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Volumn 274, Issue 1, 2016, Pages 307-329

Endothelial cells: source, barrier, and target of defensive mediators

Author keywords

atypical hemolytic uremic syndrome; complement system; endothelial cells; hemolysis; hemostasis; thrombosis

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; CLUSTERIN; COMPLEMENT; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; COMPLEMENT COMPONENT C2; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3D; COMPLEMENT COMPONENT C4; COMPLEMENT COMPONENT C4 BINDING PROTEIN; COMPLEMENT FACTOR H; COMPLEMENT INHIBITOR; COMPLEMENT MEMBRANE ATTACK COMPLEX; CYTOKINE; DECAY ACCELERATING FACTOR; ECULIZUMAB; ENDOTHELIAL PROTEIN C RECEPTOR; FIBRINOGEN; MEMBRANE COFACTOR PROTEIN; OPSONIN; PLASMA PROTEIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROPERDIN; THROMBOMODULIN; THROMBOPLASTIN; TISSUE FACTOR PATHWAY INHIBITOR; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

EID: 84992470016     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12479     Document Type: Review
Times cited : (88)

References (246)
  • 1
    • 0034053909 scopus 로고    scopus 로고
    • The endothelium: a new target for therapy
    • Cooke JP. The endothelium: a new target for therapy. Vasc Med. 2000;5:49–53.
    • (2000) Vasc Med , vol.5 , pp. 49-53
    • Cooke, J.P.1
  • 4
    • 84876398688 scopus 로고    scopus 로고
    • The complement system: history, pathways, cascade and inhibitors
    • Nesargikar PN, Spiller B, Chavez R. The complement system: history, pathways, cascade and inhibitors. Eur J Microbiol Immunol. 2012;2:103–111.
    • (2012) Eur J Microbiol Immunol , vol.2 , pp. 103-111
    • Nesargikar, P.N.1    Spiller, B.2    Chavez, R.3
  • 5
    • 84926665432 scopus 로고    scopus 로고
    • Complementing the sugar code: role of GAGs and sialic acid in complement regulation
    • Langford-Smith A, Day AJ, Bishop PN, Clark SJ. Complementing the sugar code: role of GAGs and sialic acid in complement regulation. Front Immunol. 2015;6:25.
    • (2015) Front Immunol , vol.6 , pp. 25
    • Langford-Smith, A.1    Day, A.J.2    Bishop, P.N.3    Clark, S.J.4
  • 7
    • 84929319009 scopus 로고    scopus 로고
    • Platelet secretion: from haemostasis to wound healing and beyond
    • Golebiewska EM, Poole AW. Platelet secretion: from haemostasis to wound healing and beyond. Blood Rev. 2015;29:153–162.
    • (2015) Blood Rev , vol.29 , pp. 153-162
    • Golebiewska, E.M.1    Poole, A.W.2
  • 8
    • 28344435221 scopus 로고    scopus 로고
    • Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions
    • Dong JF. Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions. J Thromb Haemost. 2005;3:1710–1716.
    • (2005) J Thromb Haemost , vol.3 , pp. 1710-1716
    • Dong, J.F.1
  • 9
    • 57749177100 scopus 로고    scopus 로고
    • ADAMTS-13 cleaves long von Willebrand factor multimeric strings anchored to endothelial cells in the absence of flow, platelets or conformation-altering chemicals
    • Turner N, Nolasco L, Dong JF, Moake J. ADAMTS-13 cleaves long von Willebrand factor multimeric strings anchored to endothelial cells in the absence of flow, platelets or conformation-altering chemicals. J Thromb Haemost. 2009;7:229–232.
    • (2009) J Thromb Haemost , vol.7 , pp. 229-232
    • Turner, N.1    Nolasco, L.2    Dong, J.F.3    Moake, J.4
  • 10
    • 84922002483 scopus 로고    scopus 로고
    • Fibrinolysis and the control of blood coagulation
    • Chapin JC, Hajjar KA. Fibrinolysis and the control of blood coagulation. Blood Rev. 2015;29:17–24.
    • (2015) Blood Rev , vol.29 , pp. 17-24
    • Chapin, J.C.1    Hajjar, K.A.2
  • 11
    • 33846849237 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of the endothelium: II. Representative vascular beds
    • Aird WC. Phenotypic heterogeneity of the endothelium: II. Representative vascular beds. Circ Res. 2007;100:174–190.
    • (2007) Circ Res , vol.100 , pp. 174-190
    • Aird, W.C.1
  • 12
    • 33846798106 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms
    • Aird WC. Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms. Circ Res. 2007;100:158–173.
    • (2007) Circ Res , vol.100 , pp. 158-173
    • Aird, W.C.1
  • 13
    • 0141814720 scopus 로고    scopus 로고
    • Endothelial cell diversity revealed by global expression profiling
    • Chi JT, Chang HY, Haraldsen G, et al. Endothelial cell diversity revealed by global expression profiling. Proc Natl Acad Sci USA. 2003;100:10623–10628.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10623-10628
    • Chi, J.T.1    Chang, H.Y.2    Haraldsen, G.3
  • 14
    • 84880948836 scopus 로고    scopus 로고
    • Molecular signatures of tissue-specific microvascular endothelial cell heterogeneity in organ maintenance and regeneration
    • Nolan DJ, Ginsberg M, Israely E, et al. Molecular signatures of tissue-specific microvascular endothelial cell heterogeneity in organ maintenance and regeneration. Dev Cell. 2013;26:204–219.
    • (2013) Dev Cell , vol.26 , pp. 204-219
    • Nolan, D.J.1    Ginsberg, M.2    Israely, E.3
  • 15
    • 57049103013 scopus 로고    scopus 로고
    • In vivo differences between endothelial transcriptional profiles of coronary and iliac arteries revealed by microarray analysis
    • Zhang J, Burridge KA, Friedman MH. In vivo differences between endothelial transcriptional profiles of coronary and iliac arteries revealed by microarray analysis. Am J Physiol Heart Circ Physiol. 2008;295:H1556–H1561.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295 , pp. H1556-H1561
    • Zhang, J.1    Burridge, K.A.2    Friedman, M.H.3
  • 16
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: happy together
    • Dejana E. Endothelial cell-cell junctions: happy together. Nat Rev Mol Cell Biol. 2004;5:261–270.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 261-270
    • Dejana, E.1
  • 17
    • 84871919637 scopus 로고    scopus 로고
    • In vivo imaging of cerebral microvascular plasticity from birth to death
    • Harb R, Whiteus C, Freitas C, Grutzendler J. In vivo imaging of cerebral microvascular plasticity from birth to death. J Cereb Blood Flow Metab. 2013;33:146–156.
    • (2013) J Cereb Blood Flow Metab , vol.33 , pp. 146-156
    • Harb, R.1    Whiteus, C.2    Freitas, C.3    Grutzendler, J.4
  • 18
    • 84907894707 scopus 로고    scopus 로고
    • Modulation of age-related insulin sensitivity by VEGF-dependent vascular plasticity in adipose tissues
    • Honek J, Seki T, Iwamoto H, et al. Modulation of age-related insulin sensitivity by VEGF-dependent vascular plasticity in adipose tissues. Proc Natl Acad Sci USA. 2014;111:14906–14911.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 14906-14911
    • Honek, J.1    Seki, T.2    Iwamoto, H.3
  • 19
    • 68049097209 scopus 로고    scopus 로고
    • Vascular consequences of dietary salt intake
    • Sanders PW. Vascular consequences of dietary salt intake. Am J Physiol Renal Physiol. 2009;297:F237–F243.
    • (2009) Am J Physiol Renal Physiol , vol.297 , pp. F237-F243
    • Sanders, P.W.1
  • 20
    • 84865396048 scopus 로고    scopus 로고
    • Dynamical systems approach to endothelial heterogeneity
    • Regan ER, Aird WC. Dynamical systems approach to endothelial heterogeneity. Circ Res. 2012;111:110–130.
    • (2012) Circ Res , vol.111 , pp. 110-130
    • Regan, E.R.1    Aird, W.C.2
  • 21
    • 0032532336 scopus 로고    scopus 로고
    • Tissue distribution and regulation of murine von Willebrand factor gene expression in vivo
    • Yamamoto K, de Waard V, Fearns C, Loskutoff DJ. Tissue distribution and regulation of murine von Willebrand factor gene expression in vivo. Blood. 1998;92:2791–2801.
    • (1998) Blood , vol.92 , pp. 2791-2801
    • Yamamoto, K.1    de Waard, V.2    Fearns, C.3    Loskutoff, D.J.4
  • 22
    • 84959565972 scopus 로고    scopus 로고
    • A role of stochastic phenotype switching in generating mosaic endothelial cell heterogeneity
    • Yuan L, Chan GC, Beeler D, et al. A role of stochastic phenotype switching in generating mosaic endothelial cell heterogeneity. Nat Commun. 2016;7:10160.
    • (2016) Nat Commun , vol.7 , pp. 10160
    • Yuan, L.1    Chan, G.C.2    Beeler, D.3
  • 23
    • 77953963085 scopus 로고    scopus 로고
    • Repressors NFI and NFY participate in organ-specific regulation of von Willebrand factor promoter activity in transgenic mice
    • Nassiri M, et al. Repressors NFI and NFY participate in organ-specific regulation of von Willebrand factor promoter activity in transgenic mice. Arterioscler Thromb Vasc Biol. 2010;30:1423–1429.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 1423-1429
    • Nassiri, M.1
  • 24
    • 33645123097 scopus 로고    scopus 로고
    • Immunohistochemical expression of endothelial markers CD31, CD34, von Willebrand factor, and Fli-1 in normal human tissues
    • Pusztaszeri MP, Seelentag W, Bosman FT. Immunohistochemical expression of endothelial markers CD31, CD34, von Willebrand factor, and Fli-1 in normal human tissues. J Histochem Cytochem. 2006;54:385–395.
    • (2006) J Histochem Cytochem , vol.54 , pp. 385-395
    • Pusztaszeri, M.P.1    Seelentag, W.2    Bosman, F.T.3
  • 25
    • 84988418999 scopus 로고    scopus 로고
    • Von Willebrand factor regulates complement on endothelial cells
    • Noone DG, Riedl M, Pluthero FG, et al. Von Willebrand factor regulates complement on endothelial cells. Kidney Int. 2016;90:123–134.
    • (2016) Kidney Int , vol.90 , pp. 123-134
    • Noone, D.G.1    Riedl, M.2    Pluthero, F.G.3
  • 26
    • 84954137061 scopus 로고    scopus 로고
    • TNF regulates essential alternative complement pathway components and impairs activation of protein c in human glomerular endothelial cells
    • Sartain SE, Turner NA, Moake JL. TNF regulates essential alternative complement pathway components and impairs activation of protein c in human glomerular endothelial cells. J Immunol. 2016;196:832–845.
    • (2016) J Immunol , vol.196 , pp. 832-845
    • Sartain, S.E.1    Turner, N.A.2    Moake, J.L.3
  • 27
    • 76949134627 scopus 로고
    • Thrombotic microangiopathic haemolytic anaemia (thrombotic microangiopathy)
    • Symmers WS. Thrombotic microangiopathic haemolytic anaemia (thrombotic microangiopathy). Br Med J. 1952;2:897–903.
    • (1952) Br Med J , vol.2 , pp. 897-903
    • Symmers, W.S.1
  • 28
    • 84936985706 scopus 로고    scopus 로고
    • Atypical aHUS: state of the art
    • Nester CM, et al. Atypical aHUS: state of the art. Mol Immunol. 2015;67:31–42.
    • (2015) Mol Immunol , vol.67 , pp. 31-42
    • Nester, C.M.1
  • 29
    • 84860341405 scopus 로고    scopus 로고
    • Improving on nature: redesigning ADAMTS13
    • Kremer Hovinga JA, Voorberg J. Improving on nature: redesigning ADAMTS13. Blood. 2012;119:3654–3655.
    • (2012) Blood , vol.119 , pp. 3654-3655
    • Kremer Hovinga, J.A.1    Voorberg, J.2
  • 30
    • 84867993202 scopus 로고    scopus 로고
    • Renal and neurological involvement in typical Shiga toxin-associated HUS
    • Trachtman H, Austin C, Lewinski M, Stahl RA. Renal and neurological involvement in typical Shiga toxin-associated HUS. Nat Rev Nephrol. 2012;8:658–669.
    • (2012) Nat Rev Nephrol , vol.8 , pp. 658-669
    • Trachtman, H.1    Austin, C.2    Lewinski, M.3    Stahl, R.A.4
  • 31
    • 84876044818 scopus 로고    scopus 로고
    • Genetics and outcome of atypical hemolytic uremic syndrome: a nationwide French series comparing children and adults
    • Fremeaux-Bacchi V, Fakhouri F, Garnier A, et al. Genetics and outcome of atypical hemolytic uremic syndrome: a nationwide French series comparing children and adults. Clin J Am Soc Nephrol. 2013;8:554–562.
    • (2013) Clin J Am Soc Nephrol , vol.8 , pp. 554-562
    • Fremeaux-Bacchi, V.1    Fakhouri, F.2    Garnier, A.3
  • 32
    • 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
  • 34
    • 84857439246 scopus 로고    scopus 로고
    • Genetics of hemolytic uremic syndromes
    • Malina M, Roumenina LT, Seeman T, et al. Genetics of hemolytic uremic syndromes. Presse Med. 2012;41:e105–e114.
    • (2012) Presse Med , vol.41 , pp. e105-e114
    • Malina, M.1    Roumenina, L.T.2    Seeman, T.3
  • 35
    • 84878608990 scopus 로고    scopus 로고
    • Recessive mutations in DGKE cause atypical hemolytic-uremic syndrome
    • Lemaire M, Fremeaux-Bacchi V, Schaefer F, et al. Recessive mutations in DGKE cause atypical hemolytic-uremic syndrome. Nat Genet. 2013;45:531–536.
