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Volumn 2, Issue 1, 2012, Pages 46-75

Factor H: A complement regulator in health and disease, and a mediator of cellular interactions

Author keywords

Apoptotic cell; Cell adhesion; Complement; Extracellular matrix; Factor H; Inflammation; Pentraxin

Indexed keywords

ADRENOMEDULLIN; C REACTIVE PROTEIN; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C3B; COMPLEMENT FACTOR H; DNA; FIBROMODULIN; FICOLIN; GLYCOSAMINOGLYCAN; HEPARIN; HISTONE; IMMUNOGLOBULIN G; LIPOCORTIN 2; MANNOSE BINDING LECTIN 2; PENTRAXIN; PRION PROTEIN;

EID: 84861727429     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom2010046     Document Type: Review
Times cited : (111)

References (166)
  • 1
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov, R. Recognition of microorganisms and activation of the immune response. Nature 2007, 449, 819-826.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 2
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport, M.J. Complement. First of two parts. N. Engl. J. Med. 2001, 344, 1058-1066.
    • (2001) N. Engl. J. Med , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 3
    • 0035849176 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • Walport, M.J. Complement. Second of two parts. N. Engl. J. Med. 2001, 344, 1140-1144.
    • (2001) N. Engl. J. Med , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 4
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • Ricklin, D.; Hajishengallis, G.; Yang, K.; Lambris, J.D. Complement: A key system for immune surveillance and homeostasis. Nat. Immunol. 2010, 11, 785-797.
    • (2010) Nat. Immunol , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 5
    • 34848886930 scopus 로고    scopus 로고
    • Loss of self-control in the complement system and innate autoreactivity
    • Meri, S. Loss of self-control in the complement system and innate autoreactivity. Ann. NY Acad. Sci. 2007, 1109, 93-105.
    • (2007) Ann. NY Acad. Sci , vol.1109 , pp. 93-105
    • Meri, S.1
  • 6
    • 36849084660 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H
    • Rodríguez de Córdoba, S.; Goicoechea de Jorge, E. Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H. Clin. Exp. Immunol. 2008, 151, 1-13.
    • (2008) Clin. Exp. Immunol , vol.151 , pp. 1-13
    • Rodríguez de Córdoba, S.1    Goicoechea de Jorge, E.2
  • 8
    • 47749126514 scopus 로고    scopus 로고
    • Factor H family proteins and human diseases
    • Józsi, M.; Zipfel, P.F. Factor H family proteins and human diseases. Trends Immunol. 2008, 29, 380-387.
    • (2008) Trends Immunol , vol.29 , pp. 380-387
    • Józsi, M.1    Zipfel, P.F.2
  • 9
    • 0000332710 scopus 로고
    • Isolation of beta 1F-globulin from human serum and its characterization as the fifth component of complement
    • Nilsson, U.R.; Müller-Eberhard, H.J. Isolation of beta 1F-globulin from human serum and its characterization as the fifth component of complement. J. Exp. Med. 1965, 122, 277-298.
    • (1965) J. Exp. Med , vol.122 , pp. 277-298
    • Nilsson, U.R.1    Müller-Eberhard, H.J.2
  • 11
    • 0242574494 scopus 로고    scopus 로고
    • Ontogeny of complement regulatory proteins-concentrations of factor H, factor I, C4b-binding protein, properdin and vitronectin in healthy children of different ages and in adults
    • de Paula, P.F.; Barbosa, J.E.; Junior, P.R.; Ferriani, V.P.; Latorre, M.R.; Nudelman, V.; Isaac, L. Ontogeny of complement regulatory proteins-concentrations of factor H, factor I, C4b-binding protein, properdin and vitronectin in healthy children of different ages and in adults. Scand. J. Immunol. 2003, 58, 572-577.
    • (2003) Scand. J. Immunol , vol.58 , pp. 572-577
    • de Paula, P.F.1    Barbosa, J.E.2    Junior, P.R.3    Ferriani, V.P.4    Latorre, M.R.5    Nudelman, V.6    Isaac, L.7
  • 14
    • 77957575143 scopus 로고    scopus 로고
    • Variant-specific quantification of factor H in plasma identifies null alleles associated with atypical hemolytic uremic syndrome
    • Hakobyan, S.; Tortajada, A.; Harris, C.L.; Rodríguez de Córdoba, S.; Morgan, B.P. Variant-specific quantification of factor H in plasma identifies null alleles associated with atypical hemolytic uremic syndrome. Kidney Int. 2010, 78, 782-788.
    • (2010) Kidney Int , vol.78 , pp. 782-788
    • Hakobyan, S.1    Tortajada, A.2    Harris, C.L.3    Rodríguez de Córdoba, S.4    Morgan, B.P.5
  • 15
    • 0018864029 scopus 로고
    • Biosynthesis of the complement components and the regulatory proteins of the alternative complement pathway by human peripheral blood monocytes
    • Whaley, K. Biosynthesis of the complement components and the regulatory proteins of the alternative complement pathway by human peripheral blood monocytes. J. Exp. Med. 1980, 151, 501-516.
    • (1980) J. Exp. Med , vol.151 , pp. 501-516
    • Whaley, K.1
  • 16
    • 0023681768 scopus 로고
    • Synthesis and regulation of complement protein factor H in human skin fibroblasts
    • Katz, Y.; Strunk, R.C. Synthesis and regulation of complement protein factor H in human skin fibroblasts. J. Immunol. 1988, 141, 559-563.
    • (1988) J. Immunol , vol.141 , pp. 559-563
    • Katz, Y.1    Strunk, R.C.2
  • 17
    • 0025359563 scopus 로고
    • Differential regulation of complement factor H and C3 production in human umbilical vein endothelial cells by IFN-gamma and IL-1
    • Brooimans, R.A.; Van der Ark, A.A.; Buurman, W.A.; Van Es, L.A.; Daha, M.R. Differential regulation of complement factor H and C3 production in human umbilical vein endothelial cells by IFN-gamma and IL-1. J. Immunol. 1990, 144, 3835-3840.
    • (1990) J. Immunol , vol.144 , pp. 3835-3840
    • Brooimans, R.A.1    Van der Ark, A.A.2    Buurman, W.A.3    Van Es, L.A.4    Daha, M.R.5
  • 19
    • 0023277944 scopus 로고
    • Regulation of the activity of platelet-bound C3 convertase of the alternative pathway of complement by platelet factor H
    • Devine, D.V.; Rosse, W.F. Regulation of the activity of platelet-bound C3 convertase of the alternative pathway of complement by platelet factor H. Proc. Natl. Acad. Sci. USA 1987, 84, 5873-5877.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5873-5877
    • Devine, D.V.1    Rosse, W.F.2
  • 20
    • 33947160639 scopus 로고    scopus 로고
    • Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments
    • Chen, M.; Forrester, J.V.; Xu, H. Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments. Exp. Eye Res. 2007, 84, 635-645.
