메뉴 건너뛰기




Volumn 189, Issue 4, 2012, Pages 1858-1867

Atypical hemolytic uremic syndrome-associated variants and autoantibodies impair binding of factor H and factor H-related protein 1 to pentraxin 3

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; BINDING PROTEIN; COMPLEMENT FACTOR H; COMPLEMENT FACTOR H LIKE PROTEIN 1; COMPLEMENT FACTOR H RELATED PROTEIN 1; PENTRAXIN 3; PROTEIN VARIANT; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84864823657     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1200357     Document Type: Article
Times cited : (50)

References (55)
  • 1
    • 38149021434 scopus 로고    scopus 로고
    • Pentraxins in innate immunity: From C-reactive protein to the long pentraxin PTX3
    • Mantovani, A., C. Garlanda, A. Doni, and B. Bottazzi. 2008. Pentraxins in innate immunity: from C-reactive protein to the long pentraxin PTX3. J. Clin. Immunol. 28: 1-13.
    • (2008) J. Clin. Immunol. , vol.28 , pp. 1-13
    • Mantovani, A.1    Garlanda, C.2    Doni, A.3    Bottazzi, B.4
  • 2
    • 63849234720 scopus 로고    scopus 로고
    • Determination of physiological plasma pentraxin 3 (PTX3) levels in healthy populations
    • Yamasaki, K., M. Kurimura, T. Kasai, M. Sagara, T. Kodama, and K. Inoue. 2009. Determination of physiological plasma pentraxin 3 (PTX3) levels in healthy populations. Clin. Chem. Lab. Med. 47: 471-477.
    • (2009) Clin. Chem. Lab. Med. , vol.47 , pp. 471-477
    • Yamasaki, K.1    Kurimura, M.2    Kasai, T.3    Sagara, M.4    Kodama, T.5    Inoue, K.6
  • 3
    • 77952316540 scopus 로고    scopus 로고
    • An integrated view of humoral innate immunity: Pentraxins as a paradigm
    • Bottazzi, B., A. Doni, C. Garlanda, and A. Mantovani. 2010. An integrated view of humoral innate immunity: pentraxins as a paradigm. Annu. Rev. Immunol. 28: 157-183.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 157-183
    • Bottazzi, B.1    Doni, A.2    Garlanda, C.3    Mantovani, A.4
  • 4
    • 0025360897 scopus 로고
    • Isolation and characterization of eight tumor necrosis factor-induced gene sequences from human fibroblasts
    • Lee, T. H., G. W. Lee, E. B. Ziff, and J. Vilcek. 1990. Isolation and characterization of eight tumor necrosis factor-induced gene sequences from human fibroblasts. Mol. Cell. Biol. 10: 1982-1988.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1982-1988
    • Lee, T.H.1    Lee, G.W.2    Ziff, E.B.3    Vilcek, J.4
  • 6
    • 77955081427 scopus 로고    scopus 로고
    • The long pentraxin PTX3: A modulator of the immunoinflammatory response in atherosclerosis and cardiovascular diseases
    • Norata, G. D., C. Garlanda, and A. L. Catapano. 2010. The long pentraxin PTX3: a modulator of the immunoinflammatory response in atherosclerosis and cardiovascular diseases. Trends Cardiovasc. Med. 20: 35-40.
    • (2010) Trends Cardiovasc. Med. , vol.20 , pp. 35-40
    • Norata, G.D.1    Garlanda, C.2    Catapano, A.L.3
  • 14
    • 79952777211 scopus 로고    scopus 로고
    • Heterocomplexes of mannose-binding lectin and the pentraxins PTX3 or serum amyloid P component trigger cross-activation of the complement system
    • Ma, Y. J., A. Doni, M. O. Skjoedt, C. Honoré, M. Arendrup, A. Mantovani, and P. Garred. 2011. Heterocomplexes of mannose-binding lectin and the pentraxins PTX3 or serum amyloid P component trigger cross-activation of the complement system. J. Biol. Chem. 286: 3405-3417.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3405-3417
    • Ma, Y.J.1    Doni, A.2    Skjoedt, M.O.3    Honoré, C.4    Arendrup, M.5    Mantovani, A.6    Garred, P.7
  • 16
    • 58849092356 scopus 로고    scopus 로고
    • Binding of the long pentraxin PTX3 to factor H: Interacting domains and function in the regulation of complement activation
    • Deban, L., H. Jarva, M. J. Lehtinen, B. Bottazzi, A. Bastone, A. Doni, T. S. Jokiranta, A. Mantovani, and S. Meri. 2008. Binding of the long pentraxin PTX3 to factor H: interacting domains and function in the regulation of complement activation. J. Immunol. 181: 8433-8440.