    • (2013) Nat Genet , vol.45 , pp. 531-536
    • Lemaire, M.1    Fremeaux-Bacchi, V.2    Schaefer, F.3
  • 36
    • 36048948905 scopus 로고    scopus 로고
    • Hemolytic uremic syndrome (HUS) secondary to cobalamin C (cblC) disorder
    • Sharma AP, Greenberg CR, Prasad AN, Prasad C. Hemolytic uremic syndrome (HUS) secondary to cobalamin C (cblC) disorder. Pediatr Nephrol. 2007;22:2097–2103.
    • (2007) Pediatr Nephrol , vol.22 , pp. 2097-2103
    • Sharma, A.P.1    Greenberg, C.R.2    Prasad, A.N.3    Prasad, C.4
  • 37
    • 0014333339 scopus 로고
    • Genetic polymorphism of the third component of human complement (C'3)
    • Alper CA, Propp RP. Genetic polymorphism of the third component of human complement (C'3). J Clin Invest. 1968;47:2181–2191.
    • (1968) J Clin Invest , vol.47 , pp. 2181-2191
    • Alper, C.A.1    Propp, R.P.2
  • 38
    • 0016875193 scopus 로고
    • Biosynthesis of complement
    • Colten HR. Biosynthesis of complement. Adv Immunol. 1976;22:67–118.
    • (1976) Adv Immunol , vol.22 , pp. 67-118
    • Colten, H.R.1
  • 39
    • 2342581415 scopus 로고    scopus 로고
    • Maturation of dendritic cells abrogates C1q production in vivo and in vitro
    • Castellano G, Woltman AM, Nauta AJ, et al. Maturation of dendritic cells abrogates C1q production in vivo and in vitro. Blood. 2004;103:3813–3820.
    • (2004) Blood , vol.103 , pp. 3813-3820
    • Castellano, G.1    Woltman, A.M.2    Nauta, A.J.3
  • 40
    • 0343962980 scopus 로고    scopus 로고
    • Complement C1q is dramatically up-regulated in brain microglia in response to transient global cerebral ischemia
    • Schafer MK, Schwaeble WJ, Post C, et al. Complement C1q is dramatically up-regulated in brain microglia in response to transient global cerebral ischemia. J Immunol. 2000;164:5446–5452.
    • (2000) J Immunol , vol.164 , pp. 5446-5452
    • Schafer, M.K.1    Schwaeble, W.J.2    Post, C.3
  • 41
    • 0028790714 scopus 로고
    • Follicular dendritic cells, interdigitating cells, and cells of the monocyte-macrophage lineage are the C1q-producing sources in the spleen. Identification of specific cell types by in situ hybridization and immunohistochemical analysis
    • Schwaeble W, Schäfer MK, Petry F, et al. Follicular dendritic cells, interdigitating cells, and cells of the monocyte-macrophage lineage are the C1q-producing sources in the spleen. Identification of specific cell types by in situ hybridization and immunohistochemical analysis. J Immunol. 1995;155:4971–4978.
    • (1995) J Immunol , vol.155 , pp. 4971-4978
    • Schwaeble, W.1    Schäfer, M.K.2    Petry, F.3
  • 42
  • 43
    • 0029053689 scopus 로고
    • Complement expression in human brain. Biosynthesis of terminal pathway components and regulators in human glial cells and cell lines
    • Gasque P, Fontaine M, Morgan BP. Complement expression in human brain. Biosynthesis of terminal pathway components and regulators in human glial cells and cell lines. J Immunol. 1995;154:4726–4733.
    • (1995) J Immunol , vol.154 , pp. 4726-4733
    • Gasque, P.1    Fontaine, M.2    Morgan, B.P.3
  • 44
    • 79251544880 scopus 로고    scopus 로고
    • Complement alternative pathway acts as a positive feedback amplification of neutrophil activation
    • Camous L, Roumenina L, Bigot S, et al. Complement alternative pathway acts as a positive feedback amplification of neutrophil activation. Blood. 2011;117:1340–1349.
    • (2011) Blood , vol.117 , pp. 1340-1349
    • Camous, L.1    Roumenina, L.2    Bigot, S.3
  • 45
    • 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
  • 46
    • 0031135489 scopus 로고    scopus 로고
    • Properdin, a positive regulator of complement activation, is released from secondary granules of stimulated peripheral blood neutrophils
    • Wirthmueller U, Dewald B, Thelen M, et al. Properdin, a positive regulator of complement activation, is released from secondary granules of stimulated peripheral blood neutrophils. J Immunol. 1997;158:4444–4451.
    • (1997) J Immunol , vol.158 , pp. 4444-4451
    • Wirthmueller, U.1    Dewald, B.2    Thelen, M.3
  • 47
    • 0026638667 scopus 로고
    • Adipsin and an endogenous pathway of complement from adipose cells
    • Choy LN, Rosen BS, Spiegelman BM. Adipsin and an endogenous pathway of complement from adipose cells. J Biol Chem. 1992;267:12736–12741.
    • (1992) J Biol Chem , vol.267 , pp. 12736-12741
    • Choy, L.N.1    Rosen, B.S.2    Spiegelman, B.M.3
  • 48
    • 0030986767 scopus 로고    scopus 로고
    • TNF-alpha stimulates the biosynthesis of complement C3 and factor B by human umbilical cord vein endothelial cells
    • Kawakami Y, Watanabe Y, Yamaguchi M, Sakaguchi H, Kono I, Ueki A. TNF-alpha stimulates the biosynthesis of complement C3 and factor B by human umbilical cord vein endothelial cells. Cancer Lett. 1997;116:21–26.
    • (1997) Cancer Lett , vol.116 , pp. 21-26
    • Kawakami, Y.1    Watanabe, Y.2    Yamaguchi, M.3    Sakaguchi, H.4    Kono, I.5    Ueki, A.6
  • 49
    • 0028980191 scopus 로고
    • Activation of the endothelium by IL-1 alpha and glucocorticoids results in major increase of complement C3 and factor B production and generation of C3a
    • Coulpier M, Andreev S, Lemercier C, et al. Activation of the endothelium by IL-1 alpha and glucocorticoids results in major increase of complement C3 and factor B production and generation of C3a. Clin Exp Immunol. 1995;101:142–149.
    • (1995) Clin Exp Immunol , vol.101 , pp. 142-149
    • Coulpier, M.1    Andreev, S.2    Lemercier, C.3
  • 50
    • 84875597120 scopus 로고    scopus 로고
    • Assembly and activation of alternative complement components on endothelial cell-anchored ultra-large von Willebrand factor links complement and hemostasis-thrombosis
    • Turner NA, Moake J. Assembly and activation of alternative complement components on endothelial cell-anchored ultra-large von Willebrand factor links complement and hemostasis-thrombosis. PLoS ONE. 2013;8:e59372.
    • (2013) PLoS ONE , vol.8
    • Turner, N.A.1    Moake, J.2
  • 51
    • 0037213717 scopus 로고    scopus 로고
    • The endothelium as physiological source of properdin: role of wall shear stress
    • Bongrazio M, Pries AR, Zakrzewicz A. The endothelium as physiological source of properdin: role of wall shear stress. Mol Immunol. 2003;39:669–675.
    • (2003) Mol Immunol , vol.39 , pp. 669-675
    • Bongrazio, M.1    Pries, A.R.2    Zakrzewicz, A.3
  • 53
    • 0026508799 scopus 로고
    • Effect of interferon-gamma on complement gene expression in different cell types
    • Lappin DF, Guc D, Hill A, McShane T, Whaley K. Effect of interferon-gamma on complement gene expression in different cell types. Biochem J. 1992;281(Pt 2):437–442.
    • (1992) Biochem J , vol.281 , pp. 437-442
    • Lappin, D.F.1    Guc, D.2    Hill, A.3    McShane, T.4    Whaley, K.5
  • 54
    • 84896529758 scopus 로고    scopus 로고
    • C1q as a unique player in angiogenesis with therapeutic implication in wound healing
    • Bossi F, Tripodo C, Rizzi L, et al. C1q as a unique player in angiogenesis with therapeutic implication in wound healing. Proc Natl Acad Sci USA. 2014;111:4209–4214.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4209-4214
    • Bossi, F.1    Tripodo, C.2    Rizzi, L.3
  • 55
    • 40849101453 scopus 로고    scopus 로고
    • Decidual endothelial cells express surface-bound C1q as a molecular bridge between endovascular trophoblast and decidual endothelium
    • Bulla R, Agostinis C, Bossi F, et al. Decidual endothelial cells express surface-bound C1q as a molecular bridge between endovascular trophoblast and decidual endothelium. Mol Immunol. 2008;45:2629–2640.
    • (2008) Mol Immunol , vol.45 , pp. 2629-2640
    • Bulla, R.1    Agostinis, C.2    Bossi, F.3
  • 56
    • 84956640309 scopus 로고    scopus 로고
    • C1q acts in the tumour microenvironment as a cancer-promoting factor independently of complement activation
    • Bulla R, Tripodo C, Rami D, et al. C1q acts in the tumour microenvironment as a cancer-promoting factor independently of complement activation. Nat Commun. 2016;7:10346.
    • (2016) Nat Commun , vol.7 , pp. 10346
    • Bulla, R.1    Tripodo, C.2    Rami, D.3
  • 57
    • 77957200674 scopus 로고    scopus 로고
    • A revised model for the secretion of tPA and cytokines from cultured endothelial cells
    • Knipe L, Meli A, Hewlett L, et al. A revised model for the secretion of tPA and cytokines from cultured endothelial cells. Blood. 2010;116:2183–2191.
    • (2010) Blood , vol.116 , pp. 2183-2191
    • Knipe, L.1    Meli, A.2    Hewlett, L.3
  • 58
    • 0037447930 scopus 로고    scopus 로고
    • Von Willebrand factor targets IL-8 to Weibel-Palade bodies in an endothelial cell line
    • Romani de Wit T, et al. Von Willebrand factor targets IL-8 to Weibel-Palade bodies in an endothelial cell line. Exp Cell Res. 2003;286:67–74.
    • (2003) Exp Cell Res , vol.286 , pp. 67-74
    • Romani de Wit, T.1
  • 59
    • 84925625051 scopus 로고    scopus 로고
    • Regulatory components of the alternative complement pathway in endothelial cell cytoplasm, factor H and factor I, are not packaged in Weibel-Palade bodies
    • Turner NA, Sartain SE, Hui SK, Moake JL. Regulatory components of the alternative complement pathway in endothelial cell cytoplasm, factor H and factor I, are not packaged in Weibel-Palade bodies. PLoS ONE. 2015;10:e0121994.
    • (2015) PLoS ONE , vol.10
    • Turner, N.A.1    Sartain, S.E.2    Hui, S.K.3    Moake, J.L.4
  • 60
    • 35449008181 scopus 로고    scopus 로고
    • Requirements for cellular co-trafficking of factor VIII and von Willebrand factor to Weibel-Palade bodies
    • van den Biggelaar M, Bierings R, Storm G, Voorberg J, Mertens K. Requirements for cellular co-trafficking of factor VIII and von Willebrand factor to Weibel-Palade bodies. J Thromb Haemost. 2007;5:2235–2242.
    • (2007) J Thromb Haemost , vol.5 , pp. 2235-2242
    • van den Biggelaar, M.1    Bierings, R.2    Storm, G.3    Voorberg, J.4    Mertens, K.5
  • 61
    • 84926140659 scopus 로고    scopus 로고
    • von Willebrand factor biosynthesis, secretion, and clearance: connecting the far ends
    • Lenting PJ, Christophe OD, Denis CV. von Willebrand factor biosynthesis, secretion, and clearance: connecting the far ends. Blood. 2015;125:2019–2028.
    • (2015) Blood , vol.125 , pp. 2019-2028
    • Lenting, P.J.1    Christophe, O.D.2    Denis, C.V.3
  • 62
    • 0036893186 scopus 로고    scopus 로고
    • ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
    • Dong JF, Moake JL, Nolasco L, et al. ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood. 2002;100:4033–4039.
    • (2002) Blood , vol.100 , pp. 4033-4039
    • Dong, J.F.1    Moake, J.L.2    Nolasco, L.3
  • 63
    • 0037111571 scopus 로고    scopus 로고
    • Cloning, expression, and functional characterization of the von Willebrand factor-cleaving protease (ADAMTS13)
    • Plaimauer B, Zimmermann K, Völkel D, et al. Cloning, expression, and functional characterization of the von Willebrand factor-cleaving protease (ADAMTS13). Blood. 2002;100:3626–3632.
    • (2002) Blood , vol.100 , pp. 3626-3632
    • Plaimauer, B.1    Zimmermann, K.2    Völkel, D.3
  • 64
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler JE. Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem. 1998;67:395–424.
    • (1998) Annu Rev Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 65
    • 0017754787 scopus 로고
    • Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand’s disease
    • Weiss HJ, Sussman II, Hoyer LW. Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand’s disease. J Clin Invest. 1977;60:390–404.
    • (1977) J Clin Invest , vol.60 , pp. 390-404
    • Weiss, H.J.1    Sussman, I.I.2    Hoyer, L.W.3
  • 66
    • 33748802581 scopus 로고    scopus 로고
    • Update on the pathophysiology and classification of von Willebrand disease: a report of the Subcommittee on von Willebrand Factor
    • Sadler JE, Budde U, Eikenboom JC, et al. Update on the pathophysiology and classification of von Willebrand disease: a report of the Subcommittee on von Willebrand Factor. J Thromb Haemost. 2006;4:2103–2114.
