메뉴 건너뛰기




Volumn 274, Issue 1, 2016, Pages 218-232

Complement in removal of the dead – balancing inflammation

Author keywords

apoptosis; clearance; complement system; factor H; intracellular complement; systemic lupus erythematosus

Indexed keywords

AUTOANTIBODY; AUTOANTIGEN; CALRETICULIN; CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1Q ANTIBODY; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C4B; COMPLEMENT COMPONENT C4B BINDING PROTEIN; COMPLEMENT COMPONENT C5A; COMPLEMENT COMPONENT C5A RECEPTOR; COMPLEMENT COMPONENT C5B; COMPLEMENT COMPONENT C6; COMPLEMENT COMPONENT C7; COMPLEMENT COMPONENT C8; COMPLEMENT FACTOR H; COMPLEMENT FACTOR I; COMPLEMENT INHIBITOR; COMPLEMENT MEMBRANE ATTACK COMPLEX; COMPLEMENT RECEPTOR; FIBRINOGEN; FICOLIN; INFLAMMASOME; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; MANNOSE BINDING LECTIN; PENTRAXIN 3; PROPERDIN;

EID: 84992449530     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12462     Document Type: Review
Times cited : (95)

References (178)
  • 1
    • 84865417273 scopus 로고    scopus 로고
    • The C1q family of proteins: insights into the emerging non-traditional functions
    • Ghebrehiwet B, Hosszu KK, Valentino A, Peerschke EI. The C1q family of proteins: insights into the emerging non-traditional functions. Front Immunol. 2012;3:52.
    • (2012) Front Immunol , vol.3 , pp. 52
    • Ghebrehiwet, B.1    Hosszu, K.K.2    Valentino, A.3    Peerschke, E.I.4
  • 2
    • 0033947551 scopus 로고    scopus 로고
    • C1q: structure, function, and receptors
    • Kishore U, Reid KB. C1q: structure, function, and receptors. Immunopharmacology. 2000;49:159–170.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 3
    • 0028178458 scopus 로고
    • beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain
    • Jiang H, Burdick D, Glabe CG, Cotman CW, Tenner AJ. beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain. J Immunol. 1994;152:5050–5059.
    • (1994) J Immunol , vol.152 , pp. 5050-5059
    • Jiang, H.1    Burdick, D.2    Glabe, C.G.3    Cotman, C.W.4    Tenner, A.J.5
  • 4
    • 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
    • Sjoberg AP, Nystrom S, Hammarstrom P, Blom AM. 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
    • Sjoberg, A.P.1    Nystrom, S.2    Hammarstrom, P.3    Blom, A.M.4
  • 5
    • 33644541441 scopus 로고    scopus 로고
    • Evidence that complement protein C1q interacts with C-reactive protein through its globular head region
    • McGrath FD, Brouwer MC, Arlaud GJ, Daha MR, Hack CE, Roos A. Evidence that complement protein C1q interacts with C-reactive protein through its globular head region. J Immunol. 2006;176:2950–2957.
    • (2006) J Immunol , vol.176 , pp. 2950-2957
    • McGrath, F.D.1    Brouwer, M.C.2    Arlaud, G.J.3    Daha, M.R.4    Hack, C.E.5    Roos, A.6
  • 6
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjoberg AP, Manderson GA, Morgelin M, Day AJ, Heinegard D, Blom AM. 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
    • Sjoberg, A.P.1    Manderson, G.A.2    Morgelin, M.3    Day, A.J.4    Heinegard, D.5    Blom, A.M.6
  • 7
    • 25444482114 scopus 로고    scopus 로고
    • The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q
    • Sjoberg A, Onnerfjord P, Morgelin M, Heinegard D, Blom AM. 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
    • Sjoberg, A.1    Onnerfjord, P.2    Morgelin, M.3    Heinegard, D.4    Blom, A.M.5
  • 8
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden CA, deCathelineau A, Hoffmann PR. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med. 2001;194:781–795.
    • (2001) J Exp Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    deCathelineau, A.2    Hoffmann, P.R.3
  • 9
    • 0026493918 scopus 로고
    • DNA binds and activates complement via residues 14-26 of the human C1q A chain
    • Jiang H, Cooper B, Robey FA, Gewurz H. DNA binds and activates complement via residues 14-26 of the human C1q A chain. J Biol Chem. 1992;267:25597–25601.
    • (1992) J Biol Chem , vol.267 , pp. 25597-25601
    • Jiang, H.1    Cooper, B.2    Robey, F.A.3    Gewurz, H.4
  • 10
    • 0020329226 scopus 로고
    • Fibronectin binds to the C1q component of complement
    • Bing DH, Almeda S, Isliker H, Lahav J, Hynes RO. Fibronectin binds to the C1q component of complement. PNAS. 1982;79:4198–4201.
    • (1982) PNAS , vol.79 , pp. 4198-4201
    • Bing, D.H.1    Almeda, S.2    Isliker, H.3    Lahav, J.4    Hynes, R.O.5
  • 11
    • 0031569975 scopus 로고    scopus 로고
    • C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: complement deficiency and systemic lupus erythematosus revisited
    • Korb LC, Ahearn JM. C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: complement deficiency and systemic lupus erythematosus revisited. J Immunol. 1997;158:4525–4528.
    • (1997) J Immunol , vol.158 , pp. 4525-4528
    • Korb, L.C.1    Ahearn, J.M.2
  • 12
    • 0035284867 scopus 로고    scopus 로고
    • The globular heads of C1q specifically recognize surface blebs of apoptotic vascular endothelial cells
    • Navratil JS, Watkins SC, Wisnieski JJ, Ahearn JM. The globular heads of C1q specifically recognize surface blebs of apoptotic vascular endothelial cells. J Immunol. 2001;166:3231–3239.
    • (2001) J Immunol , vol.166 , pp. 3231-3239
    • Navratil, J.S.1    Watkins, S.C.2    Wisnieski, J.J.3    Ahearn, J.M.4
  • 13
    • 0036083789 scopus 로고    scopus 로고
    • Direct binding of C1q to apoptotic cells and cell blebs induces complement activation
    • Nauta AJ, Trouw LA, Daha MR, et al. Direct binding of C1q to apoptotic cells and cell blebs induces complement activation. Eur J Immunol. 2002;32:1726–1736.
    • (2002) Eur J Immunol , vol.32 , pp. 1726-1736
    • Nauta, A.J.1    Trouw, L.A.2    Daha, M.R.3
  • 14
    • 37349066319 scopus 로고    scopus 로고
    • Complement deficiencies and systemic lupus erythematosus
    • Truedsson L, Bengtsson AA, Sturfelt G. Complement deficiencies and systemic lupus erythematosus. Autoimmunity. 2007;40:560–566.
    • (2007) Autoimmunity , vol.40 , pp. 560-566
    • Truedsson, L.1    Bengtsson, A.A.2    Sturfelt, G.3
  • 16
    • 82555194114 scopus 로고    scopus 로고
    • Molecular basis of hereditary C1q deficiency–revisited: identification of several novel disease-causing mutations
    • Schejbel L, Skattum L, Hagelberg S, et al. Molecular basis of hereditary C1q deficiency–revisited: identification of several novel disease-causing mutations. Genes Immun. 2011;12:626–634.
    • (2011) Genes Immun , vol.12 , pp. 626-634
    • Schejbel, L.1    Skattum, L.2    Hagelberg, S.3
  • 17
    • 84936985336 scopus 로고    scopus 로고
    • Clinical presentation of human C1q deficiency: how much of a lupus?
    • Stegert M, Bock M, Trendelenburg M. Clinical presentation of human C1q deficiency: how much of a lupus? Mol Immunol. 2015;67:3–11.
    • (2015) Mol Immunol , vol.67 , pp. 3-11
    • Stegert, M.1    Bock, M.2    Trendelenburg, M.3
  • 18
    • 0036747260 scopus 로고    scopus 로고
    • C1q, autoimmunity and apoptosis
    • Botto M, Walport MJ. C1q, autoimmunity and apoptosis. Immunobiology. 2002;205:395–406.
    • (2002) Immunobiology , vol.205 , pp. 395-406
    • Botto, M.1    Walport, M.J.2
  • 19
    • 0021722951 scopus 로고
    • Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization
    • Ghebrehiwet B, Silvestri L, McDevitt C. Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization. J Exp Med. 1984;160:1375–1389.
    • (1984) J Exp Med , vol.160 , pp. 1375-1389
    • Ghebrehiwet, B.1    Silvestri, L.2    McDevitt, C.3
  • 20
    • 0031459567 scopus 로고    scopus 로고
    • The C1q and collectin binding site within C1q receptor (cell surface calreticulin)
    • Stuart GR, Lynch NJ, Day AJ, Schwaeble WJ, Sim RB. The C1q and collectin binding site within C1q receptor (cell surface calreticulin). Immunopharmacology. 1997;38:73–80.
    • (1997) Immunopharmacology , vol.38 , pp. 73-80
    • Stuart, G.R.1    Lynch, N.J.2    Day, A.J.3    Schwaeble, W.J.4    Sim, R.B.5
  • 21
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway
    • Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol. 2000;12:1539–1546.
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 22
    • 0027956447 scopus 로고
    • Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein
    • Eggleton P, Lieu TS, Zappi EG, et al. Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein. Clin Immunol Immunopathol. 1994;72:405–409.
    • (1994) Clin Immunol Immunopathol , vol.72 , pp. 405-409
    • Eggleton, P.1    Lieu, T.S.2    Zappi, E.G.3
  • 23
    • 0027829163 scopus 로고
    • The C1q-R participates in immunoregulation and signal transduction
    • Ghebrehiwet B, Peerschke EI. The C1q-R participates in immunoregulation and signal transduction. Behring Inst Mitt. 1993;93:236–240.
    • (1993) Behring Inst Mitt , vol.93 , pp. 236-240
    • Ghebrehiwet, B.1    Peerschke, E.I.2
  • 24
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex
    • Vandivier RW, Ogden CA, Fadok VA, et al. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J Immunol. 2002;169:3978–3986.