    • (2008) J. Immunol. , vol.181 , pp. 8433-8440
    • Deban, L.1    Jarva, H.2    Lehtinen, M.J.3    Bottazzi, B.4    Bastone, A.5    Doni, A.6    Jokiranta, T.S.7    Mantovani, A.8    Meri, S.9
  • 17
    • 80051917349 scopus 로고    scopus 로고
    • Human pentraxin 3 binds to the complement regulator c4b-binding protein
    • Braunschweig, A., and M. Józsi. 2011. Human pentraxin 3 binds to the complement regulator c4b-binding protein. PLoS ONE 6: e23991.
    • (2011) PLoS ONE , vol.6
    • Braunschweig, A.1    Józsi, M.2
  • 18
    • 77954315059 scopus 로고    scopus 로고
    • Complement control protein factor H: The good, the bad, and the inadequate
    • Ferreira, V. P., M. K. Pangburn, and C. Cortés. 2010. Complement control protein factor H: the good, the bad, and the inadequate. Mol. Immunol. 47: 2187-2197.
    • (2010) Mol. Immunol. , vol.47 , pp. 2187-2197
    • Ferreira, V.P.1    Pangburn, M.K.2    Cortés, C.3
  • 19
    • 1642518600 scopus 로고    scopus 로고
    • Attachment of the soluble complement regulator factor H to cell and tissue surfaces: Relevance for pathology
    • Józsi, M., T. Manuelian, S. Heinen, M. Oppermann, and P. F. Zipfel. 2004. Attachment of the soluble complement regulator factor H to cell and tissue surfaces: relevance for pathology. Histol. Histopathol. 19: 251-258. (Pubitemid 38120210)
    • (2004) Histology and Histopathology , vol.19 , Issue.1 , pp. 251-258
    • Jozsi, M.1    Manuelian, T.2    Heinen, S.3    Oppermann, M.4    Zipfel, P.F.5
  • 20
    • 0036838535 scopus 로고    scopus 로고
    • Cutting edge: Localization of the host recognition functions of complement factor H at the carboxyl-terminal: Implications for hemolytic uremic syndrome
    • Pangburn, M. K. 2002. Cutting edge: localization of the host recognition functions of complement factor H at the carboxyl-terminal: implications for hemolytic uremic syndrome. J. Immunol. 169: 4702-4706. (Pubitemid 35217129)
    • (2002) Journal of Immunology , vol.169 , Issue.9 , pp. 4702-4706
    • Pangburn, M.K.1
  • 21
    • 33846911766 scopus 로고    scopus 로고
    • The C-terminus of complement factor H is essential for host cell protection
    • DOI 10.1016/j.molimm.2006.12.001, PII S0161589006007231
    • Józsi, M., M. Oppermann, J. D. Lambris, and P. F. Zipfel. 2007. The C-terminus of complement factor H is essential for host cell protection. Mol. Immunol. 44: 2697-2706. (Pubitemid 46240314)
    • (2007) Molecular Immunology , vol.44 , Issue.10 , pp. 2697-2706
    • Jozsi, M.1    Oppermann, M.2    Lambris, J.D.3    Zipfel, P.F.4
  • 22
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu, J., Y. Q. Wu, D. Ricklin, B. J. Janssen, J. D. Lambris, and P. Gros. 2009. Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat. Immunol. 10: 728-733.
    • (2009) Nat. Immunol. , vol.10 , pp. 728-733
    • Wu, J.1    Wu, Y.Q.2    Ricklin, D.3    Janssen, B.J.4    Lambris, J.D.5    Gros, P.6
  • 23
    • 0033033505 scopus 로고    scopus 로고
    • FHL-1/reconectin: A human complement and immune regulator with cell- adhesive function
    • DOI 10.1016/S0167-5699(98)01432-7, PII S0167569998014327
    • Zipfel, P. F., and C. Skerka. 1999. FHL-1/reconectin: a human complement and immune regulator with cell-adhesive function. Immunol. Today 20: 135-140. (Pubitemid 29130343)
    • (1999) Immunology Today , vol.20 , Issue.3 , pp. 135-140
    • Zipfel, P.F.1    Skerka, C.2
  • 24
    • 36849084660 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H
    • de Córdoba, S. R., and E. G. de Jorge. 2008. Translational mini-review series on complement factor H: genetics and disease associations of human complement factor H. Clin. Exp. Immunol. 151: 1-13.
