메뉴 건너뛰기




Volumn 65, Issue 3, 2007, Pages 230-239

Iron ions and haeme modulate the binding properties of complement subcomponent C1q and of immunoglobulins

Author keywords

[No Author keywords available]

Indexed keywords

C REACTIVE PROTEIN; COMPLEMENT COMPONENT C1Q; IMMUNOGLOBULIN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; RHEUMATOID FACTOR;

EID: 33847058366     PISSN: 03009475     EISSN: 13653083     Source Type: Journal    
DOI: 10.1111/j.1365-3083.2006.01893.x     Document Type: Article
Times cited : (33)

References (74)
  • 1
    • 0026657624 scopus 로고
    • Human antibody effector function
    • Burton DR, Woof JM. Human antibody effector function. Adv Immunol 1992;51:1-84.
    • (1992) Adv Immunol , vol.51 , pp. 1-84
    • Burton, D.R.1    Woof, J.M.2
  • 2
    • 0034046181 scopus 로고    scopus 로고
    • Regulation of antibody responses via antibodies, complement, and Fc receptors
    • Heyman B. Regulation of antibody responses via antibodies, complement, and Fc receptors. Annu Rev Immunol 2000;18:709-37.
    • (2000) Annu Rev Immunol , vol.18 , pp. 709-737
    • Heyman, B.1
  • 3
    • 0035810399 scopus 로고    scopus 로고
    • Complement
    • Walport MJ. Complement. N Engl J Med 2001;344:1058-66.
    • (2001) N Engl J Med , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 4
    • 0035849176 scopus 로고    scopus 로고
    • Complement at the interface between the inate and adaptive immunity
    • Walport MJ. Complement at the interface between the inate and adaptive immunity. N Engl J Med 2001;344:1140-4.
    • (2001) N Engl J Med , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 5
    • 0030133352 scopus 로고    scopus 로고
    • Blood radicals: Reactive nitrogen species, reactive oxygen species, transition metal ions, and the vascular system
    • Darley-Usmar V, Halliwell B. Blood radicals: reactive nitrogen species, reactive oxygen species, transition metal ions, and the vascular system. Pharm Res 1996;13:649-62.
    • (1996) Pharm Res , vol.13 , pp. 649-662
    • Darley-Usmar, V.1    Halliwell, B.2
  • 6
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan C. Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006;6:173-82.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 7
    • 0018093401 scopus 로고
    • Oxygen radicals mediate endothelial cell damage by complement-stimulated granulocytes. An in vitro model of immune vascular damage
    • Sacks T, Moldow CF, Craddock PR, Bowers TK, Jacob HS. Oxygen radicals mediate endothelial cell damage by complement-stimulated granulocytes. An in vitro model of immune vascular damage. J Clin Invest 1978;61:1161-7.
    • (1978) J Clin Invest , vol.61 , pp. 1161-1167
    • Sacks, T.1    Moldow, C.F.2    Craddock, P.R.3    Bowers, T.K.4    Jacob, H.S.5
  • 8
    • 0023713495 scopus 로고
    • Activated neutrophils release mediators that may contribute to myocardial injury and dysfunction associated with ischemia and reperfusion
    • Mullane KM, Westlin W, Kraemer R. Activated neutrophils release mediators that may contribute to myocardial injury and dysfunction associated with ischemia and reperfusion. Ann N Y Acad Sci 1988;524:103-21.
    • (1988) Ann N Y Acad Sci , vol.524 , pp. 103-121
    • Mullane, K.M.1    Westlin, W.2    Kraemer, R.3
  • 9
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ. Tissue destruction by neutrophils. N Engl J Med 1989;320:365-76.
    • (1989) N Engl J Med , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 10
  • 11
    • 0026078464 scopus 로고
    • Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: Effect of pH and iron saturation
    • Brieland JK, Fantone JC. Ferrous iron release from transferrin by human neutrophil-derived superoxide anion: effect of pH and iron saturation. Arch Biochem Biophys 1991;284:78-83.
    • (1991) Arch Biochem Biophys , vol.284 , pp. 78-83
    • Brieland, J.K.1    Fantone, J.C.2
  • 12
    • 0026526023 scopus 로고
    • Ferritin as a source of iron for oxidative damage
    • Reif DW. Ferritin as a source of iron for oxidative damage. Free Radic Biol Med 1992;12:417-27.