    • (2002) J Immunol , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1    Ogden, C.A.2    Fadok, V.A.3
  • 25
    • 33646477412 scopus 로고    scopus 로고
    • Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus
    • Donnelly S, Roake W, Brown S, et al. Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus. Arthritis Rheum. 2006;54:1543–1556.
    • (2006) Arthritis Rheum , vol.54 , pp. 1543-1556
    • Donnelly, S.1    Roake, W.2    Brown, S.3
  • 26
    • 0030611105 scopus 로고    scopus 로고
    • The systemic lupus erythematosus (SLE) disease autoantigen-calreticulin can inhibit C1q association with immune complexes
    • Kishore U, Sontheimer RD, Sastry KN, et al. The systemic lupus erythematosus (SLE) disease autoantigen-calreticulin can inhibit C1q association with immune complexes. Clin Exp Immunol. 1997;108:181–190.
    • (1997) Clin Exp Immunol , vol.108 , pp. 181-190
    • Kishore, U.1    Sontheimer, R.D.2    Sastry, K.N.3
  • 29
    • 70349238894 scopus 로고    scopus 로고
    • Autoantibodies against complement C1q specifically target C1q bound on early apoptotic cells
    • Bigler C, Schaller M, Perahud I, Osthoff M, Trendelenburg M. Autoantibodies against complement C1q specifically target C1q bound on early apoptotic cells. J Immunol. 2009;183:3512–3521.
    • (2009) J Immunol , vol.183 , pp. 3512-3521
    • Bigler, C.1    Schaller, M.2    Perahud, I.3    Osthoff, M.4    Trendelenburg, M.5
  • 30
    • 84912564905 scopus 로고    scopus 로고
    • Anti-C1q autoantibodies from active lupus nephritis patients could inhibit the clearance of apoptotic cells and complement classical pathway activation mediated by C1q in vitro
    • Pang Y, Yang XW, Song Y, Yu F, Zhao MH. Anti-C1q autoantibodies from active lupus nephritis patients could inhibit the clearance of apoptotic cells and complement classical pathway activation mediated by C1q in vitro. Immunobiology. 2014;219:980–989.
    • (2014) Immunobiology , vol.219 , pp. 980-989
    • Pang, Y.1    Yang, X.W.2    Song, Y.3    Yu, F.4    Zhao, M.H.5
  • 31
    • 0032588177 scopus 로고    scopus 로고
    • C1q inhibits autoantibody binding to calreticulin
    • Racila DM, Sontheimer RD. C1q inhibits autoantibody binding to calreticulin. Lupus. 1999;8:300–304.
    • (1999) Lupus , vol.8 , pp. 300-304
    • Racila, D.M.1    Sontheimer, R.D.2
  • 32
    • 2442650484 scopus 로고    scopus 로고
    • cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection
    • Ghebrehiwet B, Peerschke EI. cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection. Mol Immunol. 2004;41:173–183.
    • (2004) Mol Immunol , vol.41 , pp. 173-183
    • Ghebrehiwet, B.1    Peerschke, E.I.2
  • 33
    • 0028290256 scopus 로고
    • Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular “heads” of C1q
    • Ghebrehiwet B, Lim BL, Peerschke EI, Willis AC, Reid KB. Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular “heads” of C1q. J Exp Med. 1994;179:1809–1821.
    • (1994) J Exp Med , vol.179 , pp. 1809-1821
    • Ghebrehiwet, B.1    Lim, B.L.2    Peerschke, E.I.3    Willis, A.C.4    Reid, K.B.5
  • 34
    • 0030944415 scopus 로고    scopus 로고
    • cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro
    • Nepomuceno RR, Henschen-Edman AH, Burgess WH, Tenner AJ. cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity. 1997;6:119–129.
    • (1997) Immunity , vol.6 , pp. 119-129
    • Nepomuceno, R.R.1    Henschen-Edman, A.H.2    Burgess, W.H.3    Tenner, A.J.4
  • 35
    • 1542619333 scopus 로고    scopus 로고
    • Murine CD93 (C1qRp) contributes to the removal of apoptotic cells in vivo but is not required for C1q-mediated enhancement of phagocytosis
    • Norsworthy PJ, Fossati-Jimack L, Cortes-Hernandez J, et al. Murine CD93 (C1qRp) contributes to the removal of apoptotic cells in vivo but is not required for C1q-mediated enhancement of phagocytosis. J Immunol. 2004;172:3406–3414.
    • (2004) J Immunol , vol.172 , pp. 3406-3414
    • Norsworthy, P.J.1    Fossati-Jimack, L.2    Cortes-Hernandez, J.3
  • 36
    • 0037093864 scopus 로고    scopus 로고
    • Human C1qRp is identical with CD93 and the mNI-11 antigen but does not bind C1q
    • McGreal EP, Ikewaki N, Akatsu H, Morgan BP, Gasque P. Human C1qRp is identical with CD93 and the mNI-11 antigen but does not bind C1q. J Immunol. 2002;168:5222–5232.
    • (2002) J Immunol , vol.168 , pp. 5222-5232
    • McGreal, E.P.1    Ikewaki, N.2    Akatsu, H.3    Morgan, B.P.4    Gasque, P.5
  • 37
    • 0036142838 scopus 로고    scopus 로고
    • Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning
    • Steinberger P, Szekeres A, Wille S, et al. Identification of human CD93 as the phagocytic C1q receptor (C1qRp) by expression cloning. J Leukoc Biol. 2002;71:133–140.
    • (2002) J Leukoc Biol , vol.71 , pp. 133-140
    • Steinberger, P.1    Szekeres, A.2    Wille, S.3
  • 38
    • 49649121425 scopus 로고    scopus 로고
    • The lectin-like activity of human C1q and its implication in DNA and apoptotic cell recognition
    • Paidassi H, Tacnet-Delorme P, Lunardi T, Arlaud GJ, Thielens NM, Frachet P. The lectin-like activity of human C1q and its implication in DNA and apoptotic cell recognition. FEBS Lett. 2008;582:3111–3116.
    • (2008) FEBS Lett , vol.582 , pp. 3111-3116
    • Paidassi, H.1    Tacnet-Delorme, P.2    Lunardi, T.3    Arlaud, G.J.4    Thielens, N.M.5    Frachet, P.6
  • 39
    • 0028288510 scopus 로고
    • Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes
    • Casciola-Rosen LA, Anhalt G, Rosen A. Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J Exp Med. 1994;179:1317–1330.
    • (1994) J Exp Med , vol.179 , pp. 1317-1330
    • Casciola-Rosen, L.A.1    Anhalt, G.2    Rosen, A.3
  • 40
    • 2442707797 scopus 로고    scopus 로고
    • Nucleosomes are exposed at the cell surface in apoptosis
    • Radic M, Marion T, Monestier M. Nucleosomes are exposed at the cell surface in apoptosis. J Immunol. 2004;172:6692–6700.
    • (2004) J Immunol , vol.172 , pp. 6692-6700
    • Radic, M.1    Marion, T.2    Monestier, M.3
  • 41
    • 27744503953 scopus 로고    scopus 로고
    • CD46 plays a key role in tailoring innate immune recognition of apoptotic and necrotic cells
    • Elward K, et al. CD46 plays a key role in tailoring innate immune recognition of apoptotic and necrotic cells. J Biol Chem. 2005;280:36342–36354.
    • (2005) J Biol Chem , vol.280 , pp. 36342-36354
    • Elward, K.1
  • 42
    • 84866914816 scopus 로고    scopus 로고
    • Annexin A2 and A5 serve as new ligands for C1q on apoptotic cells
    • Martin M, Leffler J, Blom AM. Annexin A2 and A5 serve as new ligands for C1q on apoptotic cells. J Biol Chem. 2012;287:33733–33744.
    • (2012) J Biol Chem , vol.287 , pp. 33733-33744
    • Martin, M.1    Leffler, J.2    Blom, A.M.3
  • 43
    • 42149156053 scopus 로고    scopus 로고
    • C1q binds phosphatidylserine and likely acts as a multiligand-bridging molecule in apoptotic cell recognition
    • Paidassi H, Tacnet-Delorme P, Garlatti V, et al. C1q binds phosphatidylserine and likely acts as a multiligand-bridging molecule in apoptotic cell recognition. J Immunol. 2008;180:2329–2338.
    • (2008) J Immunol , vol.180 , pp. 2329-2338
    • Paidassi, H.1    Tacnet-Delorme, P.2    Garlatti, V.3
  • 44
    • 79952663868 scopus 로고    scopus 로고
    • Investigations on the C1q-calreticulin-phosphatidylserine interactions yield new insights into apoptotic cell recognition
    • Paidassi H, Tacnet-Delorme P, Vemeret M, et al. Investigations on the C1q-calreticulin-phosphatidylserine interactions yield new insights into apoptotic cell recognition. J Mol Biol. 2011;408:277–290.
    • (2011) J Mol Biol , vol.408 , pp. 277-290
    • Paidassi, H.1    Tacnet-Delorme, P.2    Vemeret, M.3
  • 45
    • 0033794387 scopus 로고    scopus 로고
    • Nucleosomes are major T and B cell autoantigens in systemic lupus erythematosus
    • Bruns A, Blass S, Hausdorf G, Burmester GR, Hiepe F. Nucleosomes are major T and B cell autoantigens in systemic lupus erythematosus. Arthritis Rheum. 2000;43:2307–2315.
    • (2000) Arthritis Rheum , vol.43 , pp. 2307-2315
    • Bruns, A.1    Blass, S.2    Hausdorf, G.3    Burmester, G.R.4    Hiepe, F.5
  • 46
    • 84953327772 scopus 로고    scopus 로고
    • Extracellular histones induce chemokine production in whole blood ex vivo and leukocyte recruitment in vivo
    • Westman J, Papareddy P, Dahlgren MW, et al. Extracellular histones induce chemokine production in whole blood ex vivo and leukocyte recruitment in vivo. PLoS Pathog. 2015;11:e1005319.