    • (2008) Clin. Exp. Immunol. , vol.151 , pp. 1-13
    • De Córdoba, S.R.1    De Jorge, E.G.2
  • 25
    • 47749126514 scopus 로고    scopus 로고
    • Factor H family proteins and human diseases
    • Józsi, M., and P. F. Zipfel. 2008. Factor H family proteins and human diseases. Trends Immunol. 29: 380-387.
    • (2008) Trends Immunol. , vol.29 , pp. 380-387
    • Józsi, M.1    Zipfel, P.F.2
  • 26
    • 70350279315 scopus 로고    scopus 로고
    • Atypical hemolytic-uremic syndrome
    • Noris, M., and G. Remuzzi. 2009. Atypical hemolytic-uremic syndrome. N. Engl. J. Med. 361: 1676-1687.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 1676-1687
    • Noris, M.1    Remuzzi, G.2
  • 28
    • 38949155911 scopus 로고    scopus 로고
    • Factor H autoantibodies in atypical hemolytic uremic syndrome correlate with CFHR1/CFHR3 deficiency
    • DOI 10.1182/blood-2007-09-109876
    • Józsi, M., C. Licht, S. Strobel, S. L. Zipfel, H. Richter, S. Heinen, P. F. Zipfel, and C. Skerka. 2008. Factor H autoantibodies in atypical hemolytic uremic syndrome correlate with CFHR1/CFHR3 deficiency. Blood 111: 1512-1514. (Pubitemid 351213440)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1512-1514
    • Jozsi, M.1    Licht, C.2    Strobel, S.3    Zipfel, S.L.H.4    Richter, H.5    Heinen, S.6    Zipfel, P.F.7    Skerka, C.8
  • 29
    • 34548853385 scopus 로고    scopus 로고
    • Anti-factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome
    • DOI 10.1182/blood-2007-02-071472
    • Józsi, M., S. Strobel, H. M. Dahse, W. S. Liu, P. F. Hoyer, M. Oppermann, C. Skerka, and P. F. Zipfel. 2007. Anti factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome. Blood 110: 1516-1518. (Pubitemid 47443967)
    • (2007) Blood , vol.110 , Issue.5 , pp. 1516-1518
    • Jozsi, M.1    Strobel, S.2    Dahse, H.-M.3    Liu, W.-S.4    Hoyer, P.F.5    Oppermann, M.6    Skerka, C.7    Zipfel, P.F.8
  • 31
    • 67650129379 scopus 로고    scopus 로고
    • Mutations of factor H impair regulation of surface-bound C3b by three mechanisms in atypical hemolytic uremic syndrome
    • Lehtinen, M. J., A. L. Rops, D. E. Isenman, J. van der Vlag, and T. S. Jokiranta. 2009. Mutations of factor H impair regulation of surface-bound C3b by three mechanisms in atypical hemolytic uremic syndrome. J. Biol. Chem. 284: 15650-15658.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15650-15658
    • Lehtinen, M.J.1    Rops, A.L.2    Isenman, D.E.3    Van Der Vlag, J.4    Jokiranta, T.S.5
  • 34
    • 76949087440 scopus 로고    scopus 로고
    • Characterization of complement factor H-related (CFHR) proteins in plasma reveals novel genetic variations of CFHR1 associated with atypical hemolytic uremic syndrome
    • Abarrategui-Garrido, C., R. Martínez-Barricarte, M. López-Trascasa, S. R. de Córdoba, and P. Sánchez-Corral. 2009. Characterization of complement factor H-related (CFHR) proteins in plasma reveals novel genetic variations of CFHR1 associated with atypical hemolytic uremic syndrome. Blood 114: 4261-4271.
    • (2009) Blood , vol.114 , pp. 4261-4271
    • Abarrategui-Garrido, C.1    Martínez-Barricarte, R.2    López- Trascasa, M.3    De Córdoba, S.R.4    Sánchez-Corral, P.5
  • 35
    • 75649133611 scopus 로고    scopus 로고
    • Association of factor H autoantibodies with deletions of CFHR1, CFHR3, CFHR4, and with mutations in CFH, CFI, CD46, and C3 in patients with atypical hemolytic uremic syndrome
    • Moore, I., L. Strain, I. Pappworth, D. Kavanagh, P. N. Barlow, A. P. Herbert, C. Q. Schmidt, S. J. Staniforth, L. V. Holmes, R. Ward, et al. 2010. Association of factor H autoantibodies with deletions of CFHR1, CFHR3, CFHR4, and with mutations in CFH, CFI, CD46, and C3 in patients with atypical hemolytic uremic syndrome. Blood 115: 379-387.