    • (2006) J Thromb Haemost , vol.4 , pp. 2103-2114
    • Sadler, J.E.1    Budde, U.2    Eikenboom, J.C.3
  • 67
    • 84890087195 scopus 로고    scopus 로고
    • von Willebrand factor mutation promotes thrombocytopathy by inhibiting integrin alphaIIbbeta3
    • Casari C, Berrou E, Lebret M, et al. von Willebrand factor mutation promotes thrombocytopathy by inhibiting integrin alphaIIbbeta3. J Clin Invest. 2013;123:5071–5081.
    • (2013) J Clin Invest , vol.123 , pp. 5071-5081
    • Casari, C.1    Berrou, E.2    Lebret, M.3
  • 68
    • 77954750391 scopus 로고    scopus 로고
    • Mutation and ADAMTS13-dependent modulation of disease severity in a mouse model for von Willebrand disease type 2B
    • Rayes J, Hollestelle MJ, Legendre P, et al. Mutation and ADAMTS13-dependent modulation of disease severity in a mouse model for von Willebrand disease type 2B. Blood. 2010;115:4870–4877.
    • (2010) Blood , vol.115 , pp. 4870-4877
    • Rayes, J.1    Hollestelle, M.J.2    Legendre, P.3
  • 69
    • 33846445722 scopus 로고    scopus 로고
    • Effect of von Willebrand disease type 2B and type 2M mutations on the susceptibility of von Willebrand factor to ADAMTS-13
    • Rayes J, Hommais A, Legendre P, et al. Effect of von Willebrand disease type 2B and type 2M mutations on the susceptibility of von Willebrand factor to ADAMTS-13. J Thromb Haemost. 2007;5:321–328.
    • (2007) J Thromb Haemost , vol.5 , pp. 321-328
    • Rayes, J.1    Hommais, A.2    Legendre, P.3
  • 70
    • 0025727370 scopus 로고
    • Identification of a point mutation in type IIB von Willebrand disease illustrating the regulation of von Willebrand factor affinity for the platelet membrane glycoprotein Ib-IX receptor
    • Ware J, Dent JA, Azuma H, et al. Identification of a point mutation in type IIB von Willebrand disease illustrating the regulation of von Willebrand factor affinity for the platelet membrane glycoprotein Ib-IX receptor. Proc Natl Acad Sci USA. 1991;88:2946–2950.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2946-2950
    • Ware, J.1    Dent, J.A.2    Azuma, H.3
  • 71
    • 84922380155 scopus 로고    scopus 로고
    • von Willebrand factor is a cofactor in complement regulation
    • Feng S, Liang X, Kroll MH, Chung DW, Afshar-Kharghan V. von Willebrand factor is a cofactor in complement regulation. Blood. 2015;125:1034–1037.
    • (2015) Blood , vol.125 , pp. 1034-1037
    • Feng, S.1    Liang, X.2    Kroll, M.H.3    Chung, D.W.4    Afshar-Kharghan, V.5
  • 72
    • 84894451322 scopus 로고    scopus 로고
    • The interaction between factor H and VWF increases factor H cofactor activity and regulates VWF prothrombotic status
    • Rayes J, Roumenina LT, Dimitrov JD, et al. The interaction between factor H and VWF increases factor H cofactor activity and regulates VWF prothrombotic status. Blood. 2014;123:121–125.
    • (2014) Blood , vol.123 , pp. 121-125
    • Rayes, J.1    Roumenina, L.T.2    Dimitrov, J.D.3
  • 73
    • 84887122022 scopus 로고    scopus 로고
    • Human complement factor H is a reductase for large soluble von Willebrand factor multimers–brief report
    • Nolasco L, Nolasco J, Feng S, Afshar-Kharghan V, Moake J. Human complement factor H is a reductase for large soluble von Willebrand factor multimers–brief report. Arterioscler Thromb Vasc Biol. 2013;33:2524–2528.
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , pp. 2524-2528
    • Nolasco, L.1    Nolasco, J.2    Feng, S.3    Afshar-Kharghan, V.4    Moake, J.5
  • 74
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis
    • Drake TA, Morrissey JH, Edgington TS. Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am J Pathol. 1989;134:1087–1097.
    • (1989) Am J Pathol , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrissey, J.H.2    Edgington, T.S.3
  • 75
    • 0037027467 scopus 로고    scopus 로고
    • Elevated numbers of tissue-factor exposing microparticles correlate with components of the metabolic syndrome in uncomplicated type 2 diabetes mellitus
    • Diamant M, Nieuwland R, Pablo RF, Sturk A, Smit JW, Radder JK. Elevated numbers of tissue-factor exposing microparticles correlate with components of the metabolic syndrome in uncomplicated type 2 diabetes mellitus. Circulation. 2002;106:2442–2447.
    • (2002) Circulation , vol.106 , pp. 2442-2447
    • Diamant, M.1    Nieuwland, R.2    Pablo, R.F.3    Sturk, A.4    Smit, J.W.5    Radder, J.K.6
  • 76
    • 13044304178 scopus 로고    scopus 로고
    • Blood-borne tissue factor: another view of thrombosis
    • Giesen PL, Rauch U, Bohrmann B, et al. Blood-borne tissue factor: another view of thrombosis. Proc Natl Acad Sci USA. 1999;96:2311–2315.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2311-2315
    • Giesen, P.L.1    Rauch, U.2    Bohrmann, B.3
  • 78
    • 0037035464 scopus 로고    scopus 로고
    • Platelet-monocyte aggregates: bridging thrombosis and inflammation
    • Freedman JE, Loscalzo J. Platelet-monocyte aggregates: bridging thrombosis and inflammation. Circulation. 2002;105:2130–2132.
    • (2002) Circulation , vol.105 , pp. 2130-2132
    • Freedman, J.E.1    Loscalzo, J.2
  • 79
    • 0037362704 scopus 로고    scopus 로고
    • Intravascular tissue factor initiates coagulation via circulating microvesicles and platelets
    • Muller I, et al. Intravascular tissue factor initiates coagulation via circulating microvesicles and platelets. FASEB J. 2003;17:476–478.
    • (2003) FASEB J , vol.17 , pp. 476-478
    • Muller, I.1
  • 80
    • 33749118495 scopus 로고    scopus 로고
    • A novel C5a receptor-tissue factor cross-talk in neutrophils links innate immunity to coagulation pathways
    • Ritis K, et al. A novel C5a receptor-tissue factor cross-talk in neutrophils links innate immunity to coagulation pathways. J Immunol. 2006;177:4794–4802.
    • (2006) J Immunol , vol.177 , pp. 4794-4802
    • Ritis, K.1
  • 81
    • 84963542569 scopus 로고    scopus 로고
    • Tissue factor as a link between inflammation and coagulation
    • Witkowski M, Landmesser U, Rauch U. Tissue factor as a link between inflammation and coagulation. Trends Cardiovasc Med. 2016;26:297–303.
    • (2016) Trends Cardiovasc Med , vol.26 , pp. 297-303
    • Witkowski, M.1    Landmesser, U.2    Rauch, U.3
  • 82
    • 74049100937 scopus 로고    scopus 로고
    • Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability
    • Campbell RA, Overmyer KA, Selzman CH, Sheridan BC, Wolberg AS. Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability. Blood. 2009;114:4886–4896.
    • (2009) Blood , vol.114 , pp. 4886-4896
    • Campbell, R.A.1    Overmyer, K.A.2    Selzman, C.H.3    Sheridan, B.C.4    Wolberg, A.S.5
  • 84
    • 84955622452 scopus 로고    scopus 로고
    • Inhibition of complement component C5 prevents clotting in an ex vivo model of xenogeneic activation of coagulation
    • Rataj D, Werwitzke S, Haarmeijer B, et al. Inhibition of complement component C5 prevents clotting in an ex vivo model of xenogeneic activation of coagulation. Xenotransplantation. 2016;23:117–127.
    • (2016) Xenotransplantation , vol.23 , pp. 117-127
    • Rataj, D.1    Werwitzke, S.2    Haarmeijer, B.3
  • 85
    • 84860711841 scopus 로고    scopus 로고
    • A prevalent C3 mutation in aHUS patients causes a direct C3 convertase gain of function
    • Roumenina LT, Frimat M, Miller EC, et al. A prevalent C3 mutation in aHUS patients causes a direct C3 convertase gain of function. Blood. 2012;119:4182–4191.
    • (2012) Blood , vol.119 , pp. 4182-4191
    • Roumenina, L.T.1    Frimat, M.2    Miller, E.C.3
  • 86
    • 0023940013 scopus 로고
    • Tissue-type plasminogen activator binding to human endothelial cells. Evidence for two distinct binding sites
    • Barnathan ES, Kuo A, Van der Keyl H, McCrae KR, Larsen GR, Cines DB. Tissue-type plasminogen activator binding to human endothelial cells. Evidence for two distinct binding sites. J Biol Chem. 1988;263:7792–7799.
    • (1988) J Biol Chem , vol.263 , pp. 7792-7799
    • Barnathan, E.S.1    Kuo, A.2    Van der Keyl, H.3    McCrae, K.R.4    Larsen, G.R.5    Cines, D.B.6
  • 87
    • 0024418576 scopus 로고
    • A linear amino acid sequence involved in the interaction of t-PA with its endothelial cell receptor
    • Beebe DP, Miles LA, Plow EF. A linear amino acid sequence involved in the interaction of t-PA with its endothelial cell receptor. Blood. 1989;74:2034–2037.
    • (1989) Blood , vol.74 , pp. 2034-2037
    • Beebe, D.P.1    Miles, L.A.2    Plow, E.F.3
  • 89
    • 84876480772 scopus 로고    scopus 로고
    • Comprehensive analysis of glomerular mRNA expression of pro- and antithrombotic genes in atypical haemolytic-uremic syndrome (aHUS)
    • Modde F, Agustian PA, Wittig J, et al. Comprehensive analysis of glomerular mRNA expression of pro- and antithrombotic genes in atypical haemolytic-uremic syndrome (aHUS). Virchows Arch. 2013;462:455–464.
    • (2013) Virchows Arch , vol.462 , pp. 455-464
    • Modde, F.1    Agustian, P.A.2    Wittig, J.3
  • 90
    • 78650911190 scopus 로고    scopus 로고
    • The anti-inflammatory cytokine interleukin 19 is expressed by and angiogenic for human endothelial cells
    • Jain S, Gabunia K, Kelemen SE, Panetti TS, Autieri MV. The anti-inflammatory cytokine interleukin 19 is expressed by and angiogenic for human endothelial cells. Arterioscler Thromb Vasc Biol. 2011;31:167–175.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , pp. 167-175
    • Jain, S.1    Gabunia, K.2    Kelemen, S.E.3    Panetti, T.S.4    Autieri, M.V.5
  • 91
    • 0026437599 scopus 로고
    • Synthesis of TGF-beta 1 by vascular endothelial cells is correlated with cell spreading
    • Merrilees MJ, Sodek J. Synthesis of TGF-beta 1 by vascular endothelial cells is correlated with cell spreading. J Vasc Res. 1992;29:376–384.
    • (1992) J Vasc Res , vol.29 , pp. 376-384
    • Merrilees, M.J.1    Sodek, J.2
  • 92
    • 0031870338 scopus 로고    scopus 로고
    • Apoptosis in glomerular endothelial cells during the development of glomerulosclerosis in the remnant-kidney model
    • Kitamura H, Shimizu A, Masuda Y, Ishizaki M, Sugisaki Y, Yamanaka N. Apoptosis in glomerular endothelial cells during the development of glomerulosclerosis in the remnant-kidney model. Exp Nephrol. 1998;6:328–336.
    • (1998) Exp Nephrol , vol.6 , pp. 328-336
    • Kitamura, H.1    Shimizu, A.2    Masuda, Y.3    Ishizaki, M.4    Sugisaki, Y.5    Yamanaka, N.6
  • 93
    • 0029788758 scopus 로고    scopus 로고
    • Mesangial cell-derived transforming growth factor-beta 1 reduces macrophage adhesiveness with consequent deactivation
    • Suto TS, Fine LG, Kitamura M. Mesangial cell-derived transforming growth factor-beta 1 reduces macrophage adhesiveness with consequent deactivation. Kidney Int. 1996;50:445–452.
    • (1996) Kidney Int , vol.50 , pp. 445-452
    • Suto, T.S.1    Fine, L.G.2    Kitamura, M.3
  • 94
    • 34247265992 scopus 로고    scopus 로고
    • Pathogen recognition by Toll-like receptor 2 activates Weibel-Palade body exocytosis in human aortic endothelial cells
    • Into T, et al. Pathogen recognition by Toll-like receptor 2 activates Weibel-Palade body exocytosis in human aortic endothelial cells. J Biol Chem. 2007;282:8134–8141.
    • (2007) J Biol Chem , vol.282 , pp. 8134-8141
    • Into, T.1
  • 95
    • 0037066041 scopus 로고    scopus 로고
    • Expression of toll-like receptors in human atherosclerotic lesions: a possible pathway for plaque activation
    • Edfeldt K, Swedenborg J, Hansson GK, Yan ZQ. Expression of toll-like receptors in human atherosclerotic lesions: a possible pathway for plaque activation. Circulation. 2002;105:1158–1161.
    • (2002) Circulation , vol.105 , pp. 1158-1161
    • Edfeldt, K.1    Swedenborg, J.2    Hansson, G.K.3    Yan, Z.Q.4
  • 96
    • 0345798148 scopus 로고    scopus 로고
    • TLR4 signaling induces TLR2 expression in endothelial cells via neutrophil NADPH oxidase
    • Fan J, Frey RS, Malik AB. TLR4 signaling induces TLR2 expression in endothelial cells via neutrophil NADPH oxidase. J Clin Invest. 2003;112:1234–1243.