    • (2007) Exp. Eye Res , vol.84 , pp. 635-645
    • Chen, M.1    Forrester, J.V.2    Xu, H.3
  • 21
    • 0023875503 scopus 로고
    • The complete amino acid sequence of human complement factor H
    • Ripoche, J.; Day, A.J.; Harris, T.J.; Sim, R.B. The complete amino acid sequence of human complement factor H. Biochem. J. 1988, 249, 593-602.
    • (1988) Biochem. J , vol.249 , pp. 593-602
    • Ripoche, J.1    Day, A.J.2    Harris, T.J.3    Sim, R.B.4
  • 22
    • 0012042656 scopus 로고
    • Control of the amplification convertase of complement by the plasma protein beta1H
    • Weiler, J.M.; Daha, M.R.; Austen, K.F.; Fearon, D.T. Control of the amplification convertase of complement by the plasma protein beta1H. Proc. Natl. Acad. Sci. USA 1976, 73, 3268-3272.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3268-3272
    • Weiler, J.M.1    Daha, M.R.2    Austen, K.F.3    Fearon, D.T.4
  • 23
    • 0017139872 scopus 로고
    • Modulation of the alternative complement pathway by beta 1H globulin
    • Whaley, K.; Ruddy, S. Modulation of the alternative complement pathway by beta 1H globulin. J. Exp. Med. 1976, 144, 1147-1163.
    • (1976) J. Exp. Med , vol.144 , pp. 1147-1163
    • Whaley, K.1    Ruddy, S.2
  • 24
    • 0017704496 scopus 로고
    • Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution
    • Pangburn, M.K.; Schreiber, R.D.; Müller-Eberhard, H.J. Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution. J. Exp. Med. 1977, 146, 257-270.
    • (1977) J. Exp. Med , vol.146 , pp. 257-270
    • Pangburn, M.K.1    Schreiber, R.D.2    Müller-Eberhard, H.J.3
  • 26
    • 0028875543 scopus 로고
    • Mapping of the complement regulatory domains in the human factor H-like protein 1 and in factor H1
    • Kühn, S.; Skerka, C.; Zipfel, P.F. Mapping of the complement regulatory domains in the human factor H-like protein 1 and in factor H1. J. Immunol. 1995, 155, 5663-5670.
    • (1995) J. Immunol , vol.155 , pp. 5663-5670
    • Kühn, S.1    Skerka, C.2    Zipfel, P.F.3
  • 27
    • 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. Cutting edge: Localization of the host recognition functions of complement factor H at the carboxyl-terminal: Implications for hemolytic uremic syndrome. J. Immunol. 2002, 169, 4702-4706.
    • (2002) J. Immunol , vol.169 , pp. 4702-4706
    • Pangburn, M.K.1
  • 29
    • 0025314311 scopus 로고
    • Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H
    • Meri, S.; Pangburn, M.K. Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H. Proc. Natl. Acad. Sci. USA 1990, 87, 3982-3986.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3982-3986
    • Meri, S.1    Pangburn, M.K.2
  • 30
    • 0033921990 scopus 로고    scopus 로고
    • Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement
    • Pangburn, M.K. Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement. Immunopharmacology 2000, 49, 149-157.
    • (2000) Immunopharmacology , vol.49 , pp. 149-157
    • Pangburn, M.K.1
  • 31
    • 33750336175 scopus 로고    scopus 로고
    • Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces
    • Ferreira, V.P.; Herbert, A.P.; Hocking, H.G.; Barlow, P.N.; Pangburn, M.K. Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces. J. Immunol. 2006, 177, 6308-6316.
    • (2006) J. Immunol , vol.177 , pp. 6308-6316
    • Ferreira, V.P.1    Herbert, A.P.2    Hocking, H.G.3    Barlow, P.N.4    Pangburn, M.K.5
  • 32
    • 33846911766 scopus 로고    scopus 로고
    • The C-terminus of complement factor H is essential for host cell protection
    • Józsi, M.; Oppermann, M.; Lambris, J.D.; Zipfel, P.F. The C-terminus of complement factor H is essential for host cell protection. Mol. Immunol. 2007, 44, 2697-2706.
    • (2007) Mol. Immunol , vol.44 , pp. 2697-2706
    • Józsi, M.1    Oppermann, M.2    Lambris, J.D.3    Zipfel, P.F.4
  • 33
    • 1642518600 scopus 로고    scopus 로고
    • Attachment of the soluble complement regulator factor H to cell and tissue surfaces: Relevance for pathology
    • Józsi, M.; Manuelian, T.; Heinen, S.; Oppermann, M.; Zipfel, P.F. Attachment of the soluble complement regulator factor H to cell and tissue surfaces: Relevance for pathology. Histol. Histopathol. 2004, 19, 251-258.
    • (2004) Histol. Histopathol , vol.19 , pp. 251-258
    • Józsi, M.1    Manuelian, T.2    Heinen, S.3    Oppermann, M.4    Zipfel, P.F.5
  • 34
    • 60349127531 scopus 로고    scopus 로고
    • Complement activation and inhibition: A delicate balance
    • Sjöberg, A.P.; Trouw, L.A.; Blom, A.M. Complement activation and inhibition: A delicate balance. Trends Immunol. 2008, 30, 83-90.
    • (2008) Trends Immunol , vol.30 , pp. 83-90
    • Sjöberg, A.P.1    Trouw, L.A.2    Blom, A.M.3
  • 36
    • 0029763437 scopus 로고    scopus 로고
    • Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis
    • Sharma, A.K.; Pangburn, M.K. Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis. Proc. Natl. Acad. Sci. USA 1996, 93, 10996-11001.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 37
    • 0034623118 scopus 로고    scopus 로고
    • Each of the three binding sites on complement factor H interacts with a distinct site on C3b
    • Jokiranta, T.S.; Hellwage, J.; Koistinen, V.; Zipfel, P.F.; Meri, S. Each of the three binding sites on complement factor H interacts with a distinct site on C3b. J. Biol. Chem. 2000, 275, 27657-27662.
    • (2000) J. Biol. Chem , vol.275 , pp. 27657-27662
    • Jokiranta, T.S.1    Hellwage, J.2    Koistinen, V.3    Zipfel, P.F.4    Meri, S.5
  • 40
    • 0033214998 scopus 로고    scopus 로고
    • Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11
    • Jarva, H.; Jokiranta, T.S.; Hellwage, J.; Zipfel, P.F.; Meri, S. Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11. J. Immunol. 1999, 163, 3957-3962.
    • (1999) J. Immunol , vol.163 , pp. 3957-3962
    • Jarva, H.1    Jokiranta, T.S.2    Hellwage, J.3    Zipfel, P.F.4    Meri, S.5
  • 41
    • 70449724676 scopus 로고    scopus 로고
    • Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H
    • Mihlan, M.; Stippa, S.; Józsi, M.; Zipfel, P.F. Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H. Cell Death Differ. 2009, 16, 1630-1640.