    • (2010) Blood , vol.115 , pp. 379-387
    • Moore, I.1    Strain, L.2    Pappworth, I.3    Kavanagh, D.4    Barlow, P.N.5    Herbert, A.P.6    Schmidt, C.Q.7    Staniforth, S.J.8    Holmes, L.V.9    Ward, R.10
  • 36
    • 67650508077 scopus 로고    scopus 로고
    • The high frequency of complement factor H related CFHR1 gene deletion is restricted to specific subgroups of patients with atypical haemolytic uraemic syndrome
    • Dragon-Durey, M. A., C. Blanc, F. Marliot, C. Loirat, J. Blouin, C. Sautes- Fridman, W. H. Fridman, and V. Frémeaux-Bacchi. 2009. The high frequency of complement factor H related CFHR1 gene deletion is restricted to specific subgroups of patients with atypical haemolytic uraemic syndrome. J. Med. Genet. 46: 447-450.
    • (2009) J. Med. Genet. , vol.46 , pp. 447-450
    • Dragon-Durey, M.A.1    Blanc, C.2    Marliot, F.3    Loirat, C.4    Blouin, J.5    Sautes-Fridman, C.6    Fridman, W.H.7    Frémeaux-Bacchi, V.8
  • 38
    • 0029081018 scopus 로고
    • The baculovirus expression vector pBSV-8His directs secretion of histidine-tagged proteins
    • Kühn, S., and P. F. Zipfel. 1995. The baculovirus expression vector pBSV-8His directs secretion of histidine-tagged proteins. Gene 162: 225-229.
    • (1995) Gene , vol.162 , pp. 225-229
    • Kühn, S.1    Zipfel, P.F.2
  • 39
    • 0032526881 scopus 로고    scopus 로고
    • Complement activation occurs on subendothelial extracellular matrix in vitro and is initiated by retraction or removal of overlying endothelial cells
    • Hindmarsh, E. J., and R. M. Marks. 1998. Complement activation occurs on subendothelial extracellular matrix in vitro and is initiated by retraction or removal of overlying endothelial cells. J. Immunol. 160: 6128-6136. (Pubitemid 28298077)
    • (1998) Journal of Immunology , vol.160 , Issue.12 , pp. 6128-6136
    • Hindmarsh, E.J.1    Marks, R.M.2
  • 40
    • 33646164894 scopus 로고    scopus 로고
    • Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome
    • Jokiranta, T. S., V. P. Jaakola, M. J. Lehtinen, M. Pärepalo, S. Meri, and A. Goldman. 2006. Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome. EMBO J. 25: 1784-1794.
    • (2006) EMBO J. , vol.25 , pp. 1784-1794
    • Jokiranta, T.S.1    Jaakola, V.P.2    Lehtinen, M.J.3    Pärepalo, M.4    Meri, S.5    Goldman, A.6
  • 41
    • 0035071662 scopus 로고    scopus 로고
    • The effects of extracellular pH on immune function
    • Lardner, A. 2001. The effects of extracellular pH on immune function. J. Leukoc. Biol. 69: 522-530. (Pubitemid 32294836)
    • (2001) Journal of Leukocyte Biology , vol.69 , Issue.4 , pp. 522-530
    • Lardner, A.1
  • 43
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjöberg, A. P., G. A. Manderson, M. Mörgelin, A. J. Day, D. Heinegård, and A. M. Blom. 2009. Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation. Mol. Immunol. 46: 830-839.