    • (2015) PLoS Pathog , vol.11
    • Westman, J.1    Papareddy, P.2    Dahlgren, M.W.3
  • 47
    • 0035172146 scopus 로고    scopus 로고
    • Detection of nucleosome particles in serum and plasma from patients with systemic lupus erythematosus using monoclonal antibody 4H7
    • Williams RC Jr, Malone CC, Meyers C, Decker P, Muller S. Detection of nucleosome particles in serum and plasma from patients with systemic lupus erythematosus using monoclonal antibody 4H7. J Rheumatol. 2001;28:81–94.
    • (2001) J Rheumatol , vol.28 , pp. 81-94
    • Williams, R.C.1    Malone, C.C.2    Meyers, C.3    Decker, P.4    Muller, S.5
  • 48
    • 0037023680 scopus 로고    scopus 로고
    • Apoptotic release of histones from nucleosomes
    • Wu D, Ingram A, Lahti JH, et al. Apoptotic release of histones from nucleosomes. J Biol Chem. 2002;277:12001–12008.
    • (2002) J Biol Chem , vol.277 , pp. 12001-12008
    • Wu, D.1    Ingram, A.2    Lahti, J.H.3
  • 49
    • 70449107044 scopus 로고    scopus 로고
    • Extracellular histones are major mediators of death in sepsis
    • Xu J, Zhang Z, Pelayo R, et al. Extracellular histones are major mediators of death in sepsis. Nat Med. 2009;15:1318–1321.
    • (2009) Nat Med , vol.15 , pp. 1318-1321
    • Xu, J.1    Zhang, Z.2    Pelayo, R.3
  • 50
    • 84864831388 scopus 로고    scopus 로고
    • Dying cells and extracellular histones in AKI: beyond a NET effect?
    • Rosin DL, Okusa MD. Dying cells and extracellular histones in AKI: beyond a NET effect? J Am Soc Nephrol. 2012;23:1275–1277.
    • (2012) J Am Soc Nephrol , vol.23 , pp. 1275-1277
    • Rosin, D.L.1    Okusa, M.D.2
  • 51
    • 84859375702 scopus 로고    scopus 로고
    • Neutrophil extracellular traps that are not degraded in systemic lupus erythematosus activate complement exacerbating the disease
    • Leffler J, Gullstrand B, Jönsen A, et al. Neutrophil extracellular traps that are not degraded in systemic lupus erythematosus activate complement exacerbating the disease. J Immunol. 2012;188:3522–3531.
    • (2012) J Immunol , vol.188 , pp. 3522-3531
    • Leffler, J.1    Gullstrand, B.2    Jönsen, A.3
  • 52
    • 84902803780 scopus 로고    scopus 로고
    • Relative contribution of c1q and apoptotic cell-surface calreticulin to macrophage phagocytosis
    • Verneret M, Tacnet-Delorme P, Osman R, et al. Relative contribution of c1q and apoptotic cell-surface calreticulin to macrophage phagocytosis. J Innate Immun. 2014;6:426–434.
    • (2014) J Innate Immun , vol.6 , pp. 426-434
    • Verneret, M.1    Tacnet-Delorme, P.2    Osman, R.3
  • 53
    • 34147187173 scopus 로고    scopus 로고
    • Generation of inhibitory NFkappaB complexes and phosphorylated cAMP response element-binding protein correlates with the anti-inflammatory activity of complement protein C1q in human monocytes
    • Fraser DA, Arora M, Bohlson SS, Lozano E, Tenner AJ. Generation of inhibitory NFkappaB complexes and phosphorylated cAMP response element-binding protein correlates with the anti-inflammatory activity of complement protein C1q in human monocytes. J Biol Chem. 2007;282:7360–7367.
    • (2007) J Biol Chem , vol.282 , pp. 7360-7367
    • Fraser, D.A.1    Arora, M.2    Bohlson, S.S.3    Lozano, E.4    Tenner, A.J.5
  • 54
    • 73949145491 scopus 로고    scopus 로고
    • C1q differentially modulates phagocytosis and cytokine responses during ingestion of apoptotic cells by human monocytes, macrophages, and dendritic cells
    • Fraser DA, Laust AK, Nelson EL, Tenner AJ. C1q differentially modulates phagocytosis and cytokine responses during ingestion of apoptotic cells by human monocytes, macrophages, and dendritic cells. J Immunol. 2009;183:6175–6185.
    • (2009) J Immunol , vol.183 , pp. 6175-6185
    • Fraser, D.A.1    Laust, A.K.2    Nelson, E.L.3    Tenner, A.J.4
  • 55
    • 73949103664 scopus 로고    scopus 로고
    • C1q enhances microglial clearance of apoptotic neurons and neuronal blebs, and modulates subsequent inflammatory cytokine production
    • Fraser DA, Pisalyaput K, Tenner AJ. C1q enhances microglial clearance of apoptotic neurons and neuronal blebs, and modulates subsequent inflammatory cytokine production. J Neurochem. 2010;112:733–743.
    • (2010) J Neurochem , vol.112 , pp. 733-743
    • Fraser, D.A.1    Pisalyaput, K.2    Tenner, A.J.3
  • 56
    • 84925287332 scopus 로고    scopus 로고
    • Complement protein C1q bound to apoptotic cells suppresses human macrophage and dendritic cell-mediated Th17 and Th1 T cell subset proliferation
    • Clarke EV, Weist BM, Walsh CM, Tenner AJ. Complement protein C1q bound to apoptotic cells suppresses human macrophage and dendritic cell-mediated Th17 and Th1 T cell subset proliferation. J Leukoc Biol. 2015;97:147–160.
    • (2015) J Leukoc Biol , vol.97 , pp. 147-160
    • Clarke, E.V.1    Weist, B.M.2    Walsh, C.M.3    Tenner, A.J.4
  • 57
    • 84954305629 scopus 로고    scopus 로고
    • Uncoupling complement C1s activation from C1q binding in apoptotic cell phagocytosis and immunosuppressive capacity
    • Colonna L, Parry GC, Panicker S, Elkon KB. Uncoupling complement C1s activation from C1q binding in apoptotic cell phagocytosis and immunosuppressive capacity. Clin Immunol. 2016;163:84–90.
    • (2016) Clin Immunol , vol.163 , pp. 84-90
    • Colonna, L.1    Parry, G.C.2    Panicker, S.3    Elkon, K.B.4
  • 58
    • 84862084817 scopus 로고    scopus 로고
    • Complement protein C1q directs macrophage polarization and limits inflammasome activity during the uptake of apoptotic cells
    • Benoit ME, Clarke EV, Morgado P, Fraser DA, Tenner AJ. Complement protein C1q directs macrophage polarization and limits inflammasome activity during the uptake of apoptotic cells. J Immunol. 2012;188:5682–5693.
    • (2012) J Immunol , vol.188 , pp. 5682-5693
    • Benoit, M.E.1    Clarke, E.V.2    Morgado, P.3    Fraser, D.A.4    Tenner, A.J.5
  • 59
    • 4344643316 scopus 로고    scopus 로고
    • Opsonization with C1q and mannose-binding lectin targets apoptotic cells to dendritic cells
    • Nauta AJ, Castellano G, Xu W, et al. Opsonization with C1q and mannose-binding lectin targets apoptotic cells to dendritic cells. J Immunol. 2004;173:3044–3050.
    • (2004) J Immunol , vol.173 , pp. 3044-3050
    • Nauta, A.J.1    Castellano, G.2    Xu, W.3
  • 60
    • 77952415076 scopus 로고    scopus 로고
    • Evidence that a C1q/C1qR system regulates monocyte-derived dendritic cell differentiation at the interface of innate and acquired immunity
    • Hosszu KK, Santiago-Schwarz F, Peerschke EI, Ghebrehiwet B. Evidence that a C1q/C1qR system regulates monocyte-derived dendritic cell differentiation at the interface of innate and acquired immunity. Innate Immun. 2010;16:115–127.
    • (2010) Innate Immun , vol.16 , pp. 115-127
    • Hosszu, K.K.1    Santiago-Schwarz, F.2    Peerschke, E.I.3    Ghebrehiwet, B.4
  • 61
    • 70349769369 scopus 로고    scopus 로고
    • C1q inhibits immune complex-induced interferon-alpha production in plasmacytoid dendritic cells: a novel link between C1q deficiency and systemic lupus erythematosus pathogenesis
    • Lood C, Gullstrand B, Truedsson L, et al. C1q inhibits immune complex-induced interferon-alpha production in plasmacytoid dendritic cells: a novel link between C1q deficiency and systemic lupus erythematosus pathogenesis. Arthritis Rheum. 2009;60:3081–3090.
    • (2009) Arthritis Rheum , vol.60 , pp. 3081-3090
    • Lood, C.1    Gullstrand, B.2    Truedsson, L.3
  • 63
    • 84858078015 scopus 로고    scopus 로고
    • Mannan-binding lectin deficiency – good news, bad news, doesn't matter?
    • Heitzeneder S, Seidel M, Forster-Waldl E, Heitger A. Mannan-binding lectin deficiency – good news, bad news, doesn't matter? Clin Immunol. 2012;143:22–38.
    • (2012) Clin Immunol , vol.143 , pp. 22-38
    • Heitzeneder, S.1    Seidel, M.2    Forster-Waldl, E.3    Heitger, A.4
  • 64
    • 77953402526 scopus 로고    scopus 로고
    • Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma
    • Wittenborn T, Thiel S, Jensen L, Nielsen HJ, Jensenius JC. Characteristics and biological variations of M-ficolin, a pattern recognition molecule, in plasma. J Innate Immun. 2010;2:167–180.