    • (2003) J Clin Invest , vol.112 , pp. 1234-1243
    • Fan, J.1    Frey, R.S.2    Malik, A.B.3
  • 97
    • 15444380849 scopus 로고    scopus 로고
    • IFN-alpha enhances TLR3-mediated antiviral cytokine expression in human endothelial and epithelial cells by up-regulating TLR3 expression
    • Tissari J, Siren J, Meri S, Julkunen I, Matikainen S. IFN-alpha enhances TLR3-mediated antiviral cytokine expression in human endothelial and epithelial cells by up-regulating TLR3 expression. J Immunol. 2005;174:4289–4294.
    • (2005) J Immunol , vol.174 , pp. 4289-4294
    • Tissari, J.1    Siren, J.2    Meri, S.3    Julkunen, I.4    Matikainen, S.5
  • 98
    • 84908611206 scopus 로고    scopus 로고
    • Dynamics of complement activation in aHUS and how to monitor eculizumab therapy
    • Noris M, Galbusera M, Gastoldi S, et al. Dynamics of complement activation in aHUS and how to monitor eculizumab therapy. Blood. 2014;124:1715–1726.
    • (2014) Blood , vol.124 , pp. 1715-1726
    • Noris, M.1    Galbusera, M.2    Gastoldi, S.3
  • 99
    • 70350475255 scopus 로고    scopus 로고
    • Hyperfunctional C3 convertase leads to complement deposition on endothelial cells and contributes to atypical hemolytic uremic syndrome
    • Roumenina LT, Jablonski M, Hue C, et al. Hyperfunctional C3 convertase leads to complement deposition on endothelial cells and contributes to atypical hemolytic uremic syndrome. Blood. 2009;114:2837–2845.
    • (2009) Blood , vol.114 , pp. 2837-2845
    • Roumenina, L.T.1    Jablonski, M.2    Hue, C.3
  • 100
    • 0026474486 scopus 로고
    • Relative roles of decay-accelerating factor, membrane cofactor protein, and CD59 in the protection of human endothelial cells against complement-mediated lysis
    • Brooimans RA, van Wieringen PA, van Es LA, Daha MR. Relative roles of decay-accelerating factor, membrane cofactor protein, and CD59 in the protection of human endothelial cells against complement-mediated lysis. Eur J Immunol. 1992;22:3135–3140.
    • (1992) Eur J Immunol , vol.22 , pp. 3135-3140
    • Brooimans, R.A.1    van Wieringen, P.A.2    van Es, L.A.3    Daha, M.R.4
  • 101
    • 84880923632 scopus 로고    scopus 로고
    • Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome
    • Frimat M, Tabarin F, Dimitrov JD, et al. Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome. Blood. 2013;122:282–292.
    • (2013) Blood , vol.122 , pp. 282-292
    • Frimat, M.1    Tabarin, F.2    Dimitrov, J.D.3
  • 103
    • 84870161177 scopus 로고    scopus 로고
    • Familial atypical hemolytic uremic syndrome: a review of its genetic and clinical aspects
    • Bu F, Borsa N, Gianluigi A, Smith RJ. Familial atypical hemolytic uremic syndrome: a review of its genetic and clinical aspects. Clin Dev Immunol. 2012;2012:370426.
    • (2012) Clin Dev Immunol , vol.2012 , pp. 370426
    • Bu, F.1    Borsa, N.2    Gianluigi, A.3    Smith, R.J.4
  • 104
    • 33745812440 scopus 로고    scopus 로고
    • Genetic and functional analyses of membrane cofactor protein (CD46) mutations in atypical hemolytic uremic syndrome
    • Fremeaux-Bacchi V, Moulton EA, Kavanagh D, et al. Genetic and functional analyses of membrane cofactor protein (CD46) mutations in atypical hemolytic uremic syndrome. J Am Soc Nephrol. 2006;17:2017–2025.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2017-2025
    • Fremeaux-Bacchi, V.1    Moulton, E.A.2    Kavanagh, D.3
  • 105
    • 85075591967 scopus 로고    scopus 로고
    • Complement regulator CD46: genetic variants and disease associations
    • Liszewski MK, Atkinson JP. Complement regulator CD46: genetic variants and disease associations. Hum Genomics. 2015;9:7.
    • (2015) Hum Genomics , vol.9 , pp. 7
    • Liszewski, M.K.1    Atkinson, J.P.2
  • 106
    • 84922349792 scopus 로고    scopus 로고
    • Loss of DGKepsilon induces endothelial cell activation and death independently of complement activation
    • Bruneau S, et al. Loss of DGKepsilon induces endothelial cell activation and death independently of complement activation. Blood. 2015;125:1038–1046.
    • (2015) Blood , vol.125 , pp. 1038-1046
    • Bruneau, S.1
  • 107
    • 0029946933 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP; CD46). Isoforms differ in protection against the classical pathway of complement
    • Liszewski MK, Atkinson JP. Membrane cofactor protein (MCP; CD46). Isoforms differ in protection against the classical pathway of complement. J Immunol. 1996;156:4415–4421.
    • (1996) J Immunol , vol.156 , pp. 4415-4421
    • Liszewski, M.K.1    Atkinson, J.P.2
  • 108
    • 0026538929 scopus 로고
    • The evolution of mouse and human complement C3-binding proteins: divergence of form but conservation of function
    • Holers VM, Kinoshita T, Molina H. The evolution of mouse and human complement C3-binding proteins: divergence of form but conservation of function. Immunol Today. 1992;13:231–236.
    • (1992) Immunol Today , vol.13 , pp. 231-236
    • Holers, V.M.1    Kinoshita, T.2    Molina, H.3
  • 109
    • 29144485392 scopus 로고    scopus 로고
    • Comparison of surface recognition and C3b binding properties of mouse and human complement factor H
    • Cheng ZZ, Hellwage J, Seeberger H, Zipfel PF, Meri S, Jokiranta TS. Comparison of surface recognition and C3b binding properties of mouse and human complement factor H. Mol Immunol. 2006;43:972–979.
    • (2006) Mol Immunol , vol.43 , pp. 972-979
    • Cheng, Z.Z.1    Hellwage, J.2    Seeberger, H.3    Zipfel, P.F.4    Meri, S.5    Jokiranta, T.S.6
  • 110
    • 34250329129 scopus 로고    scopus 로고
    • Spontaneous hemolytic uremic syndrome triggered by complement factor H lacking surface recognition domains
    • Pickering MC, de Jorge EG, Martinez-Barricarte R, et al. Spontaneous hemolytic uremic syndrome triggered by complement factor H lacking surface recognition domains. J Exp Med. 2007;204:1249–1256.
    • (2007) J Exp Med , vol.204 , pp. 1249-1256
    • Pickering, M.C.1    de Jorge, E.G.2    Martinez-Barricarte, R.3
  • 111
    • 85003581777 scopus 로고    scopus 로고
    • Partial Complement Factor H Deficiency Associates with C3 Glomerulopathy and Thrombotic Microangiopathy
    • Vernon KA, Ruseva MM, Cook HT, Botto M, Malik TH, Pickering MC. Partial Complement Factor H Deficiency Associates with C3 Glomerulopathy and Thrombotic Microangiopathy. J Am Soc Nephrol. 2016;27:1334–1342.
    • (2016) J Am Soc Nephrol , vol.27 , pp. 1334-1342
    • Vernon, K.A.1    Ruseva, M.M.2    Cook, H.T.3    Botto, M.4    Malik, T.H.5    Pickering, M.C.6
  • 112
    • 0036699540 scopus 로고    scopus 로고
    • Uncontrolled C3 activation causes membranoproliferative glomerulonephritis in mice deficient in complement factor H
    • Pickering MC, Cook HT, Warren J, et al. Uncontrolled C3 activation causes membranoproliferative glomerulonephritis in mice deficient in complement factor H. Nat Genet. 2002;31:424–428.
    • (2002) Nat Genet , vol.31 , pp. 424-428
    • Pickering, M.C.1    Cook, H.T.2    Warren, J.3
  • 113
    • 0028952777 scopus 로고
    • Hereditary porcine membranoproliferative glomerulonephritis type II is caused by factor H deficiency
    • Hogasen K, Jansen JH, Mollnes TE, Hovdenes J, Harboe M. Hereditary porcine membranoproliferative glomerulonephritis type II is caused by factor H deficiency. J Clin Invest. 1995;95:1054–1061.
    • (1995) J Clin Invest , vol.95 , pp. 1054-1061
    • Hogasen, K.1    Jansen, J.H.2    Mollnes, T.E.3    Hovdenes, J.4    Harboe, M.5
  • 115
    • 84857766493 scopus 로고    scopus 로고
    • Endothelium–role in regulation of coagulation and inflammation
    • van Hinsbergh VW. Endothelium–role in regulation of coagulation and inflammation. Semin Immunopathol. 2012;34:93–106.
    • (2012) Semin Immunopathol , vol.34 , pp. 93-106
    • van Hinsbergh, V.W.1
  • 116
    • 0030066667 scopus 로고    scopus 로고
    • Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils: in vivo and in vitro studies
    • Boehme MW, Deng Y, Raeth U, et al. Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils: in vivo and in vitro studies. Immunology. 1996;87:134–140.
    • (1996) Immunology , vol.87 , pp. 134-140
    • Boehme, M.W.1    Deng, Y.2    Raeth, U.3
  • 117
    • 84879175412 scopus 로고    scopus 로고
    • Thrombomodulin and the vascular endothelium: insights into functional, regulatory, and therapeutic aspects
    • Martin FA, Murphy RP, Cummins PM. Thrombomodulin and the vascular endothelium: insights into functional, regulatory, and therapeutic aspects. Am J Physiol Heart Circ Physiol. 2013;304:H1585–H1597.
    • (2013) Am J Physiol Heart Circ Physiol , vol.304 , pp. H1585-H1597
    • Martin, F.A.1    Murphy, R.P.2    Cummins, P.M.3
  • 118
    • 0029790055 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex
    • Stearns-Kurosawa DJ, Kurosawa S, Mollica JS, Ferrell GL, Esmon CT. The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex. Proc Natl Acad Sci USA. 1996;93:10212–10216.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10212-10216
    • Stearns-Kurosawa, D.J.1    Kurosawa, S.2    Mollica, J.S.3    Ferrell, G.L.4    Esmon, C.T.5
  • 119
    • 21544447526 scopus 로고    scopus 로고
    • Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition
    • Dahlback B, Villoutreix BO. Regulation of blood coagulation by the protein C anticoagulant pathway: novel insights into structure-function relationships and molecular recognition. Arterioscler Thromb Vasc Biol. 2005;25:1311–1320.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 1311-1320
    • Dahlback, B.1    Villoutreix, B.O.2
  • 120
    • 0030909690 scopus 로고    scopus 로고
    • Activated protein C prevents LPS-induced pulmonary vascular injury by inhibiting cytokine production
    • Murakami K, Okajima K, Uchiba M, et al. Activated protein C prevents LPS-induced pulmonary vascular injury by inhibiting cytokine production. Am J Physiol. 1997;272:L197–L202.
    • (1997) Am J Physiol , vol.272 , pp. L197-L202
    • Murakami, K.1    Okajima, K.2    Uchiba, M.3
  • 121
    • 17044427680 scopus 로고    scopus 로고
    • Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation
    • Feistritzer C, Riewald M. Endothelial barrier protection by activated protein C through PAR1-dependent sphingosine 1-phosphate receptor-1 crossactivation. Blood. 2005;105:3178–3184.
    • (2005) Blood , vol.105 , pp. 3178-3184
    • Feistritzer, C.1    Riewald, M.2
  • 122
    • 64849083719 scopus 로고    scopus 로고
    • Protection of vascular barrier integrity by activated protein C in murine models depends on protease-activated receptor-1
    • Schuepbach RA, Feistritzer C, Fernandez JA, Griffin JH, Riewald M. Protection of vascular barrier integrity by activated protein C in murine models depends on protease-activated receptor-1. Thromb Haemost. 2009;101:724–733.
    • (2009) Thromb Haemost , vol.101 , pp. 724-733
    • Schuepbach, R.A.1    Feistritzer, C.2    Fernandez, J.A.3    Griffin, J.H.4    Riewald, M.5
  • 123
    • 67651166873 scopus 로고    scopus 로고
    • Thrombomodulin mutations in atypical hemolytic-uremic syndrome
    • Delvaeye M, Noris M, De Vriese A, et al. Thrombomodulin mutations in atypical hemolytic-uremic syndrome. N Engl J Med. 2009;361:345–357.
    • (2009) N Engl J Med , vol.361 , pp. 345-357
    • Delvaeye, M.1    Noris, M.2    De Vriese, A.3
  • 124
    • 36348963516 scopus 로고    scopus 로고
    • Thrombomodulin is a clock-controlled gene in vascular endothelial cells
    • Takeda N, Maemura K, Horie S, et al. Thrombomodulin is a clock-controlled gene in vascular endothelial cells. J Biol Chem. 2007;282:32561–32567.
    • (2007) J Biol Chem , vol.282 , pp. 32561-32567
    • Takeda, N.1    Maemura, K.2    Horie, S.3
  • 125
    • 79960435714 scopus 로고    scopus 로고
    • Alternative pathway activation of complement by Shiga toxin promotes exuberant C3a formation that triggers microvascular thrombosis
    • Morigi M, Galbusera M, Gastoldi S, et al. Alternative pathway activation of complement by Shiga toxin promotes exuberant C3a formation that triggers microvascular thrombosis. J Immunol. 2011;187:172–180.