    • (2009) Cell Death Differ , vol.16 , pp. 1630-1640
    • Mihlan, M.1    Stippa, S.2    Józsi, M.3    Zipfel, P.F.4
  • 42
    • 74049141427 scopus 로고    scopus 로고
    • Complement factor H binds at two independent sites to C-reactive protein in acute phase concentrations
    • Okemefuna, A.I.; Nan, R.; Miller, A.; Gor, J.; Perkins, S.J. Complement factor H binds at two independent sites to C-reactive protein in acute phase concentrations. J. Biol. Chem. 2010, 285, 1053-1065.
    • (2010) J. Biol. Chem , vol.285 , pp. 1053-1065
    • Okemefuna, A.I.1    Nan, R.2    Miller, A.3    Gor, J.4    Perkins, S.J.5
  • 43
    • 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.; Jarva, H.; Lehtinen, M.J.; Bottazzi, B.; Bastone, A.; Doni, A.; Jokiranta, T.S.; Mantovani, A.; Meri, S. Binding of the long pentraxin PTX3 to factor H: Interacting domains and function in the regulation of complement activation. J. Immunol. 2008, 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
  • 44
    • 0034613686 scopus 로고    scopus 로고
    • C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity
    • Gershov, D.; Kim, S.; Brot, N.; Elkon, K.B. C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity. J. Exp. Med. 2000, 192, 1353-1364.
    • (2000) J. Exp. Med , vol.192 , pp. 1353-1364
    • Gershov, D.1    Kim, S.2    Brot, N.3    Elkon, K.B.4
  • 45
    • 35348980673 scopus 로고    scopus 로고
    • C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack
    • Trouw, L.A.; Bengtsson, A.A.; Gelderman, K.A.; Dahlbäck, B.; Sturfelt, G.; Blom, A.M. C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. J. Biol. Chem. 2007, 282, 28540-28548.
    • (2007) J. Biol. Chem , vol.282 , pp. 28540-28548
    • Trouw, L.A.1    Bengtsson, A.A.2    Gelderman, K.A.3    Dahlbäck, B.4    Sturfelt, G.5    Blom, A.M.6
  • 47
    • 25444482114 scopus 로고    scopus 로고
    • The extracellular matrix and inflammation: Fibromodulin activates the classical pathway of complement by directly binding C1q
    • Sjöberg, A.; Onnerfjord, P.; Mörgelin, M.; Heinegård, D.; Blom, A.M. The extracellular matrix and inflammation: Fibromodulin activates the classical pathway of complement by directly binding C1q. J. Biol. Chem. 2005, 280, 32301-32308.
    • (2005) J. Biol. Chem , vol.280 , pp. 32301-32308
    • Sjöberg, A.1    Onnerfjord, P.2    Mörgelin, M.3    Heinegård, D.4    Blom, A.M.5
  • 48
    • 34249740145 scopus 로고    scopus 로고
    • The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells
    • Sjöberg, A.P.; Trouw, L.A.; Clark, S.J.; Sjölander, J.; Heinegård, D.; Sim, R.B.; Day, A.J.; Blom, A.M. The factor H variant associated with age-related macular degeneration (His-384) and the non-disease-associated form bind differentially to C-reactive protein, fibromodulin, DNA, and necrotic cells. J. Biol. Chem. 2007, 282, 10894-10900.
    • (2007) J. Biol. Chem , vol.282 , pp. 10894-10900
    • Sjöberg, A.P.1    Trouw, L.A.2    Clark, S.J.3    Sjölander, J.4    Heinegård, D.5    Sim, R.B.6    Day, A.J.7    Blom, A.M.8
  • 49
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjöberg, A.; Manderson, G.A.; Mörgelin, M.; Day, A.J.; Heinegård, D.; Blom, A.M. Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation. Mol. Immunol. 2009, 46, 830-839.
    • (2009) Mol. Immunol , vol.46 , pp. 830-839
    • Sjöberg, A.1    Manderson, G.A.2    Mörgelin, M.3    Day, A.J.4    Heinegård, D.5    Blom, A.M.6
  • 51
    • 43449086676 scopus 로고    scopus 로고
    • Native, amyloid fibrils and beta-oligomers of the C-terminal domain of human prion protein display differential activation of complement and bind C1q, factor H and C4b-binding protein directly
    • Sjöberg, A.P.; Nyström, S.; Hammarström, P.; Blom, A.M. Native, amyloid fibrils and beta-oligomers of the C-terminal domain of human prion protein display differential activation of complement and bind C1q, factor H and C4b-binding protein directly. Mol. Immunol. 2008, 45, 3213-3221.
    • (2008) Mol. Immunol , vol.45 , pp. 3213-3221
    • Sjöberg, A.P.1    Nyström, S.2    Hammarström, P.3    Blom, A.M.4
  • 52
    • 0035853722 scopus 로고    scopus 로고
    • Complement factor H is a serum-binding protein for adrenomedullin, and the resulting complex modulates the bioactivities of both partners
    • Pio, R.; Martinez, A.; Unsworth, E.J.; Kowalak, J.A.; Bengoechea, J.A.; Zipfel, P.F.; Elsasser, T.H.; Cuttitta, F. Complement factor H is a serum-binding protein for adrenomedullin, and the resulting complex modulates the bioactivities of both partners. J. Biol. Chem. 2001, 276, 12292-12300.
    • (2001) J. Biol. Chem , vol.276 , pp. 12292-12300
    • Pio, R.1    Martinez, A.2    Unsworth, E.J.3    Kowalak, J.A.4    Bengoechea, J.A.5    Zipfel, P.F.6    Elsasser, T.H.7    Cuttitta, F.8
  • 53
    • 0037301209 scopus 로고    scopus 로고
    • Mapping of the adrenomedullin-binding domains in human complement factor H
    • Suppl:S59
    • Martínez, A.; Pío, R.; Zipfel, P.F.; Cuttitta, F. Mapping of the adrenomedullin-binding domains in human complement factor H. Hypertens. Res. 2003, 26, Suppl:S55-Suppl:S59.
    • (2003) Hypertens. Res , vol.26 , Issue.SUPPL.
    • Martínez, A.1    Pío, R.2    Zipfel, P.F.3    Cuttitta, F.4
  • 54
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu, J.; Wu, Y.Q.; Ricklin, D.; Janssen, B.J.; Lambris, J.D.; Gros, P. Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat. Immunol. 2009, 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
  • 57
    • 0030589294 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H
    • Blackmore, T.K.; Sadlon, T.A.; Ward, H.M.; Lublin, D.M.; Gordon, D.L. Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H. J. Immunol. 1996, 157, 5422-5427.
    • (1996) J. Immunol , vol.157 , pp. 5422-5427
    • Blackmore, T.K.1    Sadlon, T.A.2    Ward, H.M.3    Lublin, D.M.4    Gordon, D.L.5
  • 59
    • 0026044042 scopus 로고
    • Localization of the heparin-binding site on complement factor H
    • Pangburn, M.K.; Atkinson, M.A.; Meri, S. Localization of the heparin-binding site on complement factor H. J. Biol. Chem. 1991, 266, 16847-16853.
