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Volumn 34, Issue 1, 2004, Pages 221-230

Complement C1q regulates LPS-induced cytokine production in bone marrow-derived dendritic cells

Author keywords

Cytokines; Dendritic cells; Lipopolysaccharide

Indexed keywords

CD40 ANTIGEN; CD86 ANTIGEN; CELL SURFACE RECEPTOR; COLLAGEN; COMPLEMENT COMPONENT C1Q; CYTOKINE; DIFFERENTIATION ANTIGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOGLOBULIN RECEPTOR; INTERLEUKIN 12; INTERLEUKIN 12P40; INTERLEUKIN-12 SUBUNIT P40; LIPOPOLYSACCHARIDE; LY ANTIGEN; LY96 PROTEIN, MOUSE; MEMBRANE PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MYELOID DIFFERENTIATION FACTOR 88; OLIGODEOXYNUCLEOTIDE; PROTEIN P40; PROTEIN SUBUNIT; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 9144224761     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200324026     Document Type: Article
Times cited : (66)

References (56)
  • 1
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: Critical proteins linking innate and acquired immunity
    • Akira, S., Takeda, K. and Kaisho, T., Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2001. 8: 675-680.
    • (2001) Nat. Immunol. , vol.8 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisho, T.3
  • 2
    • 0037070113 scopus 로고    scopus 로고
    • Toll-like receptors as adjuvant receptors
    • 1589
    • Kaisho, T. and Akira, S., Toll-like receptors as adjuvant receptors. Biochim. Biophys. Acta. 2002. 1589: 1-13.
    • (2002) Biochim. Biophys. Acta , pp. 1-13
    • Kaisho, T.1    Akira, S.2
  • 3
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • Aderem, A. and Ulevitch, R. J., Toll-like receptors in the induction of the innate immune response. Nature 2000. 406: 782-787.
    • (2000) Nature , vol.406 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 4
    • 0033975869 scopus 로고    scopus 로고
    • Innate immune recognition: Mechanism and pathways
    • Medzhitov, R. and Janeway, C. Jr., Innate immune recognition: mechanism and pathways. Immunol. Rev. 2000. 173: 89-97.
    • (2000) Immunol. Rev. , vol.173 , pp. 89-97
    • Medzhitov, R.1    Janeway Jr., C.2
  • 5
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J. and Steinman, R. M., Dendritic cells and the control of immunity. Nature 1998. 392: 245-252.
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 6
    • 0035903288 scopus 로고    scopus 로고
    • Subsets of human dendritic cell precursors express different Toll-like receptors and respond to different microbial antigens
    • Kadowaki, N., Ho, S., Antonenko, S., Malefyt, R. W., Kastelein, R. A., Bazan, F. and Liu, Y.-J., Subsets of human dendritic cell precursors express different Toll-like receptors and respond to different microbial antigens. J. Exp. Med. 2001. 194: 863-869.
    • (2001) J. Exp. Med. , vol.194 , pp. 863-869
    • Kadowaki, N.1    Ho, S.2    Antonenko, S.3    Malefyt, R.W.4    Kastelein, R.A.5    Bazan, F.6    Liu, Y.-J.7
  • 9
    • 0343114462 scopus 로고    scopus 로고
    • Cell type-specific activation of mitogen-activated protein kinases by CpG-DNA controls interleukin-12 release from antigen-presenting cells
    • Hacker, H., Mischak, H., Hacker, G., Eser, S., Prenzel, N., Ullrich, A. and Wagner, H., Cell type-specific activation of mitogen-activated protein kinases by CpG-DNA controls interleukin-12 release from antigen-presenting cells. EMBO J. 1999. 18: 6973-6982.