    • (2010) J Innate Immun , vol.2 , pp. 167-180
    • Wittenborn, T.1    Thiel, S.2    Jensen, L.3    Nielsen, H.J.4    Jensenius, J.C.5
  • 65
    • 0033119812 scopus 로고    scopus 로고
    • P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients
    • Kilpatrick DC, Fujita T, Matsushita M. P35, an opsonic lectin of the ficolin family, in human blood from neonates, normal adults, and recurrent miscarriage patients. Immunol Lett. 1999;67:109–112.
    • (1999) Immunol Lett , vol.67 , pp. 109-112
    • Kilpatrick, D.C.1    Fujita, T.2    Matsushita, M.3
  • 66
    • 33947593528 scopus 로고    scopus 로고
    • The impact of FCN2 polymorphisms and haplotypes on the Ficolin-2 serum levels
    • Munthe-Fog L, Hummelshoj T, Hansen BE, et al. The impact of FCN2 polymorphisms and haplotypes on the Ficolin-2 serum levels. Scand J Immunol. 2007;65:383–392.
    • (2007) Scand J Immunol , vol.65 , pp. 383-392
    • Munthe-Fog, L.1    Hummelshoj, T.2    Hansen, B.E.3
  • 68
    • 38149115537 scopus 로고    scopus 로고
    • The chaperone and potential mannan-binding lectin (MBL) co-receptor calreticulin interacts with MBL through the binding site for MBL-associated serine proteases
    • Pagh R, et al. The chaperone and potential mannan-binding lectin (MBL) co-receptor calreticulin interacts with MBL through the binding site for MBL-associated serine proteases. FEBS J. 2008;275:515–526.
    • (2008) FEBS J , vol.275 , pp. 515-526
    • Pagh, R.1
  • 69
    • 0242335087 scopus 로고    scopus 로고
    • Mannose-binding lectin engagement with late apoptotic and necrotic cells
    • Nauta AJ, Raaschou-Jensen N, Roos A, et al. Mannose-binding lectin engagement with late apoptotic and necrotic cells. Eur J Immunol. 2003;33:2853–2863.
    • (2003) Eur J Immunol , vol.33 , pp. 2853-2863
    • Nauta, A.J.1    Raaschou-Jensen, N.2    Roos, A.3
  • 70
    • 14844363449 scopus 로고    scopus 로고
    • Mannose-binding lectin-deficient mice display defective apoptotic cell clearance but no autoimmune phenotype
    • Stuart LM, Takahashi K, Shi L, Savill J, Ezekowitz RA. Mannose-binding lectin-deficient mice display defective apoptotic cell clearance but no autoimmune phenotype. J Immunol. 2005;174:3220–3226.
    • (2005) J Immunol , vol.174 , pp. 3220-3226
    • Stuart, L.M.1    Takahashi, K.2    Shi, L.3    Savill, J.4    Ezekowitz, R.A.5
  • 71
    • 84911935349 scopus 로고    scopus 로고
    • Mannose-binding lectin is required for the effective clearance of apoptotic cells by adipose tissue macrophages during obesity
    • Stienstra R, Dijk W, van Beek L, et al. Mannose-binding lectin is required for the effective clearance of apoptotic cells by adipose tissue macrophages during obesity. Diabetes. 2014;63:4143–4153.
    • (2014) Diabetes , vol.63 , pp. 4143-4153
    • Stienstra, R.1    Dijk, W.2    van Beek, L.3
  • 72
    • 14244266540 scopus 로고    scopus 로고
    • Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation
    • Kuraya M, Ming Z, Liu X, Matsushita M, Fujita T. Specific binding of L-ficolin and H-ficolin to apoptotic cells leads to complement activation. Immunobiology. 2005;209:689–697.
    • (2005) Immunobiology , vol.209 , pp. 689-697
    • Kuraya, M.1    Ming, Z.2    Liu, X.3    Matsushita, M.4    Fujita, T.5
  • 73
    • 0025490665 scopus 로고
    • Serological studies of an SLE-associated antigen-antibody system discovered as a precipitation reaction in agarose gel: the HAKATA antigen-antibody system
    • Inaba S, Okochi K, Yae Y, Niklasson F, de Verder CH. Serological studies of an SLE-associated antigen-antibody system discovered as a precipitation reaction in agarose gel: the HAKATA antigen-antibody system. Fukuoka Igaku Zasshi. 1990;81:284–291.
    • (1990) Fukuoka Igaku Zasshi , vol.81 , pp. 284-291
    • Inaba, S.1    Okochi, K.2    Yae, Y.3    Niklasson, F.4    de Verder, C.H.5
  • 74
    • 34248592214 scopus 로고    scopus 로고
    • The innate immune component ficolin 3 (Hakata antigen) mediates the clearance of late apoptotic cells
    • Honore C, Hummelshoj T, Hansen BE, Madsen HO, Eggleton P, Garred P. The innate immune component ficolin 3 (Hakata antigen) mediates the clearance of late apoptotic cells. Arthritis Rheum. 2007;56:1598–1607.
    • (2007) Arthritis Rheum , vol.56 , pp. 1598-1607
    • Honore, C.1    Hummelshoj, T.2    Hansen, B.E.3    Madsen, H.O.4    Eggleton, P.5    Garred, P.6
  • 76
    • 50549100499 scopus 로고    scopus 로고
    • Pattern recognition receptors in the immune response against dying cells
    • Jeannin P, Jaillon S, Delneste Y. Pattern recognition receptors in the immune response against dying cells. Curr Opin Immunol. 2008;20:530–537.
    • (2008) Curr Opin Immunol , vol.20 , pp. 530-537
    • Jeannin, P.1    Jaillon, S.2    Delneste, Y.3
  • 77
    • 59849111369 scopus 로고    scopus 로고
    • Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin
    • Lacroix M, Dumestre-Perard C, Schoehn G, et al. Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin. J Immunol. 2009;182:456–465.
    • (2009) J Immunol , vol.182 , pp. 456-465
    • Lacroix, M.1    Dumestre-Perard, C.2    Schoehn, G.3
  • 78
    • 77957866595 scopus 로고    scopus 로고
    • Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages
    • Gorovoy M, Gaultier A, Campana WM, Firestein GS, Gonias SL. Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages. J Leukoc Biol. 2010;88:769–778.
    • (2010) J Leukoc Biol , vol.88 , pp. 769-778
    • Gorovoy, M.1    Gaultier, A.2    Campana, W.M.3    Firestein, G.S.4    Gonias, S.L.5
  • 79
    • 84880652830 scopus 로고    scopus 로고
    • Ficolin-1-PTX3 complex formation promotes clearance of altered self-cells and modulates IL-8 production
    • Ma YJ, Doni A, Romani L, et al. Ficolin-1-PTX3 complex formation promotes clearance of altered self-cells and modulates IL-8 production. J Immunol. 2013;191:1324–1333.
    • (2013) J Immunol , vol.191 , pp. 1324-1333
    • Ma, Y.J.1    Doni, A.2    Romani, L.3
  • 80
    • 0000719411 scopus 로고
    • The properdin system and immunity. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena
    • Pillemer L, Blum L, Lepow IH, Ross OA, Todd EW, Wardlaw AC. The properdin system and immunity. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena. Science. 1954;120:279–285.
    • (1954) Science , vol.120 , pp. 279-285
    • Pillemer, L.1    Blum, L.2    Lepow, I.H.3    Ross, O.A.4    Todd, E.W.5    Wardlaw, A.C.6
  • 81
    • 48249124246 scopus 로고    scopus 로고
    • The complement protein properdin binds apoptotic T cells and promotes complement activation and phagocytosis
    • Kemper C, Mitchell LM, Zhang L, Hourcade DE. The complement protein properdin binds apoptotic T cells and promotes complement activation and phagocytosis. Proc Natl Acad Sci USA. 2008;105:9023–9028.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9023-9028
    • Kemper, C.1    Mitchell, L.M.2    Zhang, L.3    Hourcade, D.E.4
  • 82
    • 77952300688 scopus 로고    scopus 로고
    • Properdin: emerging roles of a pattern-recognition molecule
    • Kemper C, Atkinson JP, Hourcade DE. Properdin: emerging roles of a pattern-recognition molecule. Annu Rev Immunol. 2010;28:131–155.
    • (2010) Annu Rev Immunol , vol.28 , pp. 131-155
    • Kemper, C.1    Atkinson, J.P.2    Hourcade, D.E.3
  • 83
    • 47249130305 scopus 로고    scopus 로고
    • Properdin binds to late apoptotic and necrotic cells independently of C3b and regulates alternative pathway complement activation
    • Xu W, Berger SP, Trouw LA, et al. Properdin binds to late apoptotic and necrotic cells independently of C3b and regulates alternative pathway complement activation. J Immunol. 2008;180:7613–7621.
    • (2008) J Immunol , vol.180 , pp. 7613-7621
    • Xu, W.1    Berger, S.P.2    Trouw, L.A.3
  • 84
    • 77954312934 scopus 로고    scopus 로고
    • Native polymeric forms of properdin selectively bind to targets and promote activation of the alternative pathway of complement
    • Ferreira VP, Cortes C, Pangburn MK. Native polymeric forms of properdin selectively bind to targets and promote activation of the alternative pathway of complement. Immunobiology. 2010;215:932–940.
    • (2010) Immunobiology , vol.215 , pp. 932-940
    • Ferreira, V.P.1    Cortes, C.2    Pangburn, M.K.3
  • 85
    • 1842557722 scopus 로고    scopus 로고
    • Complement inhibitor C4b-binding protein-friend or foe in the innate immune system?
    • Blom AM, Villoutreix BO, Dahlback B. Complement inhibitor C4b-binding protein-friend or foe in the innate immune system? Mol Immunol. 2004;40:1333–1346.
    • (2004) Mol Immunol , vol.40 , pp. 1333-1346
    • Blom, A.M.1    Villoutreix, B.O.2    Dahlback, B.3
  • 86
    • 0029091398 scopus 로고
    • Isoforms of human C4b-binding protein. I. Molecular basis for the C4BP isoform pattern and its variations in human plasma
    • Sanchez-Corral P, Criado Garcia O, Rodriguez de Cordoba S. Isoforms of human C4b-binding protein. I. Molecular basis for the C4BP isoform pattern and its variations in human plasma. J Immunol. 1995;155:4030–4036.