    • (1991) J. Biol. Chem , vol.266 , pp. 16847-16853
    • Pangburn, M.K.1    Atkinson, M.A.2    Meri, S.3
  • 60
    • 0037374138 scopus 로고    scopus 로고
    • Recognition and clearance of apoptotic cells: A role for complement and pentraxins
    • Nauta, A.J.; Daha, M.R.; van Kooten, C.; Roos, A. Recognition and clearance of apoptotic cells: A role for complement and pentraxins. Trends Immunol. 2003, 24, 148-154.
    • (2003) Trends Immunol , vol.24 , pp. 148-154
    • Nauta, A.J.1    Daha, M.R.2    van Kooten, C.3    Roos, A.4
  • 61
    • 77952316540 scopus 로고    scopus 로고
    • An integrated view of humoral innate immunity: Pentraxins as a paradigm
    • Bottazzi, B.; Doni, A.; Garlanda, C.; Mantovani, A. An integrated view of humoral innate immunity: Pentraxins as a paradigm. Annu. Rev. Immunol. 2010, 28, 157-183.
    • (2010) Annu. Rev. Immunol , vol.28 , pp. 157-183
    • Bottazzi, B.1    Doni, A.2    Garlanda, C.3    Mantovani, A.4
  • 63
    • 0042744797 scopus 로고    scopus 로고
    • C-reactive protein: A critical update
    • Pepys, M.B.; Hirschfield, G.M. C-reactive protein: A critical update. J. Clin. Invest. 2003, 111, 1805-1812.
    • (2003) J. Clin. Invest , vol.111 , pp. 1805-1812
    • Pepys, M.B.1    Hirschfield, G.M.2
  • 65
    • 0016199986 scopus 로고
    • Interaction of C-reactive protein complexes with the complement system. II. Consumption of guinea pig complement by CRP complexes: Requirement for human C1q
    • Volanakis, J.E.; Kaplan, M.H. Interaction of C-reactive protein complexes with the complement system. II. Consumption of guinea pig complement by CRP complexes: Requirement for human C1q. J. Immunol. 1974, 113, 9-17.
    • (1974) J. Immunol , vol.113 , pp. 9-17
    • Volanakis, J.E.1    Kaplan, M.H.2
  • 66
    • 34547195138 scopus 로고    scopus 로고
    • C-reactive protein collaborates with plasma lectins to boost immune response against bacteria
    • Ng, P.M.; Le Saux, A.; Lee, C.M.; Tan, N.S.; Lu, J.; Thiel, S.; Ho, B.; Ding, J.L. C-reactive protein collaborates with plasma lectins to boost immune response against bacteria. EMBO J. 2007, 26, 3431-3440.
    • (2007) EMBO J , vol.26 , pp. 3431-3440
    • Ng, P.M.1    Le Saux, A.2    Lee, C.M.3    Tan, N.S.4    Lu, J.5    Thiel, S.6    Ho, B.7    Ding, J.L.8
  • 67
    • 57749172475 scopus 로고    scopus 로고
    • Structural recognition and functional activation of FcgammaR by innate pentraxins
    • Lu, J.; Marnell, L.L.; Marjon, K.D.; Mold, C.; Du Clos, T.W.; Sun, P.D. Structural recognition and functional activation of FcgammaR by innate pentraxins. Nature 2008, 456, 989-992.
    • (2008) Nature , vol.456 , pp. 989-992
    • Lu, J.1    Marnell, L.L.2    Marjon, K.D.3    Mold, C.4    Du Clos, T.W.5    Sun, P.D.6
  • 68
    • 57749086715 scopus 로고    scopus 로고
    • Human complement factor H-related protein 4 binds and recruits native pentameric C-reactive protein to necrotic cells
    • Mihlan, M.; Hebecker, M.; Dahse, H.M.; Hälbich, S.; Huber-Lang, M.; Dahse, R.; Zipfel, P.F.; Józsi, M. Human complement factor H-related protein 4 binds and recruits native pentameric C-reactive protein to necrotic cells. Mol. Immunol. 2009, 46, 335-344.
    • (2009) Mol. Immunol , vol.46 , pp. 335-344
    • Mihlan, M.1    Hebecker, M.2    Dahse, H.M.3    Hälbich, S.4    Huber-Lang, M.5    Dahse, R.6    Zipfel, P.F.7    Józsi, M.8
  • 70
    • 33846001313 scopus 로고    scopus 로고
    • Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate: MCRP(m)
    • Ji, S.R.; Wu, Y.; Zhu, L.; Potempa, L.A.; Sheng, F.L.; Lu, W.; Zhao, J. Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate: mCRP(m). FASEB J. 2007, 21, 284-294.
    • (2007) FASEB J , vol.21 , pp. 284-294
    • Ji, S.R.1    Wu, Y.2    Zhu, L.3    Potempa, L.A.4    Sheng, F.L.5    Lu, W.6    Zhao, J.7
  • 72
    • 0032992715 scopus 로고    scopus 로고
    • Regulation of complement activation by C-reactive protein
    • Mold, C.; Gewurz, H.; Du Clos, T.W. Regulation of complement activation by C-reactive protein. Immunopharmacology 1999, 42, 23-30.
    • (1999) Immunopharmacology , vol.42 , pp. 23-30
    • Mold, C.1    Gewurz, H.2    Du Clos, T.W.3
  • 76
    • 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.; Doni, A.; Skjoedt, M.O.; Honoré, C.; Arendrup, M.; Mantovani, A.; Garred, P. Heterocomplexes of mannose-binding lectin and the pentraxins PTX3 or serum amyloid P component trigger cross-activation of the complement system. J. Biol. Chem. 2011, 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
  • 79
    • 80051917349 scopus 로고    scopus 로고
    • Human pentraxin 3 binds to the complement regulator C4b-binding protein
    • Braunschweig, A.; Józsi, M. Human pentraxin 3 binds to the complement regulator C4b-binding protein. PLoS One 2011, 6, e23991.
    • (2011) PLoS One , vol.6
    • Braunschweig, A.1    Józsi, M.2
  • 80
    • 85016369210 scopus 로고    scopus 로고
    • Interaction of the long pentraxin PTX3 with soluble complement inhibitors
    • Braunschweig, A.; Józsi, M. Interaction of the long pentraxin PTX3 with soluble complement inhibitors. Mol. Immunol. 2010, 47, 2234-2235.
    • (2010) Mol. Immunol , vol.47 , pp. 2234-2235
    • Braunschweig, A.1    Józsi, M.2
  • 81
    • 85016366361 scopus 로고    scopus 로고
    • Impaired binding of factor H to pentraxin 3 due to factor H mutations and autoantibodies associated with atypical hemolytic uremic syndrome
    • Braunschweig, A.; Strobel, S.; Józsi M. Impaired binding of factor H to pentraxin 3 due to factor H mutations and autoantibodies associated with atypical hemolytic uremic syndrome. Mol. Immunol. 2011, 48, 1722.