    • (1999) EMBO J. , vol.18 , pp. 6973-6982
    • Hacker, H.1    Mischak, H.2    Hacker, G.3    Eser, S.4    Prenzel, N.5    Ullrich, A.6    Wagner, H.7
  • 10
    • 0033040509 scopus 로고    scopus 로고
    • Membrane receptors for soluble defense collagens
    • Tenner, A. J., Membrane receptors for soluble defense collagens. Curr. Opin. Immunol. 1999. 11: 34-41.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 34-41
    • Tenner, A.J.1
  • 12
    • 0031569975 scopus 로고    scopus 로고
    • C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: Complement deficiency and systemic lupus erythematosus revisited
    • Korb, L. C. and Ahearn, J. M., C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: complement deficiency and systemic lupus erythematosus revisited. J. Immunol. 1997. 158: 4525-4528.
    • (1997) J. Immunol. , vol.158 , pp. 4525-4528
    • Korb, L.C.1    Ahearn, J.M.2
  • 14
    • 0023111156 scopus 로고
    • Modulation of FcR function by complement: Subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages
    • Bobak, D. A., Gaither, T. A., Frank, M. M. and Tenner, A. J., Modulation of FcR function by complement: subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages. J. Immunol. 1987. 138: 1150-1156.
    • (1987) J. Immunol. , vol.138 , pp. 1150-1156
    • Bobak, D.A.1    Gaither, T.A.2    Frank, M.M.3    Tenner, A.J.4
  • 15
    • 0024273027 scopus 로고
    • C1q acts synergistically with phorbol dibutyrate to activate CR1-mediated phagocytosis by human mononuclear phagocytes
    • Bobak, D. A., Frank, M. M. and Tenner, A. J., C1q acts synergistically with phorbol dibutyrate to activate CR1-mediated phagocytosis by human mononuclear phagocytes. Eur. J. Immunol. 1988. 18: 2001-2007.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 2001-2007
    • Bobak, D.A.1    Frank, M.M.2    Tenner, A.J.3
  • 16
    • 0029059577 scopus 로고
    • C1q triggers neutrophil superoxide production by a unique CD18-dependent mechanism
    • Goodman, E. B., Anderson, D. C. and Tenner, A. J., C1q triggers neutrophil superoxide production by a unique CD18-dependent mechanism. J. Leukoc. Biol. 1995. 58: 168-176.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 168-176
    • Goodman, E.B.1    Anderson, D.C.2    Tenner, A.J.3
  • 17
    • 0031697215 scopus 로고    scopus 로고
    • C1q deficiencies and C1q in autoimmunity
    • Walport, M. J., Davies, K. A. and Botto, M., C1q deficiencies and C1q in autoimmunity. Immunobiol. 1998. 199: 265-285.
    • (1998) Immunobiol. , vol.199 , pp. 265-285
    • Walport, M.J.1    Davies, K.A.2    Botto, M.3
  • 19
    • 0034284038 scopus 로고    scopus 로고
    • Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages
    • Yokota, T., Oritani, K., Takahashi, I., Ishikawa, J., Matsuyama, A., Ouchi, N., Kihara, S., Funahashi, T., Tenner, A. J., Tomiyama, Y. and Matsuzawa, Y., Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood 2000. 96: 1723-1732.
    • (2000) Blood , vol.96 , pp. 1723-1732
    • Yokota, T.1    Oritani, K.2    Takahashi, I.3    Ishikawa, J.4    Matsuyama, A.5    Ouchi, N.6    Kihara, S.7    Funahashi, T.8    Tenner, A.J.9    Tomiyama, Y.10    Matsuzawa, Y.11
  • 20
    • 0028894798 scopus 로고
    • Activation of human monocytes by streptococcal rhamnose glucose polymers is mediated by CD14 antigen, and mannan binding protein inhibits TNF-α release
    • Soell, M., Lett, E., Holveck, F., Scholler, M., Wachsmann, D. and Klein, J. P., Activation of human monocytes by streptococcal rhamnose glucose polymers is mediated by CD14 antigen, and mannan binding protein inhibits TNF-α release. J. Immunol. 1995. 154: 851-860.