    • (2011) J Immunol , vol.187 , pp. 172-180
    • Morigi, M.1    Galbusera, M.2    Gastoldi, S.3
  • 126
    • 33744987414 scopus 로고    scopus 로고
    • Generation of C5a in the absence of C3: a new complement activation pathway
    • Huber-Lang M, Sarma JV, Zetoune FS, et al. Generation of C5a in the absence of C3: a new complement activation pathway. Nat Med. 2006;12:682–687.
    • (2006) Nat Med , vol.12 , pp. 682-687
    • Huber-Lang, M.1    Sarma, J.V.2    Zetoune, F.S.3
  • 127
    • 84865428866 scopus 로고    scopus 로고
    • Thrombin generates previously unidentified C5 products that support the terminal complement activation pathway
    • Krisinger MJ, Goebeler V, Lu Z, et al. Thrombin generates previously unidentified C5 products that support the terminal complement activation pathway. Blood. 2012;120:1717–1725.
    • (2012) Blood , vol.120 , pp. 1717-1725
    • Krisinger, M.J.1    Goebeler, V.2    Lu, Z.3
  • 128
    • 84936978963 scopus 로고    scopus 로고
    • Eculizumab reduces complement activation, inflammation, endothelial damage, thrombosis, and renal injury markers in aHUS
    • Cofiell R, Kukreja A, Bedard K, et al. Eculizumab reduces complement activation, inflammation, endothelial damage, thrombosis, and renal injury markers in aHUS. Blood. 2015;125:3253–3262.
    • (2015) Blood , vol.125 , pp. 3253-3262
    • Cofiell, R.1    Kukreja, A.2    Bedard, K.3
  • 129
    • 77952682366 scopus 로고    scopus 로고
    • Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome
    • Maga TK, Nishimura CJ, Weaver AE, Frees KL, Smith RJ. Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome. Hum Mutat. 2010;31:E1445–E1460.
    • (2010) Hum Mutat , vol.31 , pp. E1445-E1460
    • Maga, T.K.1    Nishimura, C.J.2    Weaver, A.E.3    Frees, K.L.4    Smith, R.J.5
  • 130
    • 33845513582 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: results of a phase III, randomized, double-blind clinical trial
    • Saito H, Maruyama I, Shimazaki S, et al. Efficacy and safety of recombinant human soluble thrombomodulin (ART-123) in disseminated intravascular coagulation: results of a phase III, randomized, double-blind clinical trial. J Thromb Haemost. 2007;5:31–41.
    • (2007) J Thromb Haemost , vol.5 , pp. 31-41
    • Saito, H.1    Maruyama, I.2    Shimazaki, S.3
  • 131
    • 84896839643 scopus 로고    scopus 로고
    • Recombinant soluble human thrombomodulin (thrombomodulin alfa) in the treatment of neonatal disseminated intravascular coagulation
    • Shirahata A, Mimuro J, Takahashi H, et al. Recombinant soluble human thrombomodulin (thrombomodulin alfa) in the treatment of neonatal disseminated intravascular coagulation. Eur J Pediatr. 2014;173:303–311.
    • (2014) Eur J Pediatr , vol.173 , pp. 303-311
    • Shirahata, A.1    Mimuro, J.2    Takahashi, H.3
  • 132
    • 84939610926 scopus 로고    scopus 로고
    • The efficacy of recombinant human soluble thrombomodulin for the treatment of shiga toxin-associated hemolytic uremic syndrome model mice
    • Suyama K, Kawasaki Y, Miyazaki K, et al. The efficacy of recombinant human soluble thrombomodulin for the treatment of shiga toxin-associated hemolytic uremic syndrome model mice. Nephrol Dial Transplant. 2015;30:969–977.
    • (2015) Nephrol Dial Transplant , vol.30 , pp. 969-977
    • Suyama, K.1    Kawasaki, Y.2    Miyazaki, K.3
  • 133
    • 84874628239 scopus 로고    scopus 로고
    • A novel strategy for hemolytic uremic syndrome: successful treatment with thrombomodulin alpha
    • Honda T, et al. A novel strategy for hemolytic uremic syndrome: successful treatment with thrombomodulin alpha. Pediatrics. 2013;131:e928–e933.
    • (2013) Pediatrics , vol.131 , pp. e928-e933
    • Honda, T.1
  • 134
    • 0037103283 scopus 로고    scopus 로고
    • Complement c3a and c5a induce different signal transduction cascades in endothelial cells
    • Schraufstatter IU, Trieu K, Sikora L, Sriramarao P, DiScipio R. Complement c3a and c5a induce different signal transduction cascades in endothelial cells. J Immunol. 2002;169:2102–2110.
    • (2002) J Immunol , vol.169 , pp. 2102-2110
    • Schraufstatter, I.U.1    Trieu, K.2    Sikora, L.3    Sriramarao, P.4    DiScipio, R.5
  • 135
    • 0037111535 scopus 로고    scopus 로고
    • Expression and function of C5a receptor in mouse microvascular endothelial cells
    • Laudes IJ, et al. Expression and function of C5a receptor in mouse microvascular endothelial cells. J Immunol. 2002;169:5962–5970.
    • (2002) J Immunol , vol.169 , pp. 5962-5970
    • Laudes, I.J.1
  • 137
    • 0037871469 scopus 로고    scopus 로고
    • Regulation by complement C3a and C5a anaphylatoxins of cytokine production in human umbilical vein endothelial cells
    • Monsinjon T, Gasque P, Chan P, Ischenko A, Brady JJ, Fontaine MC. Regulation by complement C3a and C5a anaphylatoxins of cytokine production in human umbilical vein endothelial cells. FASEB J. 2003;17:1003–1014.
    • (2003) FASEB J , vol.17 , pp. 1003-1014
    • Monsinjon, T.1    Gasque, P.2    Chan, P.3    Ischenko, A.4    Brady, J.J.5    Fontaine, M.C.6
  • 138
    • 0028049585 scopus 로고
    • C5a-induced expression of P-selectin in endothelial cells
    • Foreman KE, et al. C5a-induced expression of P-selectin in endothelial cells. J Clin Invest. 1994;94:1147–1155.
    • (1994) J Clin Invest , vol.94 , pp. 1147-1155
    • Foreman, K.E.1
  • 139
    • 84880125774 scopus 로고    scopus 로고
    • An engineered construct combining complement regulatory and surface-recognition domains represents a minimal-size functional factor H
    • Hebecker M, Alba-Domínguez M, Roumenina LT, et al. An engineered construct combining complement regulatory and surface-recognition domains represents a minimal-size functional factor H. J Immunol. 2013;191:912–921.
    • (2013) J Immunol , vol.191 , pp. 912-921
    • Hebecker, M.1    Alba-Domínguez, M.2    Roumenina, L.T.3
  • 140
    • 0031568525 scopus 로고    scopus 로고
    • C5a-dependent up-regulation in vivo of lung vascular P-selectin
    • Mulligan MS, Schmid E, Till GO, et al. C5a-dependent up-regulation in vivo of lung vascular P-selectin. J Immunol. 1997;158:1857–1861.
    • (1997) J Immunol , vol.158 , pp. 1857-1861
    • Mulligan, M.S.1    Schmid, E.2    Till, G.O.3
  • 141
    • 1242293775 scopus 로고    scopus 로고
    • C5a-induced gene expression in human umbilical vein endothelial cells
    • Albrecht EA, Chinnaiyan AM, Varambally S, et al. C5a-induced gene expression in human umbilical vein endothelial cells. Am J Pathol. 2004;164:849–859.
    • (2004) Am J Pathol , vol.164 , pp. 849-859
    • Albrecht, E.A.1    Chinnaiyan, A.M.2    Varambally, S.3
  • 142
    • 84938401520 scopus 로고    scopus 로고
    • C5a alters blood-brain barrier integrity in a human in vitro model of systemic lupus erythematosus
    • Mahajan SD, et al. C5a alters blood-brain barrier integrity in a human in vitro model of systemic lupus erythematosus. Immunology. 2015;146:130–143.
    • (2015) Immunology , vol.146 , pp. 130-143
    • Mahajan, S.D.1
  • 143
    • 58749112341 scopus 로고    scopus 로고
    • Activation by C5a of endothelial cell caspase 8 and cFLIP
    • Albrecht EA, Sarma JV, Ward PA. Activation by C5a of endothelial cell caspase 8 and cFLIP. Inflamm Res. 2009;58:30–37.
    • (2009) Inflamm Res , vol.58 , pp. 30-37
    • Albrecht, E.A.1    Sarma, J.V.2    Ward, P.A.3
  • 144
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell WD, Lazoura E, Okada N, Okada H. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol Immunol. 2002;46:131–134.
    • (2002) Microbiol Immunol , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 145
    • 84927592139 scopus 로고    scopus 로고
    • Is the complement activation product C3a a proinflammatory molecule? Re-evaluating the evidence and the myth
    • Coulthard LG, Woodruff TM. Is the complement activation product C3a a proinflammatory molecule? Re-evaluating the evidence and the myth. J Immunol. 2015;194:3542–3548.
    • (2015) J Immunol , vol.194 , pp. 3542-3548
    • Coulthard, L.G.1    Woodruff, T.M.2
  • 146
    • 84975138635 scopus 로고    scopus 로고
    • T helper 1 immunity requires complement-driven NLRP3 inflammasome activity in CD4(+) T cells
    • Arbore G, West EE, Spolski R, et al. T helper 1 immunity requires complement-driven NLRP3 inflammasome activity in CD4(+) T cells. Science. 2016;352:aad1210.
    • (2016) Science , vol.352 , pp. aad1210
    • Arbore, G.1    West, E.E.2    Spolski, R.3
  • 147
    • 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
  • 148
    • 0031010642 scopus 로고    scopus 로고
    • The cytolytically inactive terminal complement complex activates endothelial cells to express adhesion molecules and tissue factor procoagulant activity
    • Tedesco F, Pausa M, Nardon E, Introna M, Mantovani A, Dobrina A. The cytolytically inactive terminal complement complex activates endothelial cells to express adhesion molecules and tissue factor procoagulant activity. J Exp Med. 1997;185:1619–1627.
    • (1997) J Exp Med , vol.185 , pp. 1619-1627
    • Tedesco, F.1    Pausa, M.2    Nardon, E.3    Introna, M.4    Mantovani, A.5    Dobrina, A.6
  • 149
    • 9144246217 scopus 로고    scopus 로고
    • Platelet-activating factor and kinin-dependent vascular leakage as a novel functional activity of the soluble terminal complement complex
    • Bossi F, et al. Platelet-activating factor and kinin-dependent vascular leakage as a novel functional activity of the soluble terminal complement complex. J Immunol. 2004;173:6921–6927.
    • (2004) J Immunol , vol.173 , pp. 6921-6927
    • Bossi, F.1
  • 150
    • 0038297283 scopus 로고    scopus 로고
    • Intracerebroventricular injection of the terminal complement complex causes inflammatory reaction in the rat brain
    • Casarsa C, De Luigi A, Pausa M, De Simoni MG, Tedesco F. Intracerebroventricular injection of the terminal complement complex causes inflammatory reaction in the rat brain. Eur J Immunol. 2003;33:1260–1270.
    • (2003) Eur J Immunol , vol.33 , pp. 1260-1270
    • Casarsa, C.1    De Luigi, A.2    Pausa, M.3    De Simoni, M.G.4    Tedesco, F.5
  • 151
    • 0036092972 scopus 로고    scopus 로고
    • Cytolytically inactive terminal complement complex causes transendothelial migration of polymorphonuclear leukocytes in vitro and in vivo
    • Dobrina A, et al. Cytolytically inactive terminal complement complex causes transendothelial migration of polymorphonuclear leukocytes in vitro and in vivo. Blood. 2002;99:185–192.
    • (2002) Blood , vol.99 , pp. 185-192
    • Dobrina, A.1
  • 152
    • 37549036284 scopus 로고    scopus 로고
    • Endothelial cells are a target of both complement and kinin system
    • Bossi F, Bulla R, Tedesco F. Endothelial cells are a target of both complement and kinin system. Int Immunopharmacol. 2008;8:143–147.
    • (2008) Int Immunopharmacol , vol.8 , pp. 143-147
    • Bossi, F.1    Bulla, R.2    Tedesco, F.3
  • 154
    • 79952612300 scopus 로고    scopus 로고
    • Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement
    • Kajander T, et al. Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement. Proc Natl Acad Sci USA. 2011;108:2897–2902.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2897-2902
    • Kajander, T.1
  • 155
    • 84912036123 scopus 로고    scopus 로고
    • The role of heparan sulfate as determining pathogenic factor in complement factor H-associated diseases
    • Loeven MA, Rops AL, Berden JH, Daha MR, Rabelink TJ, van der Vlag J. The role of heparan sulfate as determining pathogenic factor in complement factor H-associated diseases. Mol Immunol. 2015;63:203–208.
    • (2015) Mol Immunol , vol.63 , pp. 203-208
    • Loeven, M.A.1    Rops, A.L.2    Berden, J.H.3    Daha, M.R.4    Rabelink, T.J.5    van der Vlag, J.6
  • 156
    • 84964691860 scopus 로고    scopus 로고
    • Mutations in complement factor H impair alternative pathway regulation on mouse glomerular endothelial cells in vitro
    • Loeven MA, Rops AL, Lehtinen MJ, et al. Mutations in complement factor H impair alternative pathway regulation on mouse glomerular endothelial cells in vitro. J Biol Chem. 2016;291:4974–4981.