    • (2011) Mol. Immunol , vol.48 , pp. 1722
    • Braunschweig, A.1    Strobel, S.2    Józsi, M.3
  • 82
    • 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.; Perveen, R.; Hakobyan, S.; Morgan, B.P.; Sim, R.B.; Bishop, P.N.; Day, A.J. Impaired binding of the age-related macular degeneration-associated complement factor H 402H allotype to Bruch's membrane in human retina. J. Biol. Chem. 2010, 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
  • 85
    • 0033384014 scopus 로고    scopus 로고
    • FHL-1/reconectin and factor H: Two human complement regulators which are encoded by the same gene are differently expressed and regulated
    • Friese, M.A.; Hellwage, J.; Jokiranta, T.S.; Meri, S.; Peter, H.H.; Eibel, H.; Zipfel, P.F. FHL-1/reconectin and factor H: Two human complement regulators which are encoded by the same gene are differently expressed and regulated. Mol. Immunol. 1999, 36, 809-818.
    • (1999) Mol. Immunol , vol.36 , pp. 809-818
    • Friese, M.A.1    Hellwage, J.2    Jokiranta, T.S.3    Meri, S.4    Peter, H.H.5    Eibel, H.6    Zipfel, P.F.7
  • 86
    • 0030868761 scopus 로고    scopus 로고
    • The human complement regulatory factor-H-like protein 1, which represents a truncated form of factor H, displays cell-attachment activity
    • Hellwage, J.; Kühn, S.; Zipfel, P.F. The human complement regulatory factor-H-like protein 1, which represents a truncated form of factor H, displays cell-attachment activity. Biochem. J. 1997, 326, 321-327.
    • (1997) Biochem. J , vol.326 , pp. 321-327
    • Hellwage, J.1    Kühn, S.2    Zipfel, P.F.3
  • 88
    • 76249101650 scopus 로고    scopus 로고
    • Factor H and factor H-related protein 1 bind to human neutrophils via complement receptor 3, mediate attachment to Candida albicans, and enhance neutrophil antimicrobial activity
    • Losse, J.; Zipfel, P.F.; Józsi, M. Factor H and factor H-related protein 1 bind to human neutrophils via complement receptor 3, mediate attachment to Candida albicans, and enhance neutrophil antimicrobial activity. J. Immunol. 2010, 184, 912-921.
    • (2010) J. Immunol , vol.184 , pp. 912-921
    • Losse, J.1    Zipfel, P.F.2    Józsi, M.3
  • 89
    • 79952454215 scopus 로고    scopus 로고
    • The significance of the complement system for the pathogenesis of age-related macular degeneration-current evidence and translation into clinical application
    • Charbel Issa, P.; Chong, N.V.; Scholl, H.P. The significance of the complement system for the pathogenesis of age-related macular degeneration-current evidence and translation into clinical application. Graefes Arch. Clin. Exp. Ophthalmol. 2011, 249, 163-174.
    • (2011) Graefes Arch. Clin. Exp. Ophthalmol , vol.249 , pp. 163-174
    • Charbel Issa, P.1    Chong, N.V.2    Scholl, H.P.3
  • 94
    • 33749123246 scopus 로고    scopus 로고
    • A common CFH haplotype, with deletion of CFHR1 and CFHR3, is associated with lower risk of age-related macular degeneration
    • Hughes, A.E.; Orr, N.; Esfandiary, H.; Diaz-Torres, M.; Goodship, T.; Chakravarthy, U. A common CFH haplotype, with deletion of CFHR1 and CFHR3, is associated with lower risk of age-related macular degeneration. Nat. Genet. 2006, 38, 1173-1177.
    • (2006) Nat. Genet , vol.38 , pp. 1173-1177
    • Hughes, A.E.1    Orr, N.2    Esfandiary, H.3    Diaz-Torres, M.4    Goodship, T.5    Chakravarthy, U.6
  • 96
    • 34447581121 scopus 로고    scopus 로고
    • Biochemical analysis of a common human polymorphism associated with age-related macular degeneration
    • Yu, J.; Wiita, P.; Kawaguchi, R.; Honda, J.; Jorgensen, A.; Zhang, K.; Fischetti, V.A.; Sun, H. Biochemical analysis of a common human polymorphism associated with age-related macular degeneration. Biochemistry 2007, 46, 8451-8461.
    • (2007) Biochemistry , vol.46 , pp. 8451-8461
    • Yu, J.1    Wiita, P.2    Kawaguchi, R.3    Honda, J.4    Jorgensen, A.5    Zhang, K.6    Fischetti, V.A.7    Sun, H.8
  • 97
    • 34547102526 scopus 로고    scopus 로고
    • Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism
    • Herbert, A.P.; Deakin, J.A.; Schmidt, C.Q.; Blaum, B.S.; Egan, C.; Ferreira, V.P.; Pangburn, M.K.; Lyon, M.; Uhrín, D.; Barlow, P.N. Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism. J. Biol. Chem. 2007, 282, 18960-18968.
    • (2007) J. Biol. Chem , vol.282 , pp. 18960-18968
    • Herbert, A.P.1    Deakin, J.A.2    Schmidt, C.Q.3    Blaum, B.S.4    Egan, C.5    Ferreira, V.P.6    Pangburn, M.K.7    Lyon, M.8    Uhrín, D.9    Barlow, P.N.10
  • 99
    • 33747700932 scopus 로고    scopus 로고
    • His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form
    • Clark, S.J.; Higman, V.A.; Mulloy, B.; Perkins, S.J.; Lea, S.M.; Sim, R.B.; Day, A.J. His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form. J. Biol. Chem. 2006, 281, 24713-24720.
    • (2006) J. Biol. Chem , vol.281 , pp. 24713-24720
    • Clark, S.J.1    Higman, V.A.2    Mulloy, B.3    Perkins, S.J.4    Lea, S.M.5    Sim, R.B.6    Day, A.J.7
  • 102
  • 104
    • 53849086825 scopus 로고    scopus 로고
    • Complement factor H allotype 402H is associated with increased C3b opsonization and phagocytosis of Streptococcus pyogenes
    • Haapasalo, K.; Jarva, H.; Siljander, T.; Tewodros, W.; Vuopio-Varkila, J.; Jokiranta, T.S. Complement factor H allotype 402H is associated with increased C3b opsonization and phagocytosis of Streptococcus pyogenes. Mol. Microbiol. 2008, 70, 583-594.
    • (2008) Mol. Microbiol , vol.70 , pp. 583-594
    • Haapasalo, K.1    Jarva, H.2    Siljander, T.3    Tewodros, W.4    Vuopio-Varkila, J.5    Jokiranta, T.S.6
  • 105
    • 84855392622 scopus 로고    scopus 로고
    • Acquisition of complement factor H is important for pathogenesis of streptococcus pyogenes infections: Evidence from bacterial in vitro survival and human genetic association
    • Haapasalo, K.; Vuopio, J.; Syrjänen, J.; Suvilehto, J.; Massinen, S.; Karppelin, M.; Järvelä, I.; Meri, S.; Kere, J.; Jokiranta, T.S. Acquisition of complement factor H is important for pathogenesis of streptococcus pyogenes infections: Evidence from bacterial in vitro survival and human genetic association. J. Immunol. 2012, 188, 426-435.