    • (1995) J. Immunol. , vol.154 , pp. 851-860
    • Soell, M.1    Lett, E.2    Holveck, F.3    Scholler, M.4    Wachsmann, D.5    Klein, J.P.6
  • 21
    • 0029793838 scopus 로고    scopus 로고
    • Surfactant protein A protects growing cells and reduces TNF-α activity from LPS-stimulated macrophages
    • McIntosh, J. C., Mervin-Blake, S., Conner, E. and Wright, J. R., Surfactant protein A protects growing cells and reduces TNF-α activity from LPS-stimulated macrophages. Am. J. Physiol. 1996. 271: L310-L319.
    • (1996) Am. J. Physiol. , vol.271
    • McIntosh, J.C.1    Mervin-Blake, S.2    Conner, E.3    Wright, J.R.4
  • 23
    • 0018663083 scopus 로고
    • Reaction between the isolated globular sub-unit of the complement component C1q and IgG-complexes
    • Hughes-Jones, N. C. and Gardner, B., Reaction between the isolated globular sub-unit of the complement component C1q and IgG-complexes. Mol. Immunol. 1979. 16: 697-701.
    • (1979) Mol. Immunol. , vol.16 , pp. 697-701
    • Hughes-Jones, N.C.1    Gardner, B.2
  • 24
    • 0020702354 scopus 로고
    • Measurements of the association constant of the complexes formed between intact C1q of pepsin-treated C1q stalks and the unactivated or activated C1r2C1s2 tetramers
    • Siegel, R. C., and Schumaker, V. N., Measurements of the association constant of the complexes formed between intact C1q of pepsin-treated C1q stalks and the unactivated or activated C1r2C1s2 tetramers. Mol. Immunol. 1983. 20: 53-66.
    • (1983) Mol. Immunol. , vol.20 , pp. 53-66
    • Siegel, R.C.1    Schumaker, V.N.2
  • 26
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components
    • Takeuchi, O., Hoshino, K., Kawai, T., Sanjo, H., Takada, H., Ogawa, T., Takeda, K. and Akira, S., Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components. Immunity 1999. 11: 443-451.
    • (1999) Immunity , vol.11 , pp. 443-451
    • Takeuchi, O.1    Hoshino, K.2    Kawai, T.3    Sanjo, H.4    Takada, H.5    Ogawa, T.6    Takeda, K.7    Akira, S.8
  • 28
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R., Akashi, S., Ogata, H., Nagai, Y., Fukudome, K., Miyake, K. and Kimoto, M., MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 1999. 189: 1777-1782.
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 29
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai, T., Adachi, O., Ogawa, T., Takeda, K. and Akira, S., Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity 1999. 11: 115-122.
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 30
    • 0030891006 scopus 로고    scopus 로고
    • Identification and characterization of a novel Ets-2-related nuclear complex implicated in the activation of human interleukin-12 p40 gene promoter
    • Ma, X., Neurath, M., Gri, G. and Trinchieri, G., Identification and characterization of a novel Ets-2-related nuclear complex implicated in the activation of human interleukin-12 p40 gene promoter. J. Biol. Chem. 1997. 272: 10389-10395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10389-10395
    • Ma, X.1    Neurath, M.2    Gri, G.3    Trinchieri, G.4
  • 31
    • 0032513227 scopus 로고    scopus 로고
    • Synergic regulation of the human interleukin-12 p40 promoter by NF-kappaB and Ets transcription factors in Epstein-Barr virus-transformed B cells and macrophages
    • Gri, G., Savio, D., Trinchieri, G. and Ma, X., Synergic regulation of the human interleukin-12 p40 promoter by NF-kappaB and Ets transcription factors in Epstein-Barr virus-transformed B cells and macrophages. J. Biol. Chem. 1998. 273: 6431-6438.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6431-6438
    • Gri, G.1    Savio, D.2    Trinchieri, G.3    Ma, X.4
  • 32
    • 0029143632 scopus 로고
    • Regulation of interleukin 12 p40 expression through an NF-kappaB half-site
    • Murphy, T. L., Cleveland, M. G., Kulesza, P., Magram, J. and Murphy, K. M., Regulation of interleukin 12 p40 expression through an NF-kappaB half-site. Mol. Cell. Biol. 1995. 15: 5258-5267.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5258-5267