    • (2016) J Biol Chem , vol.291 , pp. 4974-4981
    • Loeven, M.A.1    Rops, A.L.2    Lehtinen, M.J.3
  • 157
    • 0037396993 scopus 로고    scopus 로고
    • Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome
    • Manuelian T, Hellwage J, Meri S, et al. Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome. J Clin Invest. 2003;111:1181–1190.
    • (2003) J Clin Invest , vol.111 , pp. 1181-1190
    • Manuelian, T.1    Hellwage, J.2    Meri, S.3
  • 158
    • 84934443927 scopus 로고    scopus 로고
    • Functional evaluation of factor H genetic and acquired abnormalities: application for atypical hemolytic uremic syndrome (aHUS)
    • Roumenina LT, Roquigny R, Blanc C, et al. Functional evaluation of factor H genetic and acquired abnormalities: application for atypical hemolytic uremic syndrome (aHUS). Methods Mol Biol. 2014;1100:237–247.
    • (2014) Methods Mol Biol , vol.1100 , pp. 237-247
    • Roumenina, L.T.1    Roquigny, R.2    Blanc, C.3
  • 159
    • 79953772478 scopus 로고    scopus 로고
    • Structural basis for engagement by complement factor H of C3b on a self surface
    • Morgan HP, Schmidt CQ, Guariento M, et al. Structural basis for engagement by complement factor H of C3b on a self surface. Nat Struct Mol Biol. 2011;18:463–470.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 463-470
    • Morgan, H.P.1    Schmidt, C.Q.2    Guariento, M.3
  • 160
    • 84961792791 scopus 로고    scopus 로고
    • Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode
    • Forneris F, Wu J, Xue X, et al. Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode. EMBO J. 2016;35:1133–1149.
    • (2016) EMBO J , vol.35 , pp. 1133-1149
    • Forneris, F.1    Wu, J.2    Xue, X.3
  • 161
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu J, Wu YQ, Ricklin D, Janssen BJ, Lambris JD, 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
  • 162
    • 84874610717 scopus 로고    scopus 로고
    • Combined complement gene mutations in atypical hemolytic uremic syndrome influence clinical phenotype
    • Bresin E, Rurali E, Caprioli J, et al. Combined complement gene mutations in atypical hemolytic uremic syndrome influence clinical phenotype. J Am Soc Nephrol. 2013;24:475–486.
    • (2013) J Am Soc Nephrol , vol.24 , pp. 475-486
    • Bresin, E.1    Rurali, E.2    Caprioli, J.3
  • 163
    • 77958587405 scopus 로고    scopus 로고
    • Relative role of genetic complement abnormalities in sporadic and familial aHUS and their impact on clinical phenotype
    • Noris M, Caprioli J, Bresin E, et al. Relative role of genetic complement abnormalities in sporadic and familial aHUS and their impact on clinical phenotype. Clin J Am Soc Nephrol. 2010;5:1844–1859.
    • (2010) Clin J Am Soc Nephrol , vol.5 , pp. 1844-1859
    • Noris, M.1    Caprioli, J.2    Bresin, E.3
  • 164
    • 84866556872 scopus 로고    scopus 로고
    • Overall neutralization of complement factor H by autoantibodies in the acute phase of the autoimmune form of atypical hemolytic uremic syndrome
    • Blanc C, Roumenina LT, Ashraf Y, et al. Overall neutralization of complement factor H by autoantibodies in the acute phase of the autoimmune form of atypical hemolytic uremic syndrome. J Immunol. 2012;189:3528–3537.
    • (2012) J Immunol , vol.189 , pp. 3528-3537
    • Blanc, C.1    Roumenina, L.T.2    Ashraf, Y.3
  • 165
    • 34548853385 scopus 로고    scopus 로고
    • Anti factor H autoantibodies block C-terminal recognition function of factor H in hemolytic uremic syndrome
    • Jozsi M, Strobel S, Dahse HM, et al. 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
    • Jozsi, M.1    Strobel, S.2    Dahse, H.M.3
  • 166
    • 84949661472 scopus 로고    scopus 로고
    • Heterogeneity but individual constancy of epitopes, isotypes and avidity of factor H autoantibodies in atypical hemolytic uremic syndrome
    • Nozal P, Bernabéu-Herrero ME, Uzonyi B, et al. Heterogeneity but individual constancy of epitopes, isotypes and avidity of factor H autoantibodies in atypical hemolytic uremic syndrome. Mol Immunol. 2016;70:47–55.
    • (2016) Mol Immunol , vol.70 , pp. 47-55
    • Nozal, P.1    Bernabéu-Herrero, M.E.2    Uzonyi, B.3
  • 167
    • 84927526565 scopus 로고    scopus 로고
    • Mapping interactions between complement C3 and regulators using mutations in atypical hemolytic uremic syndrome
    • Schramm EC, Roumenina LT, Rybkine T, et al. Mapping interactions between complement C3 and regulators using mutations in atypical hemolytic uremic syndrome. Blood. 2015;125:2359–2369.
    • (2015) Blood , vol.125 , pp. 2359-2369
    • Schramm, E.C.1    Roumenina, L.T.2    Rybkine, T.3
  • 168
    • 85017140592 scopus 로고    scopus 로고
    • A familial C3GN secondary to defective C3 regulation by complement receptor 1 and complement factor H
    • Chauvet S, Roumenina LT, Bruneau S, et al. A familial C3GN secondary to defective C3 regulation by complement receptor 1 and complement factor H. J Am Soc Nephrol. 2016;27:1665–1677.
    • (2016) J Am Soc Nephrol , vol.27 , pp. 1665-1677
    • Chauvet, S.1    Roumenina, L.T.2    Bruneau, S.3
  • 170
    • 84867993256 scopus 로고    scopus 로고
    • Use of eculizumab for atypical haemolytic uraemic syndrome and C3 glomerulopathies
    • Zuber J, Fakhouri F, Roumenina LT, Loirat C, Fremeaux-Bacchi V, French Study Group for a HCG. Use of eculizumab for atypical haemolytic uraemic syndrome and C3 glomerulopathies. Nat Rev Nephrol. 2012;8:643–657.
    • (2012) Nat Rev Nephrol , vol.8 , pp. 643-657
    • Zuber, J.1    Fakhouri, F.2    Roumenina, L.T.3    Loirat, C.4    Fremeaux-Bacchi, V.5
  • 171
    • 74249114451 scopus 로고    scopus 로고
    • Mutations in complement factor I as found in atypical hemolytic uremic syndrome lead to either altered secretion or altered function of factor I
    • Nilsson SC, Kalchishkova N, Trouw LA, Fremeaux-Bacchi V, Villoutreix BO, Blom AM. Mutations in complement factor I as found in atypical hemolytic uremic syndrome lead to either altered secretion or altered function of factor I. Eur J Immunol. 2010;40:172–185.
    • (2010) Eur J Immunol , vol.40 , pp. 172-185
    • Nilsson, S.C.1    Kalchishkova, N.2    Trouw, L.A.3    Fremeaux-Bacchi, V.4    Villoutreix, B.O.5    Blom, A.M.6
  • 172
    • 37849022343 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: renal diseases associated with complement factor H: novel insights from humans and animals
    • Pickering MC, Cook HT. Translational mini-review series on complement factor H: renal diseases associated with complement factor H: novel insights from humans and animals. Clin Exp Immunol. 2008;151:210–230.
    • (2008) Clin Exp Immunol , vol.151 , pp. 210-230
    • Pickering, M.C.1    Cook, H.T.2
  • 173
    • 33846094404 scopus 로고    scopus 로고
    • Gain-of-function mutations in complement factor B are associated with atypical hemolytic uremic syndrome
    • Goicoechea de Jorge E, Harris CL, Esparza-Gordillo J, et al. Gain-of-function mutations in complement factor B are associated with atypical hemolytic uremic syndrome. Proc Natl Acad Sci USA. 2007;104:240–245.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 240-245
    • Goicoechea de Jorge, E.1    Harris, C.L.2    Esparza-Gordillo, J.3
  • 174
    • 84902283995 scopus 로고    scopus 로고
    • Complement factor B mutations in atypical hemolytic uremic syndrome-disease-relevant or benign?
    • Marinozzi MC, Vergoz L, Rybkine T, et al. Complement factor B mutations in atypical hemolytic uremic syndrome-disease-relevant or benign? J Am Soc Nephrol. 2014;25:2053–2065.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 2053-2065
    • Marinozzi, M.C.1    Vergoz, L.2    Rybkine, T.3
  • 175
    • 54049137505 scopus 로고    scopus 로고
    • Mutations in complement C3 predispose to development of atypical hemolytic uremic syndrome
    • Fremeaux-Bacchi V, Miller EC, Liszewski MK, et al. Mutations in complement C3 predispose to development of atypical hemolytic uremic syndrome. Blood. 2008;112:4948–4952.
    • (2008) Blood , vol.112 , pp. 4948-4952
    • Fremeaux-Bacchi, V.1    Miller, E.C.2    Liszewski, M.K.3
  • 176
    • 84958237174 scopus 로고    scopus 로고
    • Complement gene variants determine the risk of immunoglobulin-associated MPGN and C3 glomerulopathy and predict long-term renal outcome
    • Iatropoulos P, Noris M, Mele C, et al. Complement gene variants determine the risk of immunoglobulin-associated MPGN and C3 glomerulopathy and predict long-term renal outcome. Mol Immunol. 2016;71:131–142.
    • (2016) Mol Immunol , vol.71 , pp. 131-142
    • Iatropoulos, P.1    Noris, M.2    Mele, C.3
  • 177
    • 84868585648 scopus 로고    scopus 로고
    • Sensitive and specific assays for C3 nephritic factors clarify mechanisms underlying complement dysregulation
    • Paixao-Cavalcante D, López-Trascasa M, Skattum L, et al. Sensitive and specific assays for C3 nephritic factors clarify mechanisms underlying complement dysregulation. Kidney Int. 2012;82:1084–1092.
    • (2012) Kidney Int , vol.82 , pp. 1084-1092
    • Paixao-Cavalcante, D.1    López-Trascasa, M.2    Skattum, L.3
  • 178
    • 84864554927 scopus 로고    scopus 로고
    • Acquired and genetic complement abnormalities play a critical role in dense deposit disease and other C3 glomerulopathies
    • Servais A, Noël LH, Roumenina LT, et al. Acquired and genetic complement abnormalities play a critical role in dense deposit disease and other C3 glomerulopathies. Kidney Int. 2012;82:454–464.
    • (2012) Kidney Int , vol.82 , pp. 454-464
    • Servais, A.1    Noël, L.H.2    Roumenina, L.T.3
  • 179
    • 84863115476 scopus 로고    scopus 로고
    • Causes of alternative pathway dysregulation in dense deposit disease
    • Zhang Y, et al. Causes of alternative pathway dysregulation in dense deposit disease. Clin J Am Soc Nephrol. 2012;7:265–274.
    • (2012) Clin J Am Soc Nephrol , vol.7 , pp. 265-274
    • Zhang, Y.1
  • 180
    • 84973255900 scopus 로고    scopus 로고
    • Complement genetics and susceptibility to inflammatory disease. Lessons from genotype-phenotype correlations
    • de Cordoba SR. Complement genetics and susceptibility to inflammatory disease. Lessons from genotype-phenotype correlations. Immunobiology. 2016;221:709–714.
    • (2016) Immunobiology , vol.221 , pp. 709-714
    • de Cordoba, S.R.1
  • 181
    • 80054080494 scopus 로고    scopus 로고
    • Regulation and functions of diacylglycerol kinases
    • Shulga YV, Topham MK, Epand RM. Regulation and functions of diacylglycerol kinases. Chem Rev. 2011;111:6186–6208.
    • (2011) Chem Rev , vol.111 , pp. 6186-6208
    • Shulga, Y.V.1    Topham, M.K.2    Epand, R.M.3
  • 182
    • 82555196675 scopus 로고    scopus 로고
    • Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle
    • Shulga YV, Topham MK, Epand RM. Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle. FEBS Lett. 2011;585:4025–4028.
    • (2011) FEBS Lett , vol.585 , pp. 4025-4028
    • Shulga, Y.V.1    Topham, M.K.2    Epand, R.M.3
  • 183
    • 84943169582 scopus 로고    scopus 로고
    • Atypical haemolytic uraemic syndrome in a Japanese patient with DGKE genetic mutations
    • Miyata T, Uchida Y, Ohta T, Urayama K, Yoshida Y, Fujimura Y. Atypical haemolytic uraemic syndrome in a Japanese patient with DGKE genetic mutations. Thromb Haemost. 2015;114:862–863.
    • (2015) Thromb Haemost , vol.114 , pp. 862-863
    • Miyata, T.1    Uchida, Y.2    Ohta, T.3    Urayama, K.4    Yoshida, Y.5    Fujimura, Y.6
  • 184
    • 84902135216 scopus 로고    scopus 로고
    • Phenotypic expansion of DGKE-associated diseases
    • Westland R, Bodria M, Carrea A, et al. Phenotypic expansion of DGKE-associated diseases. J Am Soc Nephrol. 2014;25:1408–1414.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 1408-1414
    • Westland, R.1    Bodria, M.2    Carrea, A.3
  • 185
    • 84940956200 scopus 로고    scopus 로고
    • Complement factor H, FHR-3 and FHR-1 variants associate in an extended haplotype conferring increased risk of atypical hemolytic uremic syndrome
    • Bernabeu-Herrero ME, Jiménez-Alcázar M, Anter J, et al. Complement factor H, FHR-3 and FHR-1 variants associate in an extended haplotype conferring increased risk of atypical hemolytic uremic syndrome. Mol Immunol. 2015;67:276–286.