    • (2012) J. Immunol , vol.188 , pp. 426-435
    • Haapasalo, K.1    Vuopio, J.2    Syrjänen, J.3    Suvilehto, J.4    Massinen, S.5    Karppelin, M.6    Järvelä, I.7    Meri, S.8    Kere, J.9    Jokiranta, T.S.10
  • 107
    • 70350279315 scopus 로고    scopus 로고
    • Atypical hemolytic-uremic syndrome
    • Noris, M.; Remuzzi, G. Atypical hemolytic-uremic syndrome. N. Engl. J. Med. 2009, 361, 1676-1687.
    • (2009) N. Engl. J. Med , vol.361 , pp. 1676-1687
    • Noris, M.1    Remuzzi, G.2
  • 112
    • 33746655453 scopus 로고    scopus 로고
    • De novo gene conversion in the RCA gene cluster (1q32) causes mutations in complement factor H associated with atypical hemolytic uremic syndrome
    • Heinen, S.; Sanchez-Corral, P.; Jackson, M.S.; Strain, L.; Goodship, J.A.; Kemp, E.J.; Skerka, C.; Jokiranta, T.S.; Meyers, K.; Wagner, E.; et al. De novo gene conversion in the RCA gene cluster (1q32) causes mutations in complement factor H associated with atypical hemolytic uremic syndrome. Hum. Mutat. 2006, 27, 292-293.
    • (2006) Hum. Mutat , vol.27 , pp. 292-293
    • Heinen, S.1    Sanchez-Corral, P.2    Jackson, M.S.3    Strain, L.4    Goodship, J.A.5    Kemp, E.J.6    Skerka, C.7    Jokiranta, T.S.8    Meyers, K.9    Wagner, E.10
  • 116
    • 38949155911 scopus 로고    scopus 로고
    • Factor H autoantibodies in atypical hemolytic uremic syndrome correlate with CFHR1/CFHR3 deficiency
    • Józsi, M.; Licht, C.; Strobel, S.; Zipfel, S.L.; Richter, H.; Heinen, S.; Zipfel, P.F.; Skerka, C. Factor H autoantibodies in atypical hemolytic uremic syndrome correlate with CFHR1/CFHR3 deficiency. Blood 2008, 111, 1512-1514.
    • (2008) Blood , vol.111 , pp. 1512-1514
    • Józsi, M.1    Licht, C.2    Strobel, S.3    Zipfel, S.L.4    Richter, H.5    Heinen, S.6    Zipfel, P.F.7    Skerka, C.8
  • 117
    • 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.; Blanc, C.; Marliot, F.; Loirat, C.; Blouin, J.; Sautes-Fridman, C.; Fridman, W.H.; Frémeaux-Bacchi, V. 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. 2009, 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
  • 118
    • 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.; Martínez-Barricarte, R.; López-Trascasa, M.; Rodríguez de Córdoba, S.; Sánchez-Corral, P. Characterization of complement factor H-related (CFHR) proteins in plasma reveals novel genetic variations of CFHR1 associated with atypical hemolytic uremic syndrome. Blood 2009, 114, 4261-4271.
    • (2009) Blood , vol.114 , pp. 4261-4271
    • Abarrategui-Garrido, C.1    Martínez-Barricarte, R.2    López-Trascasa, M.3    Rodríguez de Córdoba, S.4    Sánchez-Corral, P.5
  • 119
    • 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.; Strain, L.; Pappworth, I.; Kavanagh, D.; Barlow, P.N.; Herbert, A.P.; Schmidt, C.Q.; Staniforth, S.J.; Holmes, L.V.; Ward, R.; et al. 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 2010, 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
  • 120
    • 34548853385 scopus 로고    scopus 로고
    • Anti factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome
    • Józsi, M.; Strobel, S.; Dahse, H.M.; Liu, W.S.; Hoyer, P.F.; Oppermann, M.; Skerka, C.; Zipfel, P.F. Anti factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome. Blood 2007, 110, 1516-1518.
    • (2007) Blood , vol.110 , pp. 1516-1518
    • Józsi, 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
  • 123
    • 83655191999 scopus 로고    scopus 로고
    • Complement factor H variants I890 and L1007 while commonly associated with atypical hemolytic uremic syndrome are polymorphisms with no functional significance
    • Tortajada, A.; Pinto, S.; Martínez-Ara, J.; López-Trascasa, M.; Sánchez-Corral, P.; Rodríguez de Córdoba, S. Complement factor H variants I890 and L1007 while commonly associated with atypical hemolytic uremic syndrome are polymorphisms with no functional significance. Kidney Int. 2012, 81, 56-63.
    • (2012) Kidney Int , vol.81 , pp. 56-63
    • Tortajada, A.1    Pinto, S.2    Martínez-Ara, J.3    López-Trascasa, M.4    Sánchez-Corral, P.5    Rodríguez de Córdoba, S.6
  • 125
    • 62449129937 scopus 로고    scopus 로고
    • Hereditary and acquired complement dysregulation in membranoproliferative glomerulonephritis
    • Licht, C.; Fremeaux-Bacchi, V. Hereditary and acquired complement dysregulation in membranoproliferative glomerulonephritis. Thromb. Haemost. 2009, 101, 271-278.
    • (2009) Thromb. Haemost , vol.101 , pp. 271-278
    • Licht, C.1    Fremeaux-Bacchi, V.2
  • 126
    • 1542318912 scopus 로고    scopus 로고
    • Heterozygous and homozygous factor H deficiencies associated with hemolytic uremic syndrome or membranoproliferative glomerulonephritis: Report and genetic analysis of 16 cases
    • Dragon-Durey, M.A.; Frémeaux-Bacchi, V.; Loirat, C.; Blouin, J.; Niaudet, P.; Deschenes, G.; Coppo, P.; Herman Fridman, W.; Weiss, L. Heterozygous and homozygous factor H deficiencies associated with hemolytic uremic syndrome or membranoproliferative glomerulonephritis: Report and genetic analysis of 16 cases. J. Am. Soc. Nephrol. 2004, 15, 787-795.
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 787-795
    • Dragon-Durey, M.A.1    Frémeaux-Bacchi, V.2    Loirat, C.3    Blouin, J.4    Niaudet, P.5    Deschenes, G.6    Coppo, P.7    Herman Fridman, W.8    Weiss, L.9
  • 127
    • 0030823285 scopus 로고    scopus 로고
    • Human factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolism
    • Ault, B.H.; Schmidt, B.Z.; Fowler, N.L.; Kashtan, C.E.; Ahmed, A.E.; Vogt, B.A.; Colten, H.R. Human factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolism. J. Biol. Chem. 1997, 272, 25168-25175.
    • (1997) J. Biol. Chem , vol.272 , pp. 25168-25175
    • Ault, B.H.1    Schmidt, B.Z.2    Fowler, N.L.3    Kashtan, C.E.4    Ahmed, A.E.5    Vogt, B.A.6    Colten, H.R.7
  • 128
    • 41849110155 scopus 로고    scopus 로고
    • Genetic deficiency of complement factor H in a patient with age-related macular degeneration and membranoproliferative glomerulonephritis
    • Montes, T.; Goicoechea de Jorge, E.; Ramos, R.; Gomà, M.; Pujol, O.; Sánchez-Corral, P.; Rodríguez de Córdoba, S. Genetic deficiency of complement factor H in a patient with age-related macular degeneration and membranoproliferative glomerulonephritis. Mol. Immunol. 2008, 45, 2897-2904.