    • Murphy, T.L.1    Cleveland, M.G.2    Kulesza, P.3    Magram, J.4    Murphy, K.M.5
  • 34
    • 0030872393 scopus 로고    scopus 로고
    • Multiple control elements mediate activation of the murine and human interleukin 12 p40 promoters: Evidence of functional synergy between C/EBP and Rel proteins
    • Plevy, S. E., Gemberling, J. H., Hsu, S., Dorner, A. J. and Smale, S. T., Multiple control elements mediate activation of the murine and human interleukin 12 p40 promoters: evidence of functional synergy between C/EBP and Rel proteins. Mol. Cell. Biol. 1997. 17: 4572-4588.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4572-4588
    • Plevy, S.E.1    Gemberling, J.H.2    Hsu, S.3    Dorner, A.J.4    Smale, S.T.5
  • 36
    • 0035339861 scopus 로고    scopus 로고
    • Endotoxin-induced maturation of MyD88-deficient dendritic cells
    • Kaisho, T., Takeuchi, O., Kawai, T., Hoshino, K. and Akira, S., Endotoxin-induced maturation of MyD88-deficient dendritic cells. J. Immunol. 2001. 166: 5688-5694.
    • (2001) J. Immunol. , vol.166 , pp. 5688-5694
    • Kaisho, T.1    Takeuchi, O.2    Kawai, T.3    Hoshino, K.4    Akira, S.5
  • 37
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng, T., Barton, G. M. and Medzhitov, R., TIRAP: an adapter molecule in the Toll signaling pathway. Nat. Immunol. 2001. 9: 835-841.
    • (2001) Nat. Immunol. , vol.9 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 39
    • 0033118982 scopus 로고    scopus 로고
    • Defective IL-12 production in mitogen-activated protein (MAP) kinase kinase 3 (Mkk3)-deficient mice
    • Lu, H. T., Yang, D. D., Wysk, M., Gatti, E., Mellman, I., Davis, R. J. and Flavell R. A., Defective IL-12 production in mitogen-activated protein (MAP) kinase kinase 3 (Mkk3)-deficient mice. EMBO J. 1999. 18: 1845-1857.
    • (1999) EMBO J. , vol.18 , pp. 1845-1857
    • Lu, H.T.1    Yang, D.D.2    Wysk, M.3    Gatti, E.4    Mellman, I.5    Davis, R.J.6    Flavell, R.A.7
  • 41
    • 0032806197 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced tumor necrosis factor alpha production by human monocytes involves the Raf-1/MEK1-MEK2/ERK1-ERK2 pathway
    • van der Bruggen, T., Nijenhuis, S., van Raaij, E., Verhoef, J. and van Asbeck, B. S., Lipopolysaccharide-induced tumor necrosis factor alpha production by human monocytes involves the Raf-1/MEK1-MEK2/ERK1-ERK2 pathway. Infect. Immun. 1999. 67: 3824-3829.
    • (1999) Infect. Immun. , vol.67 , pp. 3824-3829
    • van der Bruggen, T.1    Nijenhuis, S.2    van Raaij, E.3    Verhoef, J.4    van Asbeck, B.S.5
  • 43
    • 0030858764 scopus 로고    scopus 로고
    • Lipopolysaccharide induction of the tumor necrosis factor-α promoter in human monocytic cells
    • Yao, J., Mackman, N., Edgington, T. S. and Fan, S. T., Lipopolysaccharide induction of the tumor necrosis factor-α promoter in human monocytic cells. J. Biol. Chem. 1997. 272: 17795-17801.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17795-17801
    • Yao, J.1    Mackman, N.2    Edgington, T.S.3    Fan, S.T.4
  • 44
    • 0033597252 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced tumor necrosis factor-α promoter activity is inhibitor of nuclear factor-κB kinase-dependent
    • Swantek, J. L., Christerson, L. and Cobb, M. H., Lipopolysaccharide-induced tumor necrosis factor-α promoter activity is inhibitor of nuclear factor-κB kinase-dependent. J. Biol. Chem. 1999. 274: 11667-11671.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11667-11671
    • Swantek, J.L.1    Christerson, L.2    Cobb, M.H.3
  • 47
    • 0036143654 scopus 로고    scopus 로고
    • p38-dependent marking of inflammatory genes for increased NF-κB recruitment
    • Saccani, S., Pantano, S. and Natoli, G., p38-dependent marking of inflammatory genes for increased NF-κB recruitment. Nat. Immunol. 2002. 3: 69-75.