    • (1992) Free Radic Biol Med , vol.12 , pp. 417-427
    • Reif, D.W.1
  • 13
    • 0029588565 scopus 로고
    • Ferritin as a source of iron and protection from iron-induced toxicities
    • Aust SD. Ferritin as a source of iron and protection from iron-induced toxicities. Toxicol Lett 1995;82-83:941-4.
    • (1995) Toxicol Lett
    • Aust, S.D.1
  • 15
    • 0014360531 scopus 로고
    • Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard U, Javid J, Liem HH, Hanstein A, Hanna M. Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 1968;32:811-5.
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5
  • 16
    • 0014713324 scopus 로고
    • Disposal of plasma heme in normal man and patients with intravascular hemolysis
    • Sears DA. Disposal of plasma heme in normal man and patients with intravascular hemolysis. J Clin Invest 1970;49:5-14.
    • (1970) J Clin Invest , vol.49 , pp. 5-14
    • Sears, D.A.1
  • 17
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • Kumar S, Bandyopadhyay U. Free heme toxicity and its detoxification systems in human. Toxicol Lett 2005;157:175-88.
    • (2005) Toxicol Lett , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 18
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B, Gutteridge JM. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 1984;219:1-14.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 20
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties
    • Ryter SW, Tyrrell RM. The heme synthesis and degradation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties. Free Radic Biol Med 2000;28:289-309.
    • (2000) Free Radic Biol Med , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 22
    • 0032767113 scopus 로고    scopus 로고
    • Normal human immunoglobulin suppresses experimental myasthenia gravis in SCID mice
    • Vassilev T, Yamamoto M, Aissaoui A et al. Normal human immunoglobulin suppresses experimental myasthenia gravis in SCID mice. Eur J Immunol 1999;29:2436-42.
    • (1999) Eur J Immunol , vol.29 , pp. 2436-2442
    • Vassilev, T.1    Yamamoto, M.2    Aissaoui, A.3
  • 23
    • 0027504398 scopus 로고
    • Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura
    • Debre M, Bonnet MC, Fridman WH et al. Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura. Lancet 1993;342:945-9.
    • (1993) Lancet , vol.342 , pp. 945-949
    • Debre, M.1    Bonnet, M.C.2    Fridman, W.H.3
  • 24
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer K, Imlay JA. Superoxide accelerates DNA damage by elevating free-iron levels. Proc Natl Acad Sci U S A 1996;93:13635-40.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 25
    • 0033535941 scopus 로고    scopus 로고
    • Ultraviolet A radiation induces immediate release of iron in human primary skin fibroblasts: The role of ferritin
    • Pourzand C, Watkin RD, Brown JE, Tyrrell RM. Ultraviolet A radiation induces immediate release of iron in human primary skin fibroblasts: the role of ferritin. Proc Natl Acad Sci U S A 1999;96:6751-6.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6751-6756
    • Pourzand, C.1    Watkin, R.D.2    Brown, J.E.3    Tyrrell, R.M.4
  • 26
    • 0346458616 scopus 로고    scopus 로고
    • Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: Role of mitochondrial respiratory complexes and heat shock proteins
    • Ramachandran A, Ceaser E, Darley-Usmar VM. Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes and heat shock proteins. Proc Natl Acad Sci U S A 2004;101:384-9.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 384-389
    • Ramachandran, A.1    Ceaser, E.2    Darley-Usmar, V.M.3
  • 27
    • 0036749238 scopus 로고    scopus 로고
    • Recent progress in the understanding of the structure-function relationships of the globular head regions of C1q
    • Kishore U, Kojouharova MS, Reid KB. Recent progress in the understanding of the structure-function relationships of the globular head regions of C1q. Immunobiology 2002;205:355-64.
    • (2002) Immunobiology , vol.205 , pp. 355-364
    • Kishore, U.1    Kojouharova, M.S.2    Reid, K.B.3
  • 28
    • 27544443735 scopus 로고    scopus 로고
    • Role of Ca(2+) in the Electrostatic Stability and the Functional Activity of the Globular Domain of Human C1q
    • Roumenina LT, Kantardjiev AA, Atanasov BP et al. Role of Ca(2+) in the Electrostatic Stability and the Functional Activity of the Globular Domain of Human C1q. Biochemistry 2005;44:14097-109.