    • (2015) Mol Immunol , vol.67 , pp. 276-286
    • Bernabeu-Herrero, M.E.1    Jiménez-Alcázar, M.2    Anter, J.3
  • 186
    • 75749153964 scopus 로고    scopus 로고
    • Mutations in components of complement influence the outcome of Factor I-associated atypical hemolytic uremic syndrome
    • Bienaime F, Dragon-Durey MA, Regnier CH, et al. Mutations in components of complement influence the outcome of Factor I-associated atypical hemolytic uremic syndrome. Kidney Int. 2010;77:339–349.
    • (2010) Kidney Int , vol.77 , pp. 339-349
    • Bienaime, F.1    Dragon-Durey, M.A.2    Regnier, C.H.3
  • 187
    • 84874417661 scopus 로고    scopus 로고
    • Complement genes strongly predict recurrence and graft outcome in adult renal transplant recipients with atypical hemolytic and uremic syndrome
    • Le Quintrec M, Zuber J, Moulin B, et al. Complement genes strongly predict recurrence and graft outcome in adult renal transplant recipients with atypical hemolytic and uremic syndrome. Am J Transplant. 2013;13:663–675.
    • (2013) Am J Transplant , vol.13 , pp. 663-675
    • Le Quintrec, M.1    Zuber, J.2    Moulin, B.3
  • 188
    • 80053572803 scopus 로고    scopus 로고
    • Age-related penetrance of hereditary atypical hemolytic uremic syndrome
    • Sullivan M, Rybicki LA, Winter A, et al. Age-related penetrance of hereditary atypical hemolytic uremic syndrome. Ann Hum Genet. 2011;75:639–647.
    • (2011) Ann Hum Genet , vol.75 , pp. 639-647
    • Sullivan, M.1    Rybicki, L.A.2    Winter, A.3
  • 189
    • 84891753035 scopus 로고    scopus 로고
    • Comprehensive genetic analysis of complement and coagulation genes in atypical hemolytic uremic syndrome
    • Bu F, Maga T, Meyer NC, et al. Comprehensive genetic analysis of complement and coagulation genes in atypical hemolytic uremic syndrome. J Am Soc Nephrol. 2014;25:55–64.
    • (2014) J Am Soc Nephrol , vol.25 , pp. 55-64
    • Bu, F.1    Maga, T.2    Meyer, N.C.3
  • 191
    • 77952556624 scopus 로고    scopus 로고
    • Pregnancy-associated hemolytic uremic syndrome revisited in the era of complement gene mutations
    • Fakhouri F, Roumenina L, Provot F, et al. Pregnancy-associated hemolytic uremic syndrome revisited in the era of complement gene mutations. J Am Soc Nephrol. 2010;21:859–867.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 859-867
    • Fakhouri, F.1    Roumenina, L.2    Provot, F.3
  • 192
    • 84894567032 scopus 로고    scopus 로고
    • Heme triggers TLR4 signaling leading to endothelial cell activation and vaso-occlusion in murine sickle cell disease
    • Belcher JD, Chen C, Nguyen J, et al. Heme triggers TLR4 signaling leading to endothelial cell activation and vaso-occlusion in murine sickle cell disease. Blood. 2014;123:377–390.
    • (2014) Blood , vol.123 , pp. 377-390
    • Belcher, J.D.1    Chen, C.2    Nguyen, J.3
  • 194
    • 70450233529 scopus 로고    scopus 로고
    • ADP signaling in vascular endothelial cells: ADP-dependent activation of the endothelial isoform of nitric-oxide synthase requires the expression but not the kinase activity of AMP-activated protein kinase
    • Hess CN, Kou R, Johnson RP, Li GK, Michel T. ADP signaling in vascular endothelial cells: ADP-dependent activation of the endothelial isoform of nitric-oxide synthase requires the expression but not the kinase activity of AMP-activated protein kinase. J Biol Chem. 2009;284:32209–32224.
    • (2009) J Biol Chem , vol.284 , pp. 32209-32224
    • Hess, C.N.1    Kou, R.2    Johnson, R.P.3    Li, G.K.4    Michel, T.5
  • 195
    • 0026486191 scopus 로고
    • Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: a mechanism for stabilizing neutrophil adhesion
    • Sugama Y, Tiruppathi C, Offakidevi K, Andersen TT, Fenton JW 2nd, Malik AB. Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: a mechanism for stabilizing neutrophil adhesion. J Cell Biol. 1992;119:935–944.
    • (1992) J Cell Biol , vol.119 , pp. 935-944
    • Sugama, Y.1    Tiruppathi, C.2    Offakidevi, K.3    Andersen, T.T.4    Fenton, J.W.5    Malik, A.B.6
  • 196
    • 70349240615 scopus 로고    scopus 로고
    • Weibel-Palade bodies–sentinels of acute stress
    • Goligorsky MS, Patschan D, Kuo MC. Weibel-Palade bodies–sentinels of acute stress. Nat Rev Nephrol. 2009;5:423–426.
    • (2009) Nat Rev Nephrol , vol.5 , pp. 423-426
    • Goligorsky, M.S.1    Patschan, D.2    Kuo, M.C.3
  • 197
    • 17144418992 scopus 로고    scopus 로고
    • Platelet activation leads to activation and propagation of the complement system
    • Del Conde I, Cruz MA, Zhang H, Lopez JA, Afshar-Kharghan V. Platelet activation leads to activation and propagation of the complement system. J Exp Med. 2005;201:871–879.
    • (2005) J Exp Med , vol.201 , pp. 871-879
    • Del Conde, I.1    Cruz, M.A.2    Zhang, H.3    Lopez, J.A.4    Afshar-Kharghan, V.5
  • 198
    • 27144476793 scopus 로고    scopus 로고
    • Activated platelets induce Weibel-Palade-body secretion and leukocyte rolling in vivo: role of P-selectin
    • Dole VS, Bergmeier W, Mitchell HA, Eichenberger SC, Wagner DD. Activated platelets induce Weibel-Palade-body secretion and leukocyte rolling in vivo: role of P-selectin. Blood. 2005;106:2334–2339.
    • (2005) Blood , vol.106 , pp. 2334-2339
    • Dole, V.S.1    Bergmeier, W.2    Mitchell, H.A.3    Eichenberger, S.C.4    Wagner, D.D.5
  • 199
    • 38449088657 scopus 로고    scopus 로고
    • Hematin promotes complement alternative pathway-mediated deposition of C3 activation fragments on human erythrocytes: potential implications for the pathogenesis of anemia in malaria
    • Pawluczkowycz AW, Lindorfer MA, Waitumbi JN, Taylor RP. Hematin promotes complement alternative pathway-mediated deposition of C3 activation fragments on human erythrocytes: potential implications for the pathogenesis of anemia in malaria. J Immunol. 2007;179:5543–5552.
    • (2007) J Immunol , vol.179 , pp. 5543-5552
    • Pawluczkowycz, A.W.1    Lindorfer, M.A.2    Waitumbi, J.N.3    Taylor, R.P.4
  • 201
    • 33847058366 scopus 로고    scopus 로고
    • Iron ions and haeme modulate the binding properties of complement subcomponent C1q and of immunoglobulins
    • Dimitrov JD, Roumenina LT, Doltchinkova VR, Vassilev TL. Iron ions and haeme modulate the binding properties of complement subcomponent C1q and of immunoglobulins. Scand J Immunol. 2007;65:230–239.
    • (2007) Scand J Immunol , vol.65 , pp. 230-239
    • Dimitrov, J.D.1    Roumenina, L.T.2    Doltchinkova, V.R.3    Vassilev, T.L.4
  • 202
    • 79955537165 scopus 로고    scopus 로고
    • Heme interacts with c1q and inhibits the classical complement pathway
    • Roumenina LT, Radanova M, Atanasov BP, et al. Heme interacts with c1q and inhibits the classical complement pathway. J Biol Chem. 2011;286:16459–16469.
    • (2011) J Biol Chem , vol.286 , pp. 16459-16469
    • Roumenina, L.T.1    Radanova, M.2    Atanasov, B.P.3
  • 203
    • 11244281582 scopus 로고    scopus 로고
    • Fatal congenital thrombotic thrombocytopenic purpura with apparent ADAMTS13 inhibitor: in vitro inhibition of ADAMTS13 activity by hemoglobin
    • Studt JD, et al. Fatal congenital thrombotic thrombocytopenic purpura with apparent ADAMTS13 inhibitor: in vitro inhibition of ADAMTS13 activity by hemoglobin. Blood. 2005;105:542–544.
    • (2005) Blood , vol.105 , pp. 542-544
    • Studt, J.D.1
  • 204
    • 56749170891 scopus 로고    scopus 로고
    • Heme induces endothelial tissue factor expression: potential role in hemostatic activation in patients with hemolytic anemia
    • Setty BN, Betal SG, Zhang J, Stuart MJ. Heme induces endothelial tissue factor expression: potential role in hemostatic activation in patients with hemolytic anemia. J Thromb Haemost. 2008;6:2202–2209.
    • (2008) J Thromb Haemost , vol.6 , pp. 2202-2209
    • Setty, B.N.1    Betal, S.G.2    Zhang, J.3    Stuart, M.J.4
  • 205
    • 84925415904 scopus 로고    scopus 로고
    • Prevalence and gene characteristics of antibodies with cofactor-induced HIV-1 specificity
    • Lecerf M, Scheel T, Pashov AD, et al. Prevalence and gene characteristics of antibodies with cofactor-induced HIV-1 specificity. J Biol Chem. 2015;290:5203–5213.
    • (2015) J Biol Chem , vol.290 , pp. 5203-5213
    • Lecerf, M.1    Scheel, T.2    Pashov, A.D.3
  • 206
    • 0034695098 scopus 로고    scopus 로고
    • The biology of the receptor for advanced glycation end products and its ligands
    • Schmidt AM, Yan SD, Yan SF, Stern DM. The biology of the receptor for advanced glycation end products and its ligands. Biochim Biophys Acta. 2000;1498:99–111.
    • (2000) Biochim Biophys Acta , vol.1498 , pp. 99-111
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 207
    • 58549094758 scopus 로고    scopus 로고
    • The pathologic continuum of diabetic vascular disease
    • Orasanu G, Plutzky J. The pathologic continuum of diabetic vascular disease. J Am Coll Cardiol. 2009;53:S35–S42.
    • (2009) J Am Coll Cardiol , vol.53 , pp. S35-S42
    • Orasanu, G.1    Plutzky, J.2
  • 210
    • 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
  • 211
    • 78651410434 scopus 로고    scopus 로고
    • The development of atypical hemolytic uremic syndrome depends on complement C5
    • de Jorge EG, Macor P. Paixão-Cavalcante D. et al. The development of atypical hemolytic uremic syndrome depends on complement C5. J Am Soc Nephrol. 2011;22:137–145.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 137-145
    • de Jorge, E.G.1    Macor, P.2    Paixão-Cavalcante, D.3
  • 212
    • 35948959015 scopus 로고    scopus 로고
    • Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria
    • Rother RP, Rollins SA, Mojcik CF, Brodsky RA, Bell L. Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria. Nat Biotechnol. 2007;25:1256–1264.
    • (2007) Nat Biotechnol , vol.25 , pp. 1256-1264
    • Rother, R.P.1    Rollins, S.A.2    Mojcik, C.F.3    Brodsky, R.A.4    Bell, L.5
  • 213
    • 84927571620 scopus 로고    scopus 로고
    • Complement–tapping into new sites and effector systems
    • Kolev M, Le Friec G, Kemper C. Complement–tapping into new sites and effector systems. Nat Rev Immunol. 2014;14:811–820.
    • (2014) Nat Rev Immunol , vol.14 , pp. 811-820
    • Kolev, M.1    Le Friec, G.2    Kemper, C.3
  • 214
    • 33748904355 scopus 로고    scopus 로고
    • The complement inhibitor eculizumab in paroxysmal nocturnal hemoglobinuria
    • Hillmen P, et al. The complement inhibitor eculizumab in paroxysmal nocturnal hemoglobinuria. N Engl J Med. 2006;355:1233–1243.
    • (2006) N Engl J Med , vol.355 , pp. 1233-1243
    • Hillmen, P.1
  • 215
    • 84878589219 scopus 로고    scopus 로고
    • Terminal complement inhibitor eculizumab in atypical hemolytic-uremic syndrome
    • Legendre CM, Licht C, Muus P, et al. Terminal complement inhibitor eculizumab in atypical hemolytic-uremic syndrome. N Engl J Med. 2013;368:2169–2181.
    • (2013) N Engl J Med , vol.368 , pp. 2169-2181
    • Legendre, C.M.1    Licht, C.2    Muus, P.3
  • 216
    • 84948716605 scopus 로고    scopus 로고
    • Complement, a target for therapy in inflammatory and degenerative diseases
    • Morgan BP, Harris CL. Complement, a target for therapy in inflammatory and degenerative diseases. Nat Rev Drug Discovery. 2015;14:857–877.
    • (2015) Nat Rev Drug Discovery , vol.14 , pp. 857-877
    • Morgan, B.P.1    Harris, C.L.2
  • 217
    • 84927124445 scopus 로고    scopus 로고
    • The molecular and structural bases for the association of complement C3 mutations with atypical hemolytic uremic syndrome
    • Martinez-Barricarte R, Heurich M, López-Perrote A, et al. The molecular and structural bases for the association of complement C3 mutations with atypical hemolytic uremic syndrome. Mol Immunol. 2015;66:263–273.
    • (2015) Mol Immunol , vol.66 , pp. 263-273
    • Martinez-Barricarte, R.1    Heurich, M.2    López-Perrote, A.3
  • 219
    • 27144494245 scopus 로고    scopus 로고
    • Thrombus formation induced by antibodies to beta2-glycoprotein I is complement dependent and requires a priming factor
    • Fischetti F, et al. Thrombus formation induced by antibodies to beta2-glycoprotein I is complement dependent and requires a priming factor. Blood. 2005;106:2340–2346.