    • (1995) J Immunol , vol.155 , pp. 4030-4036
    • Sanchez-Corral, P.1    Criado Garcia, O.2    Rodriguez de Cordoba, S.3
  • 87
    • 0037199490 scopus 로고    scopus 로고
    • Structural requirements for the intracellular subunit polymerization of the complement inhibitor C4b-binding protein
    • Kask L, Hillarp A, Ramesh B, Dahlback B, Blom AM. Structural requirements for the intracellular subunit polymerization of the complement inhibitor C4b-binding protein. Biochemistry. 2002;41:9349–9357.
    • (2002) Biochemistry , vol.41 , pp. 9349-9357
    • Kask, L.1    Hillarp, A.2    Ramesh, B.3    Dahlback, B.4    Blom, A.M.5
  • 88
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom AM, Kask L, Dahlback B. Structural requirements for the complement regulatory activities of C4BP. J Biol Chem. 2001;276:27136–27144.
    • (2001) J Biol Chem , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlback, B.3
  • 89
    • 0033516648 scopus 로고    scopus 로고
    • A cluster of positively charged amino acids in the N-terminal modules of the C4BP a-chain is crucial for C4b binding and factor I cofactor function
    • Blom AM, Webb J, Villoutreix BO, Dahlbäck B. A cluster of positively charged amino acids in the N-terminal modules of the C4BP a-chain is crucial for C4b binding and factor I cofactor function. J Biol Chem. 1999;274:19237–19245.
    • (1999) J Biol Chem , vol.274 , pp. 19237-19245
    • Blom, A.M.1    Webb, J.2    Villoutreix, B.O.3    Dahlbäck, B.4
  • 90
    • 0037210218 scopus 로고    scopus 로고
    • CCP1-4 of the C4b-binding protein alpha-chain are required for factor I mediated cleavage of complement factor C3b
    • Blom AM, Kask L, Dahlback B. CCP1-4 of the C4b-binding protein alpha-chain are required for factor I mediated cleavage of complement factor C3b. Mol Immunol. 2003;39:547–556.
    • (2003) Mol Immunol , vol.39 , pp. 547-556
    • Blom, A.M.1    Kask, L.2    Dahlback, B.3
  • 91
    • 0011369135 scopus 로고
    • Modulation of the classical pathway C3 convertase by plasma protein C4b binding and C3b inactivator
    • Gigli I, Fujita T, Nussenzweig V. Modulation of the classical pathway C3 convertase by plasma protein C4b binding and C3b inactivator. Proc Natl Acad Sci USA. 1979;76:6596–6600.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6596-6600
    • Gigli, I.1    Fujita, T.2    Nussenzweig, V.3
  • 92
    • 0018185413 scopus 로고
    • Human C4b-binding protein, isolation and characterization
    • Scharfstein J, Ferreira A, Gigli I, Nussenzweig V. Human C4b-binding protein, isolation and characterization. J Exp Med. 1978;148:207–222.
    • (1978) J Exp Med , vol.148 , pp. 207-222
    • Scharfstein, J.1    Ferreira, A.2    Gigli, I.3    Nussenzweig, V.4
  • 93
    • 0040528742 scopus 로고
    • Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C4b
    • Dahlback B, Smith CA, Muller-Eberhard HJ. Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C4b. Proc Natl Acad Sci USA. 1983;80:3461–3465.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3461-3465
    • Dahlback, B.1    Smith, C.A.2    Muller-Eberhard, H.J.3
  • 94
    • 0035830943 scopus 로고    scopus 로고
    • Localization of a hydrophobic binding site for anticoagulant protein S on the beta -chain of complement regulator C4b-binding protein
    • Webb JH, Villoutreix BO, Dahlback B, Blom AM. Localization of a hydrophobic binding site for anticoagulant protein S on the beta -chain of complement regulator C4b-binding protein. J Biol Chem. 2001;276:4330–4337.
    • (2001) J Biol Chem , vol.276 , pp. 4330-4337
    • Webb, J.H.1    Villoutreix, B.O.2    Dahlback, B.3    Blom, A.M.4
  • 95
    • 0028103281 scopus 로고
    • Differential regulation of alpha and beta chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S
    • Garcia de Frutos P, Alim RI, Hardig Y, Zoller B, Dahlback B. Differential regulation of alpha and beta chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S. Blood. 1994;84:815–822.
    • (1994) Blood , vol.84 , pp. 815-822
    • Garcia de Frutos, P.1    Alim, R.I.2    Hardig, Y.3    Zoller, B.4    Dahlback, B.5
  • 96
    • 0029126988 scopus 로고
    • Isoforms of human C4b-binding protein. II. Differential modulation of the C4BPA and C4BPB genes by acute phase cytokines
    • Criado Garcia O, Sanchez-Corral P, Rodriguez de Cordoba S. Isoforms of human C4b-binding protein. II. Differential modulation of the C4BPA and C4BPB genes by acute phase cytokines. J Immunol. 1995;155:4037–4043.
    • (1995) J Immunol , vol.155 , pp. 4037-4043
    • Criado Garcia, O.1    Sanchez-Corral, P.2    Rodriguez de Cordoba, S.3
  • 97
    • 77957808702 scopus 로고    scopus 로고
    • Dependence on vitamin K-dependent protein S for eukaryotic cell secretion of the beta-chain of C4b-binding protein
    • Carlsson S, Dahlback B. Dependence on vitamin K-dependent protein S for eukaryotic cell secretion of the beta-chain of C4b-binding protein. J Biol Chem. 2010;285:32038–32046.
    • (2010) J Biol Chem , vol.285 , pp. 32038-32046
    • Carlsson, S.1    Dahlback, B.2
  • 98
    • 34548288545 scopus 로고    scopus 로고
    • Non-small cell lung cancer cells produce a functional set of complement factor I and its soluble cofactors
    • Okroj M, Hsu YF, Ajona D, Pio R, Blom AM. Non-small cell lung cancer cells produce a functional set of complement factor I and its soluble cofactors. Mol Immunol. 2008;45:169–179.
    • (2008) Mol Immunol , vol.45 , pp. 169-179
    • Okroj, M.1    Hsu, Y.F.2    Ajona, D.3    Pio, R.4    Blom, A.M.5
  • 99
    • 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 LA, Bengtsson AA, Gelderman KA, Dahlback B, Sturfelt G, Blom AM. 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    Dahlback, B.4    Sturfelt, G.5    Blom, A.M.6
  • 100
    • 22344454254 scopus 로고    scopus 로고
    • C4b-binding protein binds to necrotic cells and DNA, limiting DNA release and inhibiting complement activation
    • Trouw LA, Nilsson SC, Goncalves I, Landberg G, Blom AM. C4b-binding protein binds to necrotic cells and DNA, limiting DNA release and inhibiting complement activation. J Exp Med. 2005;201:1937–1948.
    • (2005) J Exp Med , vol.201 , pp. 1937-1948
    • Trouw, L.A.1    Nilsson, S.C.2    Goncalves, I.3    Landberg, G.4    Blom, A.M.5
  • 101
    • 0036721697 scopus 로고    scopus 로고
    • Vitamin K-dependent protein S localizing complement regulator C4b-binding protein to the surface of apoptotic cells
    • Webb JH, Blom AM, Dahlback B. Vitamin K-dependent protein S localizing complement regulator C4b-binding protein to the surface of apoptotic cells. J Immunol. 2002;169:2580–2586.
    • (2002) J Immunol , vol.169 , pp. 2580-2586
    • Webb, J.H.1    Blom, A.M.2    Dahlback, B.3
  • 102
    • 20244362188 scopus 로고    scopus 로고
    • Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells
    • Anderson HA, Maylock CA, Williams JA, Paweletz CP, Shu H, Shacter E. Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells. Nat Immunol. 2003;4:87–91.
    • (2003) Nat Immunol , vol.4 , pp. 87-91
    • Anderson, H.A.1    Maylock, C.A.2    Williams, J.A.3    Paweletz, C.P.4    Shu, H.5    Shacter, E.6
  • 103
    • 2642533647 scopus 로고    scopus 로고
    • The C4b-binding protein-protein S complex inhibits the phagocytosis of apoptotic cells
    • Kask L, Trouw LA, Dahlback B, Blom AM. The C4b-binding protein-protein S complex inhibits the phagocytosis of apoptotic cells. J Biol Chem. 2004;279:23869–23873.
    • (2004) J Biol Chem , vol.279 , pp. 23869-23873
    • Kask, L.1    Trouw, L.A.2    Dahlback, B.3    Blom, A.M.4
  • 104
    • 44649151935 scopus 로고    scopus 로고
    • Measurement of factor H variants in plasma using variant-specific monoclonal antibodies: application to assessing risk of age-related macular degeneration
    • Hakobyan S, Harris CL, Tortajada A, et al. Measurement of factor H variants in plasma using variant-specific monoclonal antibodies: application to assessing risk of age-related macular degeneration. Invest Ophthalmol Vis Sci. 2008;49:1983–1990.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 1983-1990
    • Hakobyan, S.1    Harris, C.L.2    Tortajada, A.3
  • 105
    • 0023875503 scopus 로고
    • The complete amino acid sequence of human complement factor H
    • Ripoche J, Day AJ, Harris TJ, Sim RB. 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
  • 107
    • 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 MK. 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
  • 108
    • 33750336175 scopus 로고    scopus 로고
    • Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces
    • Ferreira VP, Herbert AP, Hocking HG, Barlow PN, Pangburn MK. 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
  • 109
    • 84861727429 scopus 로고    scopus 로고
    • Factor h: a complement regulator in health and disease, and a mediator of cellular interactions
    • Kopp A, Hebecker M, Svobodova E, Jozsi M. Factor h: a complement regulator in health and disease, and a mediator of cellular interactions. Biomolecules. 2012;2:46–75.