    • (2009) Mol. Immunol. , vol.46 , pp. 830-839
    • Sjöberg, A.P.1    Manderson, G.A.2    Mörgelin, M.3    Day, A.J.4    Heinegård, D.5    Blom, A.M.6
  • 46
    • 84862321570 scopus 로고    scopus 로고
    • The proteomic profile of circulating pentraxin 3 (PTX3) complex in sepsis demonstrates the interaction with azurocidin 1 and other components of neutrophil extracellular traps
    • 10.1074/mcp.M111.015073
    • Daigo, K., N. Yamaguchi, T. Kawamura, K. Matsubara, S. Jiang, R. Ohashi, Y. Sudou, T. Kodama, M. Naito, K. Inoue, and T. Hamakubo. 2012. The proteomic profile of circulating pentraxin 3 (PTX3) complex in sepsis demonstrates the interaction with azurocidin 1 and other components of neutrophil extracellular traps. Mol. Cell. Proteomics 11: M111.015073. 10.1074/mcp.M111.015073.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Daigo, K.1    Yamaguchi, N.2    Kawamura, T.3    Matsubara, K.4    Jiang, S.5    Ohashi, R.6    Sudou, Y.7    Kodama, T.8    Naito, M.9    Inoue, K.10    Hamakubo, T.11
  • 47
    • 60349127531 scopus 로고    scopus 로고
    • Complement activation and inhibition: A delicate balance
    • Sjöberg, A. P., L. A. Trouw, and A. M. Blom. 2009. Complement activation and inhibition: a delicate balance. Trends Immunol. 30: 83-90.
    • (2009) Trends Immunol. , vol.30 , pp. 83-90
    • Sjöberg, A.P.1    Trouw, L.A.2    Blom, A.M.3
  • 48
    • 0031881259 scopus 로고    scopus 로고
    • Decay-accelerating factor is a component of subendothelial extracellular matrix in vitro, and is augmented by activation of endothelial protein kinase C
    • DOI 10.1002/(SICI)1521-4141(199803)28:03<1052::AID-IMMU1052>3.0. CO;2-W
    • Hindmarsh, E. J., and R. M. Marks. 1998. Decay-accelerating factor is a component of subendothelial extracellular matrix in vitro, and is augmented by activation of endothelial protein kinase C. Eur. J. Immunol. 28: 1052-1062. (Pubitemid 28116219)
    • (1998) European Journal of Immunology , vol.28 , Issue.3 , pp. 1052-1062
    • Hindmarsh, E.J.1    Marks, R.M.2
  • 49
    • 77956897697 scopus 로고    scopus 로고
    • Impaired binding of the age-related macular degeneration-associated complement factor H 402H allotype to Bruch's membrane in human retina
    • Clark, S. J., R. Perveen, S. Hakobyan, B. P. Morgan, R. B. Sim, P. N. Bishop, and A. J. Day. 2010. Impaired binding of the age-related macular degeneration-associated complement factor H 402H allotype to Bruch's membrane in human retina. J. Biol. Chem. 285: 30192-30202.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30192-30202
    • Clark, S.J.1    Perveen, R.2    Hakobyan, S.3    Morgan, B.P.4    Sim, R.B.5    Bishop, P.N.6    Day, A.J.7
  • 53
    • 33645577856 scopus 로고    scopus 로고
    • Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: Mutational studies using recombinant globular head modules of human C1q A, B, and C chains
    • Roumenina, L. T., M. M. Ruseva, A. Zlatarova, R. Ghai, M. Kolev, N. Olova, M. Gadjeva, A. Agrawal, B. Bottazzi, A. Mantovani, et al. 2006. Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: mutational studies using recombinant globular head modules of human C1q A, B, and C chains. Biochemistry 45: 4093-4104.
    • (2006) Biochemistry , vol.45 , pp. 4093-4104
    • Roumenina, L.T.1    Ruseva, M.M.2    Zlatarova, A.3    Ghai, R.4    Kolev, M.5    Olova, N.6    Gadjeva, M.7    Agrawal, A.8    Bottazzi, B.9    Mantovani, A.10
  • 54
    • 2342582709 scopus 로고    scopus 로고
    • Functional analysis in serum from atypical Hemolytic Uremic Syndrome patients reveals impaired protection of host cells associated with mutations in factor H
    • DOI 10.1016/j.molimm.2004.01.003, PII S0161589004000422
    • Sánchez-Corral, P., C. González-Rubio, S. Rodríguez de Córdoba, and M. López-Trascasa. 2004. Functional analysis in serum from atypical Hemolytic Uremic Syndrome patients reveals impaired protection of host cells associated with mutations in factor H. Mol. Immunol. 41: 81-84. (Pubitemid 38609399)
    • (2004) Molecular Immunology , vol.41 , Issue.1 , pp. 81-84
    • Sanchez-Corral, P.1    Gonzalez-Rubio, C.2    Rodriguez, D.C.S.3    Lopez-Trascasa, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.