    • (2005) Biochemistry , vol.44 , pp. 14097-14109
    • Roumenina, L.T.1    Kantardjiev, A.A.2    Atanasov, B.P.3
  • 29
    • 0025304360 scopus 로고
    • Carbodiimide crosslinking of human C1q and rabbit IgG
    • Wines BD, Easterbrook-Smith SB. Carbodiimide crosslinking of human C1q and rabbit IgG. Mol Immunol 1990;27:221-6.
    • (1990) Mol Immunol , vol.27 , pp. 221-226
    • Wines, B.D.1    Easterbrook-Smith, S.B.2
  • 30
    • 10644271456 scopus 로고    scopus 로고
    • Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: In vivo implications
    • Suresh MV, Singh SK, Agrawal A. Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: in vivo implications. J Biol Chem 2004;279:52552-7.
    • (2004) J Biol Chem , vol.279 , pp. 52552-52557
    • Suresh, M.V.1    Singh, S.K.2    Agrawal, A.3
  • 31
    • 33645577856 scopus 로고    scopus 로고
    • Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: A mutational analyses using recombinant globular regions of C1q A, B and C chains
    • Roumenina LT, Rouseva M, Zlatarova A et al. Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: a mutational analyses using recombinant globular regions of C1q A, B and C chains. Biochemistry 2006;45:4093-104.
    • (2006) Biochemistry , vol.45 , pp. 4093-4104
    • Roumenina, L.T.1    Rouseva, M.2    Zlatarova, A.3
  • 32
    • 0034656371 scopus 로고    scopus 로고
    • Acidic pH amplifies iron-mediated lipid peroxidation in cells
    • Schafer FQ, Buettner GR. Acidic pH amplifies iron-mediated lipid peroxidation in cells. Free Radic Biol Med 2000;28:1175-81.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1175-1181
    • Schafer, F.Q.1    Buettner, G.R.2
  • 33
    • 0033947551 scopus 로고    scopus 로고
    • C1q: Structure, function, and receptors
    • Kishore U, Reid KB. C1q: structure, function, and receptors. Immunopharmacology 2000;49:159-70.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 34
    • 0032869793 scopus 로고    scopus 로고
    • In stroke, complement will get you nowhere
    • del Zoppo GJ. In stroke, complement will get you nowhere. Nat Med 1999;5:995-6.
    • (1999) Nat Med , vol.5 , pp. 995-996
    • del Zoppo, G.J.1
  • 35
    • 0035041301 scopus 로고    scopus 로고
    • Innate immune responses to transplants: A significant variable with cadaver donors
    • Baldwin WM III, Larsen CP, Fairchild RL. Innate immune responses to transplants: a significant variable with cadaver donors. Immunity 2001;14:369-76.
    • (2001) Immunity , vol.14 , pp. 369-376
    • Baldwin III, W.M.1    Larsen, C.P.2    Fairchild, R.L.3
  • 36
    • 0141991166 scopus 로고    scopus 로고
    • Yin and Yang: Complement activation and regulation in Alzheimer's disease
    • Shen Y, Meri S. Yin and Yang: complement activation and regulation in Alzheimer's disease. Prog Neurobiol 2003;70:463-72.
    • (2003) Prog Neurobiol , vol.70 , pp. 463-472
    • Shen, Y.1    Meri, S.2
  • 37
    • 2542505506 scopus 로고    scopus 로고
    • The role of complement in the development of systemic lupus erythematosus
    • Manderson AP, Botto M, Walport MJ. The role of complement in the development of systemic lupus erythematosus. Annu Rev Immunol 2004;22:431-56.
    • (2004) Annu Rev Immunol , vol.22 , pp. 431-456
    • Manderson, A.P.1    Botto, M.2    Walport, M.J.3
  • 38
    • 2442700517 scopus 로고    scopus 로고
    • Initiation of complement activation following oxidative stress. In vitro and in vivo observations
    • Hart ML, Walsh MC, Stahl GL. Initiation of complement activation following oxidative stress. In vitro and in vivo observations. Mol Immunol 2004;41:165-71.