    • (2012) Biomolecules , vol.2 , pp. 46-75
    • Kopp, A.1    Hebecker, M.2    Svobodova, E.3    Jozsi, M.4
  • 110
    • 77950499825 scopus 로고    scopus 로고
    • Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells
    • Leffler J, Herbert AP, Norstrom E, et al. Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells. J Biol Chem. 2010;285:3766–3776.
    • (2010) J Biol Chem , vol.285 , pp. 3766-3776
    • Leffler, J.1    Herbert, A.P.2    Norstrom, E.3
  • 112
    • 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 KB. 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;192:1353–1363.
    • (2000) J Exp Med , vol.192 , pp. 1353-1363
    • Gershov, D.1    Kim, S.2    Brot, N.3    Elkon, K.B.4
  • 113
    • 33744956898 scopus 로고    scopus 로고
    • Regulation of complement activation by C-reactive protein: targeting of the inhibitory activity of C4b-binding protein
    • Sjoberg AP, Trouw LA, McGrath FD, Hack CE, Blom AM. Regulation of complement activation by C-reactive protein: targeting of the inhibitory activity of C4b-binding protein. J Immunol. 2006;176:7612–7620.
    • (2006) J Immunol , vol.176 , pp. 7612-7620
    • Sjoberg, A.P.1    Trouw, L.A.2    McGrath, F.D.3    Hack, C.E.4    Blom, A.M.5
  • 114
    • 82655181511 scopus 로고    scopus 로고
    • Monomeric C-reactive protein modulates classic complement activation on necrotic cells
    • Mihlan M, Blom AM, Kupreishvili K, et al. Monomeric C-reactive protein modulates classic complement activation on necrotic cells. Faseb J. 2011;25:4198–4210.
    • (2011) Faseb J , vol.25 , pp. 4198-4210
    • Mihlan, M.1    Blom, A.M.2    Kupreishvili, K.3
  • 115
    • 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 HM, et al. 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
  • 116
    • 0025663467 scopus 로고
    • Independent association of serum amyloid P component, protein S, and complement C4b with complement C4b-binding protein and subsequent association of the complex with membranes
    • Schwalbe RA, Dahlback B, Nelsestuen GL. Independent association of serum amyloid P component, protein S, and complement C4b with complement C4b-binding protein and subsequent association of the complex with membranes. J Biol Chem. 1990;265:21749–21757.
    • (1990) J Biol Chem , vol.265 , pp. 21749-21757
    • Schwalbe, R.A.1    Dahlback, B.2    Nelsestuen, G.L.3
  • 117
    • 0022966845 scopus 로고
    • Evidence for the binding of human serum amyloid P component to Clq and Fab gamma
    • Bristow CL, Boackle RJ. Evidence for the binding of human serum amyloid P component to Clq and Fab gamma. Mol Immunol. 1986;23:1045–1052.
    • (1986) Mol Immunol , vol.23 , pp. 1045-1052
    • Bristow, C.L.1    Boackle, R.J.2
  • 118
    • 2542580839 scopus 로고    scopus 로고
    • Autoimmunity and glomerulonephritis in mice with targeted deletion of the serum amyloid P component gene: SAP deficiency or strain combination?
    • Gillmore JD, Hutchinson WL, Herbert J, et al. Autoimmunity and glomerulonephritis in mice with targeted deletion of the serum amyloid P component gene: SAP deficiency or strain combination? Immunology. 2004;112:255–264.
    • (2004) Immunology , vol.112 , pp. 255-264
    • Gillmore, J.D.1    Hutchinson, W.L.2    Herbert, J.3
  • 119
    • 0034672233 scopus 로고    scopus 로고
    • The long pentraxin PTX3 binds to apoptotic cells and regulates their clearance by antigen-presenting dendritic cells
    • Rovere P, Peri G, Fazzini F, et al. The long pentraxin PTX3 binds to apoptotic cells and regulates their clearance by antigen-presenting dendritic cells. Blood. 2000;96:4300–4306.
    • (2000) Blood , vol.96 , pp. 4300-4306
    • Rovere, P.1    Peri, G.2    Fazzini, F.3
  • 120
    • 0345270024 scopus 로고    scopus 로고
    • Biochemical and functional characterization of the interaction between pentraxin 3 and C1q
    • Nauta AJ, Bottazzi B, Mantovani A, et al. Biochemical and functional characterization of the interaction between pentraxin 3 and C1q. Eur J Immunol. 2003;33:465–473.
    • (2003) Eur J Immunol , vol.33 , pp. 465-473
    • Nauta, A.J.1    Bottazzi, B.2    Mantovani, A.3
  • 121
    • 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 MJ, et al. 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
  • 122
    • 84922689090 scopus 로고    scopus 로고
    • PTX3 is an extrinsic oncosuppressor regulating complement-dependent inflammation in cancer
    • Bonavita E, Gentile S, Rubino M, et al. PTX3 is an extrinsic oncosuppressor regulating complement-dependent inflammation in cancer. Cell. 2015;160:700–714.
    • (2015) Cell , vol.160 , pp. 700-714
    • Bonavita, E.1    Gentile, S.2    Rubino, M.3
  • 123
    • 80051917349 scopus 로고    scopus 로고
    • Human pentraxin 3 binds to the complement regulator c4b-binding protein
    • Braunschweig A, Jozsi 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    Jozsi, M.2
  • 124
    • 33750717983 scopus 로고    scopus 로고
    • The tissue pentraxin PTX3 limits C1q-mediated complement activation and phagocytosis of apoptotic cells by dendritic cells
    • Baruah P, Dumitriu IE, Peri G, et al. The tissue pentraxin PTX3 limits C1q-mediated complement activation and phagocytosis of apoptotic cells by dendritic cells. J Leukoc Biol. 2006;80:87–95.
    • (2006) J Leukoc Biol , vol.80 , pp. 87-95
    • Baruah, P.1    Dumitriu, I.E.2    Peri, G.3
  • 125
    • 0036850609 scopus 로고    scopus 로고
    • Serum amyloid P component and C-reactive protein opsonize apoptotic cells for phagocytosis through Fcgamma receptors
    • Mold C, Baca R, Du Clos TW. Serum amyloid P component and C-reactive protein opsonize apoptotic cells for phagocytosis through Fcgamma receptors. J Autoimmun. 2002;19:147–154.
    • (2002) J Autoimmun , vol.19 , pp. 147-154
    • Mold, C.1    Baca, R.2    Du Clos, T.W.3
  • 126
    • 33748422653 scopus 로고    scopus 로고
    • Autoimmunity to protective molecules: is it the perpetuum mobile (vicious cycle) of autoimmune rheumatic diseases?
    • Kravitz MS, Shoenfeld Y. Autoimmunity to protective molecules: is it the perpetuum mobile (vicious cycle) of autoimmune rheumatic diseases? Nat Clin Pract Rheumatol. 2006;2:481–490.
    • (2006) Nat Clin Pract Rheumatol , vol.2 , pp. 481-490
    • Kravitz, M.S.1    Shoenfeld, Y.2
  • 127
    • 84944173170 scopus 로고    scopus 로고
    • PTX3, Anti-PTX3, and anti-C1q autoantibodies in lupus glomerulonephritis
    • Bassi N, Del Prete D, Ghirardello A, et al. PTX3, Anti-PTX3, and anti-C1q autoantibodies in lupus glomerulonephritis. Clin Rev Allergy Immunol. 2015;49:217–226.
    • (2015) Clin Rev Allergy Immunol , vol.49 , pp. 217-226
    • Bassi, N.1    Del Prete, D.2    Ghirardello, A.3
  • 128
    • 84954409820 scopus 로고    scopus 로고
    • Factor H uptake regulates intracellular C3 activation during apoptosis and decreases the inflammatory potential of nucleosomes
    • Martin M, Leffler J, Smolag K, et al. Factor H uptake regulates intracellular C3 activation during apoptosis and decreases the inflammatory potential of nucleosomes. Cell Death Differ. 2016;23:903–911.
    • (2016) Cell Death Differ , vol.23 , pp. 903-911
    • Martin, M.1    Leffler, J.2    Smolag, K.3
  • 129
    • 84890226478 scopus 로고    scopus 로고
    • Intracellular complement activation sustains T cell homeostasis and mediates effector differentiation
    • Liszewski MK, Kolev M, Le Friec G, et al. Intracellular complement activation sustains T cell homeostasis and mediates effector differentiation. Immunity. 2013;39:1143–1157.
    • (2013) Immunity , vol.39 , pp. 1143-1157
    • Liszewski, M.K.1    Kolev, M.2    Le Friec, G.3
  • 130
    • 59249097049 scopus 로고    scopus 로고
    • Complement receptor 1: disease associations and therapeutic implications
    • Khera R, Das N. Complement receptor 1: disease associations and therapeutic implications. Mol Immunol. 2009;46:761–772.
    • (2009) Mol Immunol , vol.46 , pp. 761-772
    • Khera, R.1    Das, N.2
  • 131
    • 0018758819 scopus 로고
    • Mac-1: a macrophage differentiation antigen identified by monoclonal antibody
    • Springer T, Galfre G, Secher DS, Milstein C. Mac-1: a macrophage differentiation antigen identified by monoclonal antibody. Eur J Immunol. 1979;9:301–306.
    • (1979) Eur J Immunol , vol.9 , pp. 301-306
    • Springer, T.1    Galfre, G.2    Secher, D.S.3    Milstein, C.4
  • 132
    • 0023204980 scopus 로고
    • Cellular distribution of complement receptor type 4 (CR4): expression on human platelets
    • Vik DP, Fearon DT. Cellular distribution of complement receptor type 4 (CR4): expression on human platelets. J Immunol. 1987;138:254–258.
