
    • Sheng Y., Sali A., Herzog H., Lahnstein J., and Krilis S.A. Site-directed mutagenesis of recombinant human beta 2-glycoprotein I identifies a cluster of lysine residues that are critical for phospholipid binding and anti-cardiolipin antibody activity. J. Immunol. 157 (1996) 3744-3751
    • (1996) J. Immunol. , vol.157 , pp. 3744-3751
    • Sheng, Y.1    Sali, A.2    Herzog, H.3    Lahnstein, J.4    Krilis, S.A.5
  • 96
    • 13544259567 scopus 로고    scopus 로고
    • 2-glycoprotein I to anionic phospholipids facilitates processing and presentation of a cryptic epitope that activates pathogenic autoreactive T cells
    • 2-glycoprotein I to anionic phospholipids facilitates processing and presentation of a cryptic epitope that activates pathogenic autoreactive T cells. Blood 105 (2005) 1552-1557
    • (2005) Blood , vol.105 , pp. 1552-1557
    • Kuwana, M.1    Matsuura, E.2    Kobayashi, K.3    Okazaki, Y.4    Kaburaki, J.5    Ikeda, Y.6    Kawakami, Y.7
  • 97
    • 38049023658 scopus 로고    scopus 로고
    • Excessive exposure to anionic surfaces maintains autoantibody response to 2-glycoprotein I in patients with antiphospholipid syndrome
    • Yamaguchi Y., Seta N., Kaburaki J., Kobayashi K., Matsuura E., and Kuwana M. Excessive exposure to anionic surfaces maintains autoantibody response to 2-glycoprotein I in patients with antiphospholipid syndrome. Blood 110 (2007) 4312-4318
    • (2007) Blood , vol.110 , pp. 4312-4318
    • Yamaguchi, Y.1    Seta, N.2    Kaburaki, J.3    Kobayashi, K.4    Matsuura, E.5    Kuwana, M.6
  • 99
    • 13544276197 scopus 로고    scopus 로고
    • 2-glycoprotein I cause LAC, and their presence correlates strongly with thrombosis
    • 2-glycoprotein I cause LAC, and their presence correlates strongly with thrombosis. Blood 105 (2005) 1540-1545
    • (2005) Blood , vol.105 , pp. 1540-1545
    • de Laat, B.1    Derksen, R.H.W.M.2    Urbanus, R.T.3    de Groot, P.G.4
  • 100
    • 0030584823 scopus 로고    scopus 로고
    • Human beta2-glycoprotein I as an anticardiolipin cofactor determined using mutants expressed by a baculovirus system
    • Igarashi M., Matsuura E., Igarashi Y., Nagae H., Ichikawa K., Triplett D.A., and Koike T. Human beta2-glycoprotein I as an anticardiolipin cofactor determined using mutants expressed by a baculovirus system. Blood 87 (1996) 3262-3270
    • (1996) Blood , vol.87 , pp. 3262-3270
    • Igarashi, M.1    Matsuura, E.2    Igarashi, Y.3    Nagae, H.4    Ichikawa, K.5    Triplett, D.A.6    Koike, T.7
  • 101
    • 0032521680 scopus 로고    scopus 로고
    • Target recognition of beta2-glycoprotein I (beta2GPI)-dependent anticardiolipin antibodies: Evidence for involvement of the fourth domain of beta2GPI in antibody binding
    • George J., Gilburd B., Hojnik M., Levy Y., Langevitz P., Matsuura E., Koike T., and Shoenfeld Y. Target recognition of beta2-glycoprotein I (beta2GPI)-dependent anticardiolipin antibodies: Evidence for involvement of the fourth domain of beta2GPI in antibody binding. J. Immunol. 160 (1998) 3917-3923
    • (1998) J. Immunol. , vol.160 , pp. 3917-3923
    • George, J.1    Gilburd, B.2    Hojnik, M.3    Levy, Y.4    Langevitz, P.5    Matsuura, E.6    Koike, T.7    Shoenfeld, Y.8
  • 102
    • 0032217240 scopus 로고    scopus 로고
    • Anti-beta2 glycoprotein I (beta2GPI) autoantibodies recognize an epitope on the first domain of beta2GPI
    • Iverson G.M., Victoria E.J., and Marquis D.M. Anti-beta2 glycoprotein I (beta2GPI) autoantibodies recognize an epitope on the first domain of beta2GPI. Proc. Natl. Acad. Sci. USA 95 (1998) 15542-15546
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15542-15546
    • Iverson, G.M.1    Victoria, E.J.2    Marquis, D.M.3
  • 103
    • 0028175428 scopus 로고
    • Human alpha-lactalbumin and bovine beta-lactoglobulin absorption in infants
    • Kuitunen M., Savilahti E., and Sarnesto A. Human alpha-lactalbumin and bovine beta-lactoglobulin absorption in infants. Allergy 49 (1994) 354-360
    • (1994) Allergy , vol.49 , pp. 354-360
    • Kuitunen, M.1    Savilahti, E.2    Sarnesto, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.