    • (2004) Mol Immunol , vol.41 , pp. 165-171
    • Hart, M.L.1    Walsh, M.C.2    Stahl, G.L.3
  • 41
    • 33646366683 scopus 로고    scopus 로고
    • Targeting C-reactive protein for the treatment of cardiovascular disease
    • Pepys MB, Hirschfield GM, Tennent GA et al. Targeting C-reactive protein for the treatment of cardiovascular disease. Nature 2006;440:1217-21.
    • (2006) Nature , vol.440 , pp. 1217-1221
    • Pepys, M.B.1    Hirschfield, G.M.2    Tennent, G.A.3
  • 42
    • 0031965781 scopus 로고    scopus 로고
    • Hemin binding and oxidation of lipoproteins in serum: Mechanisms and effect on the interaction of LDL with human macrophages
    • Camejo G, Halberg C, Manschik-Lundin A et al. Hemin binding and oxidation of lipoproteins in serum: mechanisms and effect on the interaction of LDL with human macrophages. J Lipid Res 1998;39:755-66.
    • (1998) J Lipid Res , vol.39 , pp. 755-766
    • Camejo, G.1    Halberg, C.2    Manschik-Lundin, A.3
  • 43
    • 0036682472 scopus 로고    scopus 로고
    • Pro-oxidant and cytotoxic effects of circulating heme
    • Jeney V, Balla J, Yachie A et al. Pro-oxidant and cytotoxic effects of circulating heme. Blood 2002;100:879-87.
    • (2002) Blood , vol.100 , pp. 879-887
    • Jeney, V.1    Balla, J.2    Yachie, A.3
  • 44
    • 0037794084 scopus 로고    scopus 로고
    • Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron
    • Grinshtein N, Bamm VV, Tsemakhovich VA, Shaklai N. Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron. Biochemistry 2003;42:6977-85.
    • (2003) Biochemistry , vol.42 , pp. 6977-6985
    • Grinshtein, N.1    Bamm, V.V.2    Tsemakhovich, V.A.3    Shaklai, N.4
  • 45
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft RL, Mueller GC. Hemin-mediated oxidative degradation of proteins. J Biol Chem 1984;259:301-5.
    • (1984) J Biol Chem , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 46
    • 0024574001 scopus 로고
    • Oxidative effects of heme and porphyrins on proteins and lipids
    • Vincent SH. Oxidative effects of heme and porphyrins on proteins and lipids. Semin Hematol 1989;26:105-13.
    • (1989) Semin Hematol , vol.26 , pp. 105-113
    • Vincent, S.H.1
  • 47
    • 0030023384 scopus 로고    scopus 로고
    • Hemoglobin induced apolipoprotein B crosslinking in low-density lipoprotein peroxidation
    • Miller YI, Felikman Y, Shaklai N. Hemoglobin induced apolipoprotein B crosslinking in low-density lipoprotein peroxidation. Arch Biochem Biophys 1996;326:252-60.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 252-260
    • Miller, Y.I.1    Felikman, Y.2    Shaklai, N.3
  • 48
    • 0033516656 scopus 로고    scopus 로고
    • Oxidative cross-linking of ApoB100 and hemoglobin results in low density lipoprotein modification in blood. Relevance to atherogenesis caused by hemodialysis
    • Ziouzenkova O, Asatryan L, Akmal M et al. Oxidative cross-linking of ApoB100 and hemoglobin results in low density lipoprotein modification in blood. Relevance to atherogenesis caused by hemodialysis. J Biol Chem 1999;274:18916-24.
    • (1999) J Biol Chem , vol.274 , pp. 18916-18924
    • Ziouzenkova, O.1    Asatryan, L.2    Akmal, M.3
  • 49
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • Aft RL, Mueller GC. Hemin-mediated DNA strand scission. J Biol Chem 1983;258:12069-72.
    • (1983) J Biol Chem , vol.258 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 50
    • 0036790992 scopus 로고    scopus 로고
    • Protein nitration is mediated by heme and free metals through Fentontype chemistry: An alternative to the NO/O2- reaction
    • Thomas DD, Espey MG, Vitek MP, Miranda KM, Wink DA. Protein nitration is mediated by heme and free metals through Fentontype chemistry: an alternative to the NO/O2- reaction. Proc Natl Acad Sci U S A 2002;99:12691-6.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12691-12696
    • Thomas, D.D.1    Espey, M.G.2    Vitek, M.P.3    Miranda, K.M.4    Wink, D.A.5
  • 51
  • 52
    • 0035885926 scopus 로고    scopus 로고
    • Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase
    • Wagener FA, Eggert A, Boerman OC et al. Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase. Blood 2001;98:1802-11.