    • (1987) J Immunol , vol.138 , pp. 254-258
    • Vik, D.P.1    Fearon, D.T.2
  • 134
    • 55949119669 scopus 로고    scopus 로고
    • A role of macrophage complement receptor CRIg in immune clearance and inflammation
    • He JQ, Wiesmann C, van Lookeren Campagne M. A role of macrophage complement receptor CRIg in immune clearance and inflammation. Mol Immunol. 2008;45:4041–4047.
    • (2008) Mol Immunol , vol.45 , pp. 4041-4047
    • He, J.Q.1    Wiesmann, C.2    van Lookeren Campagne, M.3
  • 135
    • 0036164008 scopus 로고    scopus 로고
    • Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus
    • Baumann I, Kolowos W, Voll RE, et al. Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus. Arthritis Rheum. 2002;46:191–201.
    • (2002) Arthritis Rheum , vol.46 , pp. 191-201
    • Baumann, I.1    Kolowos, W.2    Voll, R.E.3
  • 136
    • 0035153242 scopus 로고    scopus 로고
    • Secondary necrosis is a source of proteolytically modified forms of specific intracellular autoantigens: implications for systemic autoimmunity
    • Wu X, Molinaro C, Johnson N, Casiano CA. Secondary necrosis is a source of proteolytically modified forms of specific intracellular autoantigens: implications for systemic autoimmunity. Arthritis Rheum. 2001;44:2642–2652.
    • (2001) Arthritis Rheum , vol.44 , pp. 2642-2652
    • Wu, X.1    Molinaro, C.2    Johnson, N.3    Casiano, C.A.4
  • 137
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: a renewed sense of self
    • Matzinger P. The danger model: a renewed sense of self. Science. 2002;296:301–305.
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1
  • 138
    • 34247891509 scopus 로고    scopus 로고
    • Immunologically active autoantigens: the role of toll-like receptors in the development of chronic inflammatory disease
    • Marshak-Rothstein A, Rifkin IR. Immunologically active autoantigens: the role of toll-like receptors in the development of chronic inflammatory disease. Annu Rev Immunol. 2007;25:419–441.
    • (2007) Annu Rev Immunol , vol.25 , pp. 419-441
    • Marshak-Rothstein, A.1    Rifkin, I.R.2
  • 140
    • 79951777504 scopus 로고    scopus 로고
    • Nucleosome-induced neutrophil activation occurs independently of TLR9 and endosomal acidification: implications for systemic lupus erythematosus
    • Lindau D, Ronnefarth V, Erbacher A, Rammensee HG, Decker P. Nucleosome-induced neutrophil activation occurs independently of TLR9 and endosomal acidification: implications for systemic lupus erythematosus. Eur J Immunol. 2011;41:669–681.
    • (2011) Eur J Immunol , vol.41 , pp. 669-681
    • Lindau, D.1    Ronnefarth, V.2    Erbacher, A.3    Rammensee, H.G.4    Decker, P.5
  • 141
    • 84896289533 scopus 로고    scopus 로고
    • Cooperation of factor VII-activating protease and serum DNase I in the release of nucleosomes from necrotic cells
    • Stephan F, Marsman G, Bakker LM, et al. Cooperation of factor VII-activating protease and serum DNase I in the release of nucleosomes from necrotic cells. Arthritis Rheumatol. 2014;66:686–693.
    • (2014) Arthritis Rheumatol , vol.66 , pp. 686-693
    • Stephan, F.1    Marsman, G.2    Bakker, L.M.3
  • 142
    • 57349183177 scopus 로고    scopus 로고
    • Nucleosome-releasing factor: a new role for factor VII-activating protease (FSAP)
    • Zeerleder S, Zwart B, te Velthuis H, et al. Nucleosome-releasing factor: a new role for factor VII-activating protease (FSAP). Faseb J. 2008;22:4077–4084.
    • (2008) Faseb J , vol.22 , pp. 4077-4084
    • Zeerleder, S.1    Zwart, B.2    te Velthuis, H.3
  • 144
    • 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 MK. 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
  • 145
    • 0032522811 scopus 로고    scopus 로고
    • Human polymorphonuclear leukocytes adhere to complement factor H through an interaction that involves alphaMbeta2 (CD11b/CD18)
    • DiScipio RG, Daffern PJ, Schraufstatter IU, Sriramarao P. Human polymorphonuclear leukocytes adhere to complement factor H through an interaction that involves alphaMbeta2 (CD11b/CD18). JImmunol. 1998;160:4057–4066.
    • (1998) JImmunol , vol.160 , pp. 4057-4066
    • DiScipio, R.G.1    Daffern, P.J.2    Schraufstatter, I.U.3    Sriramarao, P.4
  • 146
    • 84858006658 scopus 로고    scopus 로고
    • Human complement factor H modulates C1q-mediated phagocytosis of apoptotic cells
    • Kang YH, Urban BC, Sim RB, Kishore U. Human complement factor H modulates C1q-mediated phagocytosis of apoptotic cells. Immunobiology. 2012;217:455–464.
    • (2012) Immunobiology , vol.217 , pp. 455-464
    • Kang, Y.H.1    Urban, B.C.2    Sim, R.B.3    Kishore, U.4
  • 147
    • 84941312858 scopus 로고    scopus 로고
    • Secreted aspartic protease 2 of Candida albicans inactivates factor H and the macrophage factor H-receptors CR3 (CD11b/CD18) and CR4 (CD11c/CD18)
    • Svoboda E, et al. Secreted aspartic protease 2 of Candida albicans inactivates factor H and the macrophage factor H-receptors CR3 (CD11b/CD18) and CR4 (CD11c/CD18). Immunol Lett. 2015;168:13–21.
    • (2015) Immunol Lett , vol.168 , pp. 13-21
    • Svoboda, E.1
  • 148
    • 84975077060 scopus 로고    scopus 로고
    • The complement inhibitor factor H generates an anti-inflammatory and tolerogenic state in monocyte-derived dendritic cells
    • Olivar R, et al. The complement inhibitor factor H generates an anti-inflammatory and tolerogenic state in monocyte-derived dendritic cells. J Immunol. 2016;196:427–490.
    • (2016) J Immunol , vol.196 , pp. 427-490
    • Olivar, R.1
  • 149
    • 84874842539 scopus 로고    scopus 로고
    • The alpha7beta0 isoform of the complement regulator C4b-binding protein induces a semimature, anti-inflammatory state in dendritic cells
    • Olivar R, Luque A, Naranjo-Gomez M, et al. The alpha7beta0 isoform of the complement regulator C4b-binding protein induces a semimature, anti-inflammatory state in dendritic cells. J Immunol. 2013;190:2857–2872.
    • (2013) J Immunol , vol.190 , pp. 2857-2872
    • Olivar, R.1    Luque, A.2    Naranjo-Gomez, M.3
  • 150
    • 79960013939 scopus 로고    scopus 로고
    • Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis
    • Ao W, Zheng H, Chen XW, Shen Y, Yang CD. Anti-annexin II antibody is associated with thrombosis and/or pregnancy morbidity in antiphospholipid syndrome and systemic lupus erythematosus with thrombosis. Rheumatol Int. 2011;31:865–869.
    • (2011) Rheumatol Int , vol.31 , pp. 865-869
    • Ao, W.1    Zheng, H.2    Chen, X.W.3    Shen, Y.4    Yang, C.D.5
  • 151
    • 33744481250 scopus 로고    scopus 로고
    • Autoantibodies against the fibrinolytic receptor, annexin 2, in antiphospholipid syndrome
    • Cesarman-Maus G, Rios-Luna NP, Deora AB, et al. Autoantibodies against the fibrinolytic receptor, annexin 2, in antiphospholipid syndrome. Blood. 2006;107:4375–4382.
    • (2006) Blood , vol.107 , pp. 4375-4382
    • Cesarman-Maus, G.1    Rios-Luna, N.P.2    Deora, A.B.3
  • 152
    • 84863624989 scopus 로고    scopus 로고
    • Annexin A5 and anti-annexin antibodies in patients with systemic lupus erythematosus
    • Hrycek A, Cieslik P. Annexin A5 and anti-annexin antibodies in patients with systemic lupus erythematosus. Rheumatol Int. 2012;32:1335–1342.
    • (2012) Rheumatol Int , vol.32 , pp. 1335-1342
    • Hrycek, A.1    Cieslik, P.2
  • 153
    • 4344625903 scopus 로고    scopus 로고
    • Antinuclear autoantibodies in systemic lupus erythematosus
    • Sawalha AH, Harley JB. Antinuclear autoantibodies in systemic lupus erythematosus. Curr Opin Rheumatol. 2004;16:534–540.
    • (2004) Curr Opin Rheumatol , vol.16 , pp. 534-540
    • Sawalha, A.H.1    Harley, J.B.2
  • 154
    • 84864925248 scopus 로고    scopus 로고
    • Factor H autoantibodies and deletion of complement factor H-related protein-1 in rheumatic diseases in comparison to atypical hemolytic uremic syndrome
    • Foltyn Zadura A, Zipfel PA, Bokarewa MI, et al. Factor H autoantibodies and deletion of complement factor H-related protein-1 in rheumatic diseases in comparison to atypical hemolytic uremic syndrome. Arthritis Res Ther. 2012;14:R185.
    • (2012) Arthritis Res Ther , vol.14 , pp. R185
    • Foltyn Zadura, A.1    Zipfel, P.A.2    Bokarewa, M.I.3
  • 155
    • 0035699547 scopus 로고    scopus 로고
    • Complement activation and inflammatory processes in Drusen formation and age related macular degeneration
    • Johnson LV, Leitner WP, Staples MK, Anderson DH. Complement activation and inflammatory processes in Drusen formation and age related macular degeneration. Exp Eye Res. 2001;73:887–896.
    • (2001) Exp Eye Res , vol.73 , pp. 887-896
    • Johnson, L.V.1    Leitner, W.P.2    Staples, M.K.3    Anderson, D.H.4
  • 156
    • 0036741098 scopus 로고    scopus 로고
    • A role for local inflammation in the formation of drusen in the aging eye
    • Anderson DH, Mullins RF, Hageman GS, Johnson LV. A role for local inflammation in the formation of drusen in the aging eye. Am J Ophthalmol. 2002;134:411–431.