    • (2002) Nat. Immunol. , vol.3 , pp. 69-75
    • Saccani, S.1    Pantano, S.2    Natoli, G.3
  • 48
    • 0035469890 scopus 로고    scopus 로고
    • Lipopolysaccharide activation of the MEK-ERK1/2 pathway in human monocytic cells mediates tissue factor and tumor necrosis factor α expression by inducing Elk-1 phosphorylation and Egr-1 expression
    • Guha, M., O'Connell, M. A., Pawlinski, R., Hollis, A., McGovern, P., Yan, S. F., Stern, D. and Mackman, N., Lipopolysaccharide activation of the MEK-ERK1/2 pathway in human monocytic cells mediates tissue factor and tumor necrosis factor α expression by inducing Elk-1 phosphorylation and Egr-1 expression. Blood 2001. 98: 1429-1439.
    • (2001) Blood , vol.98 , pp. 1429-1439
    • Guha, M.1    O'Connell, M.A.2    Pawlinski, R.3    Hollis, A.4    McGovern, P.5    Yan, S.F.6    Stern, D.7    Mackman, N.8
  • 49
    • 0032740614 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase
    • Feng, G. J., Goodridge, H. S., Harnett, M. M., Wei, X. Q., Nikolaev, A. V., Higson, A. P. and Liew, F. Y., Extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase. J. Immunol. 1999. 163: 6403-6412.
    • (1999) J. Immunol. , vol.163 , pp. 6403-6412
    • Feng, G.J.1    Goodridge, H.S.2    Harnett, M.M.3    Wei, X.Q.4    Nikolaev, A.V.5    Higson, A.P.6    Liew, F.Y.7
  • 50
    • 0029761275 scopus 로고    scopus 로고
    • TRAF6 is a signal transducer of interleukin-1
    • Cao, Z., Xiong, J., Takeuchi, M., Kurama, T. and Goeddel, D. V., TRAF6 is a signal transducer of interleukin-1. Nature 1996. 383: 443-446.
    • (1996) Nature , vol.383 , pp. 443-446
    • Cao, Z.1    Xiong, J.2    Takeuchi, M.3    Kurama, T.4    Goeddel, D.V.5
  • 53
    • 0026481133 scopus 로고
    • Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor
    • Inaba, K., Inaba, M., Romani, N., Aya, H., Deguchi, M., Ikehara, S., Muramatsu, S. and Steinman, R.M., Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor. J. Exp. Med. 1992. 176: 1693-1702.
    • (1992) J. Exp. Med. , vol.176 , pp. 1693-1702
    • Inaba, K.1    Inaba, M.2    Romani, N.3    Aya, H.4    Deguchi, M.5    Ikehara, S.6    Muramatsu, S.7    Steinman, R.M.8
  • 54
    • 0036319517 scopus 로고    scopus 로고
    • A variety of microbial components induce tolerance to lipopolysaccharide by differentially affecting MyD88-dependent and -independent pathways
    • Sato, S., Takeuchi, O., Hujita, T., Tomizawa, H., Takeda, K. and Akira, S., A variety of microbial components induce tolerance to lipopolysaccharide by differentially affecting MyD88-dependent and -independent pathways. Int. Immunol. 2002. 14: 783-791.
    • (2002) Int. Immunol. , vol.14 , pp. 783-791
    • Sato, S.1    Takeuchi, O.2    Hujita, T.3    Tomizawa, H.4    Takeda, K.5    Akira, S.6


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