    • (2001) Blood , vol.98 , pp. 1802-1811
    • Wagener, F.A.1    Eggert, A.2    Boerman, O.C.3
  • 54
    • 0041967387 scopus 로고    scopus 로고
    • Different faces of the heme-heme oxygenase system in inflammation
    • Wagener FA, Volk HD, Willis D et al. Different faces of the heme-heme oxygenase system in inflammation. Pharmacol Rev 2003;55:551-71.
    • (2003) Pharmacol Rev , vol.55 , pp. 551-571
    • Wagener, F.A.1    Volk, H.D.2    Willis, D.3
  • 55
    • 3242741986 scopus 로고    scopus 로고
    • Heme inhibits human neutrophil apoptosis: Involvement of phosphoinositide 3-kinase, MAPK, and NF-kappaB
    • Arruda MA, Rossi AG, de Freitas MS, Barja-Fidalgo C, Graca-Souza AV. Heme inhibits human neutrophil apoptosis: involvement of phosphoinositide 3-kinase, MAPK, and NF-kappaB. J Immunol 2004;173:2023-30.
    • (2004) J Immunol , vol.173 , pp. 2023-2030
    • Arruda, M.A.1    Rossi, A.G.2    de Freitas, M.S.3    Barja-Fidalgo, C.4    Graca-Souza, A.V.5
  • 56
    • 1242318747 scopus 로고    scopus 로고
    • Localization of the ligand binding sites on the human C1q globular region using recombinant globular head fragments and single-chain antibodies
    • Kojouharova MS, Tsacheva I, Tchorbadjieva M, Reid KB, Kishore U. Localization of the ligand binding sites on the human C1q globular region using recombinant globular head fragments and single-chain antibodies. Biochim Biophys Acta 2003;1652:64-74.
    • (2003) Biochim Biophys Acta , vol.1652 , pp. 64-74
    • Kojouharova, M.S.1    Tsacheva, I.2    Tchorbadjieva, M.3    Reid, K.B.4    Kishore, U.5
  • 58
    • 0036340622 scopus 로고    scopus 로고
    • Rheumatoid factors: Host resistance or autoimmunity?
    • Newkirk MM. Rheumatoid factors: host resistance or autoimmunity? Clin Immunol 2002;104:1-13.
    • (2002) Clin Immunol , vol.104 , pp. 1-13
    • Newkirk, M.M.1
  • 62
    • 0037073888 scopus 로고    scopus 로고
    • Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation
    • Wentworth P Jr, McDunn JE, Wentworth AD et al. Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation. Science 2002;298:2195-9.
    • (2002) Science , vol.298 , pp. 2195-2199
    • Wentworth Jr, P.1    McDunn, J.E.2    Wentworth, A.D.3
  • 63
    • 2342617587 scopus 로고    scopus 로고
    • The antibody-catalyzed water oxidation pathway - a new chemical arm to immune defense?
    • Nieva J, Wentworth P. The antibody-catalyzed water oxidation pathway - a new chemical arm to immune defense? Trends Biochem Sci 2004;29:274-8.
    • (2004) Trends Biochem Sci , vol.29 , pp. 274-278
    • Nieva, J.1    Wentworth, P.2
  • 64
    • 0032213581 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of immunoglobulin G impairs Fc receptor-mediated binding to macrophages
    • Margiloff L, Chaplia L, Chow A, Singhal PC, Mattana J. Metal-catalyzed oxidation of immunoglobulin G impairs Fc receptor-mediated binding to macrophages. Free Radic Biol Med 1998;25:780-5.
    • (1998) Free Radic Biol Med , vol.25 , pp. 780-785
    • Margiloff, L.1    Chaplia, L.2    Chow, A.3    Singhal, P.C.4    Mattana, J.5
  • 65
    • 0034544448 scopus 로고    scopus 로고
    • Inflammatory properties of IgG modified by oxygen radicals and peroxynitrite
    • Uesugi M, Yoshida K, Jasin HE. Inflammatory properties of IgG modified by oxygen radicals and peroxynitrite. J Immunol 2000;165:6532-7.