    • (2008) Mol. Immunol , vol.45 , pp. 2897-2904
    • Montes, T.1    Goicoechea de Jorge, E.2    Ramos, R.3    Gomà, M.4    Pujol, O.5    Sánchez-Corral, P.6    Rodríguez de Córdoba, S.7
  • 130
    • 0026549476 scopus 로고
    • Activation of the alternative pathway of complement by monoclonal lambda light chains in membranoproliferative glomerulonephritis
    • Meri, S.; Koistinen, V.; Miettinen, A.; Törnroth, T.; Seppälä, I.J. Activation of the alternative pathway of complement by monoclonal lambda light chains in membranoproliferative glomerulonephritis. J. Exp. Med. 1992, 175, 939-950.
    • (1992) J. Exp. Med , vol.175 , pp. 939-950
    • Meri, S.1    Koistinen, V.2    Miettinen, A.3    Törnroth, T.4    Seppälä, I.J.5
  • 131
    • 0032875669 scopus 로고    scopus 로고
    • Nephritogenic lambda light chain dimer: A unique human miniautoantibody against complement factor H
    • Jokiranta, T.S.; Solomon, A.; Pangburn, M.K.; Zipfel, P.F.; Meri, S. Nephritogenic lambda light chain dimer: A unique human miniautoantibody against complement factor H. J. Immunol. 1999, 163, 4590-4596.
    • (1999) J. Immunol , vol.163 , pp. 4590-4596
    • Jokiranta, T.S.1    Solomon, A.2    Pangburn, M.K.3    Zipfel, P.F.4    Meri, S.5
  • 134
    • 0029896853 scopus 로고    scopus 로고
    • Complement activation on human neuroblastoma cell lines in vitro: Route of activation and expression of functional complement regulatory proteins
    • Gasque, P.; Thomas, A.; Fontaine, M.; Morgan, B.P. Complement activation on human neuroblastoma cell lines in vitro: Route of activation and expression of functional complement regulatory proteins. J. Neuroimmunol. 1996, 66, 29-40.
    • (1996) J. Neuroimmunol , vol.66 , pp. 29-40
    • Gasque, P.1    Thomas, A.2    Fontaine, M.3    Morgan, B.P.4
  • 135
    • 0034040022 scopus 로고    scopus 로고
    • Exceptional resistance of human H2 glioblastoma cells to complement-mediated killing by expression and utilization of factor H and factor H-like protein 1
    • Junnikkala, S.; Jokiranta, T.S.; Friese, M.A.; Jarva, H.; Zipfel, P.F.; Meri, S. Exceptional resistance of human H2 glioblastoma cells to complement-mediated killing by expression and utilization of factor H and factor H-like protein 1. J. Immunol. 2000, 164, 6075-6081.
    • (2000) J. Immunol , vol.164 , pp. 6075-6081
    • Junnikkala, S.1    Jokiranta, T.S.2    Friese, M.A.3    Jarva, H.4    Zipfel, P.F.5    Meri, S.6
  • 136
  • 137
    • 4344689094 scopus 로고    scopus 로고
    • Expression of complement factor H by lung cancer cells: Effects on the activation of the alternative pathway of complement
    • Ajona, D.; Castaño, Z.; Garayoa, M.; Zudaire, E.; Pajares, M.J.; Martinez, A.; Cuttitta, F.; Montuenga, L.M.; Pio, R. Expression of complement factor H by lung cancer cells: Effects on the activation of the alternative pathway of complement. Cancer Res. 2004, 64, 6310-6318.
    • (2004) Cancer Res , vol.64 , pp. 6310-6318
    • Ajona, D.1    Castaño, Z.2    Garayoa, M.3    Zudaire, E.4    Pajares, M.J.5    Martinez, A.6    Cuttitta, F.7    Montuenga, L.M.8    Pio, R.9
  • 141
    • 0034596062 scopus 로고    scopus 로고
    • Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack
    • Fedarko, N.S.; Fohr, B.; Robey, P.G.; Young, M.F.; Fisher, L.W. Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. J. Biol. Chem. 2000, 275, 16666-16672.
    • (2000) J. Biol. Chem , vol.275 , pp. 16666-16672
    • Fedarko, N.S.1    Fohr, B.2    Robey, P.G.3    Young, M.F.4    Fisher, L.W.5
  • 143
    • 0019191997 scopus 로고
    • Release of endogenous C3b inactivator from lymphocytes in response to triggering membrane receptors for β1H globulin
    • Lambris, J.D.; Dobson, N.J.; Ross, G.D. Release of endogenous C3b inactivator from lymphocytes in response to triggering membrane receptors for β1H globulin. J. Exp. Med. 1980, 152, 1625-1644.
    • (1980) J. Exp. Med , vol.152 , pp. 1625-1644
    • Lambris, J.D.1    Dobson, N.J.2    Ross, G.D.3
  • 144
    • 0019801851 scopus 로고
    • beta 1H stimulates mouse-spleen B lymphocytes as demonstrated by increased thymidine incorporation and formation of B cell blasts
    • Hammann, K.P.; Raile, A.; Schmitt, M.; Mussel, H.H.; Peters, H.; Scheiner, O.; Dierich, M.P. beta 1H stimulates mouse-spleen B lymphocytes as demonstrated by increased thymidine incorporation and formation of B cell blasts. Immunobiology 1981, 160, 289-301.
    • (1981) Immunobiology , vol.160 , pp. 289-301
    • Hammann, K.P.1    Raile, A.2    Schmitt, M.3    Mussel, H.H.4    Peters, H.5    Scheiner, O.6    Dierich, M.P.7
  • 146
    • 0020071683 scopus 로고
    • Characterization of the lymphocyte membrane receptor for factor H (β1H-globulin) with an antibody to anti-factor H idiotype
    • Lambris, J.D.; Ross, G.D. Characterization of the lymphocyte membrane receptor for factor H (β1H-globulin) with an antibody to anti-factor H idiotype. J. Exp. Med. 1982, 155, 1400-1411.
    • (1982) J. Exp. Med , vol.155 , pp. 1400-1411
    • Lambris, J.D.1    Ross, G.D.2
  • 147
    • 0023655709 scopus 로고
    • Complement Factor H-binding protein of Raji cells and tonsil B lymphocytes
    • Erdei, A.; Sim, R.B. Complement Factor H-binding protein of Raji cells and tonsil B lymphocytes. Biochem. J. 1987, 246, 149-156.
    • (1987) Biochem. J , vol.246 , pp. 149-156
    • Erdei, A.1    Sim, R.B.2
  • 148
    • 0027496024 scopus 로고
    • Characterization of factor H binding to human polymorphonuclear leukocytes
    • Avery, V.M.; Gordon, D.L. Characterization of factor H binding to human polymorphonuclear leukocytes. J. Immunol. 1993, 151, 5545-5553.