    • (2005) Blood , vol.106 , pp. 2340-2346
    • Fischetti, F.1
  • 221
    • 84880920024 scopus 로고    scopus 로고
    • Physiological and therapeutic complement regulators in kidney transplantation
    • Roumenina LT, Zuber J, Fremeaux-Bacchi V. Physiological and therapeutic complement regulators in kidney transplantation. Curr Opin Organ Transplant. 2013;18:421–429.
    • (2013) Curr Opin Organ Transplant , vol.18 , pp. 421-429
    • Roumenina, L.T.1    Zuber, J.2    Fremeaux-Bacchi, V.3
  • 222
    • 84875603640 scopus 로고    scopus 로고
    • Pathogenesis of antineutrophil cytoplasmic autoantibody-associated small-vessel vasculitis
    • Jennette JC, Falk RJ, Hu P, Xiao H. Pathogenesis of antineutrophil cytoplasmic autoantibody-associated small-vessel vasculitis. Annu Rev Pathol. 2013;8:139–160.
    • (2013) Annu Rev Pathol , vol.8 , pp. 139-160
    • Jennette, J.C.1    Falk, R.J.2    Hu, P.3    Xiao, H.4
  • 223
    • 33747681533 scopus 로고    scopus 로고
    • Cross-talk between the complement system and endothelial cells in physiologic conditions and in vascular diseases
    • Fischetti F, Tedesco F. Cross-talk between the complement system and endothelial cells in physiologic conditions and in vascular diseases. Autoimmunity. 2006;39:417–428.
    • (2006) Autoimmunity , vol.39 , pp. 417-428
    • Fischetti, F.1    Tedesco, F.2
  • 224
    • 84864485595 scopus 로고    scopus 로고
    • Brief report: induction of sustained remission in recurrent catastrophic antiphospholipid syndrome via inhibition of terminal complement with eculizumab
    • Shapira I, Andrade D, Allen SL, Salmon JE. Brief report: induction of sustained remission in recurrent catastrophic antiphospholipid syndrome via inhibition of terminal complement with eculizumab. Arthritis Rheum. 2012;64:2719–2723.
    • (2012) Arthritis Rheum , vol.64 , pp. 2719-2723
    • Shapira, I.1    Andrade, D.2    Allen, S.L.3    Salmon, J.E.4
  • 225
    • 84881372189 scopus 로고    scopus 로고
    • Eculizumab improves posttransplant thrombotic microangiopathy due to antiphospholipid syndrome recurrence but fails to prevent chronic vascular changes
    • Canaud G, Kamar N, Anglicheau D, et al. Eculizumab improves posttransplant thrombotic microangiopathy due to antiphospholipid syndrome recurrence but fails to prevent chronic vascular changes. Am J Transplant. 2013;13:2179–2185.
    • (2013) Am J Transplant , vol.13 , pp. 2179-2185
    • Canaud, G.1    Kamar, N.2    Anglicheau, D.3
  • 226
    • 0023278579 scopus 로고
    • HUS and TTP: variable expression of a single entity
    • Remuzzi G. HUS and TTP: variable expression of a single entity. Kidney Int. 1987;32:292–308.
    • (1987) Kidney Int , vol.32 , pp. 292-308
    • Remuzzi, G.1
  • 227
    • 84860474599 scopus 로고    scopus 로고
    • Complement activation in thrombotic thrombocytopenic purpura
    • Reti M, et al. Complement activation in thrombotic thrombocytopenic purpura. J Thromb Haemost. 2012;10:791–798.
    • (2012) J Thromb Haemost , vol.10 , pp. 791-798
    • Reti, M.1
  • 228
    • 84885339216 scopus 로고    scopus 로고
    • Complement activation and mortality during an acute episode of thrombotic thrombocytopenic purpura
    • Wu TC, et al. Complement activation and mortality during an acute episode of thrombotic thrombocytopenic purpura. J Thromb Haemost. 2013;11:1925–1927.
    • (2013) J Thromb Haemost , vol.11 , pp. 1925-1927
    • Wu, T.C.1
  • 229
    • 77950833468 scopus 로고    scopus 로고
    • Infection frequently triggers thrombotic microangiopathy in patients with preexisting risk factors: a single-institution experience
    • Douglas KW, Pollock KG, Young D, Catlow J, Green R. Infection frequently triggers thrombotic microangiopathy in patients with preexisting risk factors: a single-institution experience. J Clin Apheresis. 2010;25:47–53.
    • (2010) J Clin Apheresis , vol.25 , pp. 47-53
    • Douglas, K.W.1    Pollock, K.G.2    Young, D.3    Catlow, J.4    Green, R.5
  • 230
    • 0042703238 scopus 로고    scopus 로고
    • The association of pregnancy with thrombotic thrombocytopenic purpura-hemolytic uremic syndrome
    • George JN. The association of pregnancy with thrombotic thrombocytopenic purpura-hemolytic uremic syndrome. Curr Opin Hematol. 2003;10:339–344.
    • (2003) Curr Opin Hematol , vol.10 , pp. 339-344
    • George, J.N.1
  • 231
    • 84867997580 scopus 로고    scopus 로고
    • STEC-HUS, atypical HUS and TTP are all diseases of complement activation
    • Noris M, Mescia F, Remuzzi G. STEC-HUS, atypical HUS and TTP are all diseases of complement activation. Nat Rev Nephrol. 2012;8:622–633.
    • (2012) Nat Rev Nephrol , vol.8 , pp. 622-633
    • Noris, M.1    Mescia, F.2    Remuzzi, G.3
  • 232
    • 0032874149 scopus 로고    scopus 로고
    • Transcriptional expression of tissue factor pathway inhibitor, thrombomodulin and von Willebrand factor in normal human tissues
    • Bajaj MS, Kuppuswamy MN, Manepalli AN, Bajaj SP. Transcriptional expression of tissue factor pathway inhibitor, thrombomodulin and von Willebrand factor in normal human tissues. Thromb Haemost. 1999;82:1047–1052.
    • (1999) Thromb Haemost , vol.82 , pp. 1047-1052
    • Bajaj, M.S.1    Kuppuswamy, M.N.2    Manepalli, A.N.3    Bajaj, S.P.4
  • 233
    • 0023089665 scopus 로고
    • Endotoxin enhances tissue factor and suppresses thrombomodulin expression of human vascular endothelium in vitro
    • Moore KL, Andreoli SP, Esmon NL, Esmon CT, Bang NU. Endotoxin enhances tissue factor and suppresses thrombomodulin expression of human vascular endothelium in vitro. J Clin Invest. 1987;79:124–130.
    • (1987) J Clin Invest , vol.79 , pp. 124-130
    • Moore, K.L.1    Andreoli, S.P.2    Esmon, N.L.3    Esmon, C.T.4    Bang, N.U.5
  • 234
    • 0022601049 scopus 로고
    • Modulation of endothelial cell hemostatic properties by tumor necrosis factor
    • Nawroth PP, Stern DM. Modulation of endothelial cell hemostatic properties by tumor necrosis factor. J Exp Med. 1986;163:740–745.
    • (1986) J Exp Med , vol.163 , pp. 740-745
    • Nawroth, P.P.1    Stern, D.M.2
  • 235
    • 77956490806 scopus 로고    scopus 로고
    • Tissue factor up-regulation in proinflammatory conditions confers thrombin generation capacity to endothelial colony-forming cells without influencing non-coagulant properties in vitro
    • Cuccuini W, et al. Tissue factor up-regulation in proinflammatory conditions confers thrombin generation capacity to endothelial colony-forming cells without influencing non-coagulant properties in vitro. J Thromb Haemost. 2010;8:2042–2052.
    • (2010) J Thromb Haemost , vol.8 , pp. 2042-2052
    • Cuccuini, W.1
  • 236
    • 0027725139 scopus 로고
    • Expression of tissue factor, thrombomodulin, and E-selectin in baboons with lethal Escherichia coli sepsis
    • Drake TA, Cheng J, Chang A, Taylor FB Jr. Expression of tissue factor, thrombomodulin, and E-selectin in baboons with lethal Escherichia coli sepsis. Am J Pathol. 1993;142:1458–1470.
    • (1993) Am J Pathol , vol.142 , pp. 1458-1470
    • Drake, T.A.1    Cheng, J.2    Chang, A.3    Taylor, F.B.4
  • 237
    • 26244462687 scopus 로고    scopus 로고
    • Tissue factor-dependent coagulation is preferentially up-regulated within arterial branching areas in a baboon model of Escherichia coli sepsis
    • Lupu C, et al. Tissue factor-dependent coagulation is preferentially up-regulated within arterial branching areas in a baboon model of Escherichia coli sepsis. Am J Pathol. 2005;167:1161–1172.
    • (2005) Am J Pathol , vol.167 , pp. 1161-1172
    • Lupu, C.1
  • 238
    • 33745021587 scopus 로고    scopus 로고
    • Vascular endothelial growth factor is an important determinant of sepsis morbidity and mortality
    • Yano K, et al. Vascular endothelial growth factor is an important determinant of sepsis morbidity and mortality. J Exp Med. 2006;203:1447–1458.
    • (2006) J Exp Med , vol.203 , pp. 1447-1458
    • Yano, K.1
  • 239
    • 0022636799 scopus 로고
    • Thrombomodulin, an endothelial anticoagulant protein, is absent from the human brain
    • Ishii H, Salem HH, Bell CE, Laposata EA, Majerus PW. Thrombomodulin, an endothelial anticoagulant protein, is absent from the human brain. Blood. 1986;67:362–365.
    • (1986) Blood , vol.67 , pp. 362-365
    • Ishii, H.1    Salem, H.H.2    Bell, C.E.3    Laposata, E.A.4    Majerus, P.W.5
  • 240
    • 0034324926 scopus 로고    scopus 로고
    • Down-regulation of murine tissue factor pathway inhibitor mRNA by endotoxin and tumor necrosis factor-alpha in vitro and in vivo
    • Shimokawa T, Yamamoto K, Kojima T, Saito H. Down-regulation of murine tissue factor pathway inhibitor mRNA by endotoxin and tumor necrosis factor-alpha in vitro and in vivo. Thromb Res. 2000;100:211–221.
    • (2000) Thromb Res , vol.100 , pp. 211-221
    • Shimokawa, T.1    Yamamoto, K.2    Kojima, T.3    Saito, H.4
  • 241
    • 0030776168 scopus 로고    scopus 로고
    • Human protein C receptor is present primarily on endothelium of large blood vessels: implications for the control of the protein C pathway
    • Laszik Z, Mitro A, Taylor FB Jr, Ferrell G, Esmon CT. Human protein C receptor is present primarily on endothelium of large blood vessels: implications for the control of the protein C pathway. Circulation. 1997;96:3633–3640.
    • (1997) Circulation , vol.96 , pp. 3633-3640
    • Laszik, Z.1    Mitro, A.2    Taylor, F.B.3    Ferrell, G.4    Esmon, C.T.5
  • 242
    • 0034161458 scopus 로고    scopus 로고
    • Endotoxin and thrombin elevate rodent endothelial cell protein C receptor mRNA levels and increase receptor shedding in vivo
    • Gu JM, Katsuura Y, Ferrell GL, Grammas P, Esmon CT. Endotoxin and thrombin elevate rodent endothelial cell protein C receptor mRNA levels and increase receptor shedding in vivo. Blood. 2000;95:1687–1693.
    • (2000) Blood , vol.95 , pp. 1687-1693
    • Gu, J.M.1    Katsuura, Y.2    Ferrell, G.L.3    Grammas, P.4    Esmon, C.T.5
  • 243
    • 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 RA, van der Ark AA, Buurman WA, van Es LA, Daha MR. 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
  • 244
    • 0030887335 scopus 로고    scopus 로고
    • TNF-alpha regulation of C3 gene expression and protein biosynthesis in rat glomerular endothelial cells
    • Sheerin NS, Zhou W, Adler S, Sacks SH. TNF-alpha regulation of C3 gene expression and protein biosynthesis in rat glomerular endothelial cells. Kidney Int. 1997;51:703–710.
    • (1997) Kidney Int , vol.51 , pp. 703-710
    • Sheerin, N.S.1    Zhou, W.2    Adler, S.3    Sacks, S.H.4
  • 245
    • 84860773873 scopus 로고    scopus 로고
    • Human leukocyte antigen-specific antibodies and gamma-interferon stimulate human microvascular and glomerular endothelial cells to produce complement factor C4
    • Hamer R, Molostvov G, Lowe D, et al. Human leukocyte antigen-specific antibodies and gamma-interferon stimulate human microvascular and glomerular endothelial cells to produce complement factor C4. Transplantation. 2012;93:867–873.
    • (2012) Transplantation , vol.93 , pp. 867-873
    • Hamer, R.1    Molostvov, G.2    Lowe, D.3
  • 246
    • 0034869769 scopus 로고    scopus 로고
    • Complement factor I is upregulated in rat hepatocytes by interleukin-6 but not by interferon-gamma, interleukin-1beta, or tumor necrosis factor-alpha
    • Schlaf G, Demberg T, Koleva M, Jungermann K, Gotze O. Complement factor I is upregulated in rat hepatocytes by interleukin-6 but not by interferon-gamma, interleukin-1beta, or tumor necrosis factor-alpha. Biol Chem. 2001;382:1089–1094.
    • (2001) Biol Chem , vol.382 , pp. 1089-1094
    • Schlaf, G.1    Demberg, T.2    Koleva, M.3    Jungermann, K.4    Gotze, O.5


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