    • (2000) J Immunol , vol.165 , pp. 6532-6537
    • Uesugi, M.1    Yoshida, K.2    Jasin, H.E.3
  • 66
    • 0030591314 scopus 로고    scopus 로고
    • The C1q binding activity of IgG is modified in vitro by reactive oxygen species: Implications for rheumatoid arthritis
    • Griffiths HR, Lunec J. The C1q binding activity of IgG is modified in vitro by reactive oxygen species: implications for rheumatoid arthritis. FEBS Lett 1996;388:161-4.
    • (1996) FEBS Lett , vol.388 , pp. 161-164
    • Griffiths, H.R.1    Lunec, J.2
  • 67
    • 0026024172 scopus 로고
    • Effects of reactive oxygen species on immunoglobulin G function
    • Griffiths HR, Lunec J. Effects of reactive oxygen species on immunoglobulin G function. Mol Aspects Med 1991;12:107-19.
    • (1991) Mol Aspects Med , vol.12 , pp. 107-119
    • Griffiths, H.R.1    Lunec, J.2
  • 68
    • 85044703884 scopus 로고    scopus 로고
    • Mechanisms for increasing the activity of polyreactive immunoglobulins in vivo
    • Bobrovnik SA. Mechanisms for increasing the activity of polyreactive immunoglobulins in vivo. Ukr Biokhim Zh 1999;71:129-35.
    • (1999) Ukr Biokhim Zh , vol.71 , pp. 129-135
    • Bobrovnik, S.A.1
  • 69
    • 7044245628 scopus 로고    scopus 로고
    • The appearance and disappearance of antiphospholipid autoantibodies subsequent to oxidation-reduction reactions
    • McIntyre JA. The appearance and disappearance of antiphospholipid autoantibodies subsequent to oxidation-reduction reactions. Thromb Res 2004;114:579-87.
    • (2004) Thromb Res , vol.114 , pp. 579-587
    • McIntyre, J.A.1
  • 71
    • 28744455410 scopus 로고    scopus 로고
    • Redox-reactive autoantibodies: Detection and physiological relevance
    • McIntyre JA, Wagenknecht DR, Faulk WP. Redox-reactive autoantibodies: detection and physiological relevance. Autoimmun Rev 2006;5:76-83.
    • (2006) Autoimmun Rev , vol.5 , pp. 76-83
    • McIntyre, J.A.1    Wagenknecht, D.R.2    Faulk, W.P.3
  • 72
    • 0019955727 scopus 로고
    • An immunohistological analysis of lymphocyte subpopulations and their microenvironment in the synovial membranes of patients with rheumatoid arthritis using monoclonal antibodies
    • Duke O, Panayi GS, Janossy G, Poulter LW. An immunohistological analysis of lymphocyte subpopulations and their microenvironment in the synovial membranes of patients with rheumatoid arthritis using monoclonal antibodies. Clin Exp Immunol 1982;49:22-30.
    • (1982) Clin Exp Immunol , vol.49 , pp. 22-30
    • Duke, O.1    Panayi, G.S.2    Janossy, G.3    Poulter, L.W.4
  • 73
    • 0021339874 scopus 로고
    • Immunohistologic characterization of synovial membrane lymphocytes in rheumatoid arthritis
    • Young CL, Adamson TC III, Vaughan JH, Fox RI. Immunohistologic characterization of synovial membrane lymphocytes in rheumatoid arthritis. Arthritis Rheum 1984;27:32-9.
    • (1984) Arthritis Rheum , vol.27 , pp. 32-39
    • Young, C.L.1    Adamson III, T.C.2    Vaughan, J.H.3    Fox, R.I.4
  • 74
    • 0037144519 scopus 로고    scopus 로고
    • Evolution of autoantibody responses via somatic hypermutation outside of germinal centers
    • William J, Euler C, Christensen S, Shlomchik MJ. Evolution of autoantibody responses via somatic hypermutation outside of germinal centers. Science 2002;297:2066-72.
    • (2002) Science , vol.297 , pp. 2066-2072
    • William, J.1    Euler, C.2    Christensen, S.3    Shlomchik, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.