    • (1993) J. Immunol , vol.151 , pp. 5545-5553
    • Avery, V.M.1    Gordon, D.L.2
  • 149
    • 0032522811 scopus 로고    scopus 로고
    • Human polymorphonuclear leukocytes adhere to complement factor H through an interaction that involves alphaMbeta2 (CD11b/CD18)
    • DiScipio, R.G.; Daffern, P.J.; Schraufstätter, I.U.; Sriramarao, P. Human polymorphonuclear leukocytes adhere to complement factor H through an interaction that involves alphaMbeta2 (CD11b/CD18). J. Immunol. 1998, 160, 4057-4066.
    • (1998) J. Immunol , vol.160 , pp. 4057-4066
    • DiScipio, R.G.1    Daffern, P.J.2    Schraufstätter, I.U.3    Sriramarao, P.4
  • 150
    • 77954933122 scopus 로고    scopus 로고
    • Complement regulator Factor H mediates a two-step uptake of Streptococcus pneumoniae by human cells
    • Agarwal, V.; Asmat, T.M.; Luo, S.; Jensch, I.; Zipfel, P.F.; Hammerschmidt, S. Complement regulator Factor H mediates a two-step uptake of Streptococcus pneumoniae by human cells. J. Biol. Chem. 2010, 285, 23486-23495.
    • (2010) J. Biol. Chem , vol.285 , pp. 23486-23495
    • Agarwal, V.1    Asmat, T.M.2    Luo, S.3    Jensch, I.4    Zipfel, P.F.5    Hammerschmidt, S.6
  • 151
    • 77958118756 scopus 로고    scopus 로고
    • Factor H facilitates adherence of Neisseria gonorrhoeae to complement receptor 3 on eukaryotic cells
    • Agarwal, S.; Ram, S.; Ngampasutadol, J.; Gulati, S.; Zipfel, P.F.; Rice, P.A. Factor H facilitates adherence of Neisseria gonorrhoeae to complement receptor 3 on eukaryotic cells. J. Immunol. 2010, 185, 4344-4353.
    • (2010) J. Immunol , vol.185 , pp. 4344-4353
    • Agarwal, S.1    Ram, S.2    Ngampasutadol, J.3    Gulati, S.4    Zipfel, P.F.5    Rice, P.A.6
  • 152
    • 0036789954 scopus 로고    scopus 로고
    • Association of factor H of the alternative pathway of complement with agrin and complement receptor 3 in the Alzheimer's disease brain
    • Strohmeyer, R.; Ramirez, M.; Cole, G.J.; Mueller, K.; Rogers, J. Association of factor H of the alternative pathway of complement with agrin and complement receptor 3 in the Alzheimer's disease brain. J. Neuroimmunol. 2002, 131, 135-146.
    • (2002) J. Neuroimmunol , vol.131 , pp. 135-146
    • Strohmeyer, R.1    Ramirez, M.2    Cole, G.J.3    Mueller, K.4    Rogers, J.5
  • 154
    • 0025882503 scopus 로고
    • Evidence for an active hydrophobic form of factor H that is able to induce secretion of interleukin 1-beta or by human monocytes
    • Iferroudjene, D.; Schouft, M.T.; Lemercier, C.; Gilbert, D.; Fontaine, M. Evidence for an active hydrophobic form of factor H that is able to induce secretion of interleukin 1-beta or by human monocytes. Eur. J. Immunol. 1991, 21, 967-972.
    • (1991) Eur. J. Immunol , vol.21 , pp. 967-972
    • Iferroudjene, D.1    Schouft, M.T.2    Lemercier, C.3    Gilbert, D.4    Fontaine, M.5
  • 157
    • 0021264152 scopus 로고
    • Release of prostaglandin E and thromboxane from macrophages by stimulation with factor H
    • Hartung, H.P.; Hadding, U.; Bitter-Suermann, D.; Gemsa, D. Release of prostaglandin E and thromboxane from macrophages by stimulation with factor H. Clin. Exp. Immunol. 1984, 56, 453-458.
    • (1984) Clin. Exp. Immunol , vol.56 , pp. 453-458
    • Hartung, H.P.1    Hadding, U.2    Bitter-Suermann, D.3    Gemsa, D.4
  • 158
    • 84858006658 scopus 로고    scopus 로고
    • Human complement Factor H modulates C1q-mediated phagocytosis of apoptotic cells
    • October 23 doi:10.1016/j.imbio.2011.10.008
    • Kang, Y.H.; Urban, B.C.; Sim, R.B.; Kishore, U. Human complement Factor H modulates C1q-mediated phagocytosis of apoptotic cells. Immunobiology 2011, October 23, doi:10.1016/j.imbio.2011.10.008.
    • (2011) Immunobiology
    • Kang, Y.H.1    Urban, B.C.2    Sim, R.B.3    Kishore, U.4
  • 160
    • 0033166496 scopus 로고    scopus 로고
    • Identification of human complement Factor H as a ligand for L-selectin
    • Malhotra, R.; Ward, M.; Sim, R.B.; Bird, M.I. Identification of human complement Factor H as a ligand for L-selectin. Biochem. J. 1999, 341, 61-69.
    • (1999) Biochem. J , vol.341 , pp. 61-69
    • Malhotra, R.1    Ward, M.2    Sim, R.B.3    Bird, M.I.4
  • 162
    • 55349092344 scopus 로고    scopus 로고
    • Factor H binds to platelet integrin alphaIIbbeta3
    • Mnjoyan, Z.; Li, J.; Afshar-Kharghan, V. Factor H binds to platelet integrin alphaIIbbeta3. Platelets 2008, 19, 512-519.
    • (2008) Platelets , vol.19 , pp. 512-519
    • Mnjoyan, Z.1    Li, J.2    Afshar-Kharghan, V.3
  • 164
    • 79151485902 scopus 로고    scopus 로고
    • Production of biologically active complement factor H in therapeutically useful quantities
    • Schmidt, C.Q.; Slingsby, F.C.; Richards, A.; Barlow, P.N. Production of biologically active complement factor H in therapeutically useful quantities. Protein Expr. Purif. 2011, 76, 254-263.
    • (2011) Protein Expr. Purif , vol.76 , pp. 254-263
    • Schmidt, C.Q.1    Slingsby, F.C.2    Richards, A.3    Barlow, P.N.4
  • 166
    • 80052145222 scopus 로고    scopus 로고
    • Interactions of complement proteins C1q and factor H with lipid A and Escherichia coli: Further evidence that factor H regulates the classical complement pathway
    • Tan, L.A.; Yang, A.C.; Kishore, U.; Sim, R.B. Interactions of complement proteins C1q and factor H with lipid A and Escherichia coli: Further evidence that factor H regulates the classical complement pathway. Protein Cell 2011, 2, 320-332.
    • (2011) Protein Cell , vol.2 , pp. 320-332
    • Tan, L.A.1    Yang, A.C.2    Kishore, U.3    Sim, R.B.4


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