    • (2002) Am J Ophthalmol , vol.134 , pp. 411-431
    • Anderson, D.H.1    Mullins, R.F.2    Hageman, G.S.3    Johnson, L.V.4
  • 157
    • 0034012166 scopus 로고    scopus 로고
    • Drusen associated with aging and age-related macular degeneration contain proteins common to extracellular deposits associated with atherosclerosis, elastosis, amyloidosis, and dense deposit disease
    • Mullins RF, Russell SR, Anderson DH, Hageman GS. Drusen associated with aging and age-related macular degeneration contain proteins common to extracellular deposits associated with atherosclerosis, elastosis, amyloidosis, and dense deposit disease. Faseb J. 2000;14:835–846.
    • (2000) Faseb J , vol.14 , pp. 835-846
    • Mullins, R.F.1    Russell, S.R.2    Anderson, D.H.3    Hageman, G.S.4
  • 158
    • 21044453724 scopus 로고    scopus 로고
    • A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration
    • Hageman GS, Anderson DH, Johnson LV, et al. A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration. Proc Natl Acad Sci USA. 2005;102:7227–7232.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7227-7232
    • Hageman, G.S.1    Anderson, D.H.2    Johnson, L.V.3
  • 159
    • 20244380171 scopus 로고    scopus 로고
    • Complement factor H polymorphism in age-related macular degeneration
    • Klein RJ, Zeiss C, Chew EY, et al. Complement factor H polymorphism in age-related macular degeneration. Science. 2005;308:385–389.
    • (2005) Science , vol.308 , pp. 385-389
    • Klein, R.J.1    Zeiss, C.2    Chew, E.Y.3
  • 161
    • 20244388812 scopus 로고    scopus 로고
    • Complement factor H variant increases the risk of age-related macular degeneration
    • Haines JL, Hauser MA, Schmidt S, et al. Complement factor H variant increases the risk of age-related macular degeneration. Science. 2005;308:419–421.
    • (2005) Science , vol.308 , pp. 419-421
    • Haines, J.L.1    Hauser, M.A.2    Schmidt, S.3
  • 162
    • 84910115978 scopus 로고    scopus 로고
    • Identification of factor H-like protein 1 as the predominant complement regulator in Bruch’s membrane: implications for age-related macular degeneration
    • Clark SJ, Schmidt CQ, White AM, Hakobyan S, Morgan BP, Bishop PN. Identification of factor H-like protein 1 as the predominant complement regulator in Bruch’s membrane: implications for age-related macular degeneration. J Immunol. 2014;193:4962–4970.
    • (2014) J Immunol , vol.193 , pp. 4962-4970
    • Clark, S.J.1    Schmidt, C.Q.2    White, A.M.3    Hakobyan, S.4    Morgan, B.P.5    Bishop, P.N.6
  • 163
    • 84887080613 scopus 로고    scopus 로고
    • Rare variants in CFI, C3 and C9 are associated with high risk of advanced age-related macular degeneration
    • Seddon JM, Yu Y, Miller EC, et al. Rare variants in CFI, C3 and C9 are associated with high risk of advanced age-related macular degeneration. Nat Genet. 2013;45:1366–1370.
    • (2013) Nat Genet , vol.45 , pp. 1366-1370
    • Seddon, J.M.1    Yu, Y.2    Miller, E.C.3
  • 164
    • 84879692071 scopus 로고    scopus 로고
    • A functional variant in the CFI gene confers a high risk of age-related macular degeneration
    • van de Ven JP, Nilsson SC, Tan PL, et al. A functional variant in the CFI gene confers a high risk of age-related macular degeneration. Nat Genet. 2013;45:813–817.
    • (2013) Nat Genet , vol.45 , pp. 813-817
    • van de Ven, J.P.1    Nilsson, S.C.2    Tan, P.L.3
  • 165
    • 0036875316 scopus 로고    scopus 로고
    • The role of apoptosis in age-related macular degeneration
    • Dunaief JL, Dentchev T, Ying GS, Milam AH. The role of apoptosis in age-related macular degeneration. Arch Ophthalmol. 2002;120:1435–1442.
    • (2002) Arch Ophthalmol , vol.120 , pp. 1435-1442
    • Dunaief, J.L.1    Dentchev, T.2    Ying, G.S.3    Milam, A.H.4
  • 166
    • 84865369140 scopus 로고    scopus 로고
    • Oxidative stress activates NLRP3 inflammasomes in ARPE-19 cells–implications for age-related macular degeneration (AMD)
    • Kauppinen A, Niskanen H, Suuronen T, Kinnunen K, Salminen A, Kaarniranta K. Oxidative stress activates NLRP3 inflammasomes in ARPE-19 cells–implications for age-related macular degeneration (AMD). Immunol Lett. 2012;147:29–33.
    • (2012) Immunol Lett , vol.147 , pp. 29-33
    • Kauppinen, A.1    Niskanen, H.2    Suuronen, T.3    Kinnunen, K.4    Salminen, A.5    Kaarniranta, K.6
  • 168
    • 0033795036 scopus 로고    scopus 로고
    • The role of oxidative stress in the pathogenesis of age-related macular degeneration
    • Beatty S, Koh H, Phil M, Henson D, Boulton M. The role of oxidative stress in the pathogenesis of age-related macular degeneration. Surv Ophthalmol. 2000;45:115–134.
    • (2000) Surv Ophthalmol , vol.45 , pp. 115-134
    • Beatty, S.1    Koh, H.2    Phil, M.3    Henson, D.4    Boulton, M.5
  • 169
    • 77249147331 scopus 로고    scopus 로고
    • The pivotal role of the complement system in aging and age-related macular degeneration: hypothesis re-visited
    • Anderson DH, Radeke MJ, Gallo NB, et al. The pivotal role of the complement system in aging and age-related macular degeneration: hypothesis re-visited. Prog Retin Eye Res. 2010;29:95–112.
    • (2010) Prog Retin Eye Res , vol.29 , pp. 95-112
    • Anderson, D.H.1    Radeke, M.J.2    Gallo, N.B.3
  • 170
    • 79959966904 scopus 로고    scopus 로고
    • Complement gene expression and regulation in mouse retina and retinal pigment epithelium/choroid
    • Luo C, Chen M, Xu H. Complement gene expression and regulation in mouse retina and retinal pigment epithelium/choroid. Mol Vis. 2011;17:1588–1597.
    • (2011) Mol Vis , vol.17 , pp. 1588-1597
    • Luo, C.1    Chen, M.2    Xu, H.3
  • 171
    • 84918826384 scopus 로고    scopus 로고
    • Expression of human complement factor h prevents age-related macular degeneration-like retina damage and kidney abnormalities in aged cfh knockout mice
    • Ding JD, Kelly U, Landowski M, et al. Expression of human complement factor h prevents age-related macular degeneration-like retina damage and kidney abnormalities in aged cfh knockout mice. Am J Pathol. 2015;185:29–42.
    • (2015) Am J Pathol , vol.185 , pp. 29-42
    • Ding, J.D.1    Kelly, U.2    Landowski, M.3
  • 172
    • 60549101748 scopus 로고    scopus 로고
    • Serum cystatin C level, kidney disease markers, and incidence of age-related macular degeneration: the Beaver Dam Eye Study
    • Klein R, Knudtson MD, Lee KE, Klein BE. Serum cystatin C level, kidney disease markers, and incidence of age-related macular degeneration: the Beaver Dam Eye Study. Arch Ophthalmol. 2009;127:193–199.
    • (2009) Arch Ophthalmol , vol.127 , pp. 193-199
    • Klein, R.1    Knudtson, M.D.2    Lee, K.E.3    Klein, B.E.4
  • 174
    • 84880667818 scopus 로고    scopus 로고
    • Cutting edge: the NLRP3 inflammasome links complement-mediated inflammation and IL-1beta release
    • Laudisi F, Spretafico R, Evrard M, et al. Cutting edge: the NLRP3 inflammasome links complement-mediated inflammation and IL-1beta release. J Immunol. 2013;191:1006–1010.
    • (2013) J Immunol , vol.191 , pp. 1006-1010
    • Laudisi, F.1    Spretafico, R.2    Evrard, M.3
  • 176
    • 84968813349 scopus 로고    scopus 로고
    • Complement-mediated ‘bystander’ damage initiates host NLRP3 inflammasome activation
    • Suresh R, Chandrasekaran P, Sutterwala FS, Mosser DM. Complement-mediated ‘bystander’ damage initiates host NLRP3 inflammasome activation. J Cell Sci. 2016;129:1928–1939.
    • (2016) J Cell Sci , vol.129 , pp. 1928-1939
    • Suresh, R.1    Chandrasekaran, P.2    Sutterwala, F.S.3    Mosser, D.M.4
  • 177
    • 84888240043 scopus 로고    scopus 로고
    • C3a modulates IL-1beta secretion in human monocytes by regulating ATP efflux and subsequent NLRP3 inflammasome activation
    • Asgari E, Le Friec G, Yamamoto H, et al. C3a modulates IL-1beta secretion in human monocytes by regulating ATP efflux and subsequent NLRP3 inflammasome activation. Blood. 2013;122:3473–3481.
    • (2013) Blood , vol.122 , pp. 3473-3481
    • Asgari, E.1    Le Friec, G.2    Yamamoto, H.3
  • 178
    • 84951746392 scopus 로고    scopus 로고
    • Complement component C5a primes retinal pigment epithelial cells for inflammasome activation by lipofuscin-mediated photooxidative damage
    • Brandstetter C, Holz FG, Krohne TU. Complement component C5a primes retinal pigment epithelial cells for inflammasome activation by lipofuscin-mediated photooxidative damage. J Biol Chem. 2015;290:31189–31198.
    • (2015) J Biol Chem , vol.290 , pp. 31189-31198
    • Brandstetter, C.1    Holz, F.G.2    Krohne, T.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.