메뉴 건너뛰기




Volumn 277, Issue 9, 2010, Pages 2051-2066

Human lactoferrin activates NF-κB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling

Author keywords

Human lactoferrin; Innate immunity; Lipopolysaccharide; Nuclear factor B (NF B); Toll like receptor 4 (TLR4)

Indexed keywords

CHEMOKINE; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LACTOFERRIN; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 5; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 77951225235     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07620.x     Document Type: Article
Times cited : (102)

References (50)
  • 3
    • 0032737846 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein
    • Vorland LH (1999) Lactoferrin: a multifunctional glycoprotein. APMIS 107, 971 981.
    • (1999) APMIS , vol.107 , pp. 971-981
    • Vorland, L.H.1
  • 4
    • 33748416650 scopus 로고    scopus 로고
    • Interactions of lactoferrin with cells involved in immune function
    • DOI 10.1139/O06-045
    • Legrand D, Elass E, Carpentier M Mazurier J (2006) Interactions of lactoferrin with cells involved in immune function. Biochem Cell Biol 84, 282 290. (Pubitemid 44341302)
    • (2006) Biochemistry and Cell Biology , vol.84 , Issue.3 , pp. 282-290
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 6
    • 0031684157 scopus 로고    scopus 로고
    • Synergic antistaphylococcal properties of lactoferrin and lysozyme
    • Leitch EC Willcox MD (1998) Synergic antistaphylococcal properties of lactoferrin and lysozyme. J Med Microbiol 47, 837 842.
    • (1998) J Med Microbiol , vol.47 , pp. 837-842
    • Leitch, E.C.1    Willcox, M.D.2
  • 7
    • 43049179999 scopus 로고    scopus 로고
    • LPS/TLR4 signal transduction pathway
    • Lu Y-C, Yeh W-C Ohashi PS (2008) LPS/TLR4 signal transduction pathway. Cytokine 42, 145 151.
    • (2008) Cytokine , vol.42 , pp. 145-151
    • Lu, Y.-C.1    Yeh, W.-C.2    Ohashi, P.S.3
  • 10
    • 0034440799 scopus 로고    scopus 로고
    • Human lactoferrin interacts with soluble CD14 and inhibits expression of endothelial adhesion molecules, E-selectin and ICAM-1, induced by the CD14-lipopolysaccharide complex
    • DOI 10.1128/IAI.68.12.6519-6525.2000
    • Baveye S, Elass E, Fernig DG, Blanquart C, Mazurier J Legrand D (2000) Human lactoferrin interacts with soluble CD14 and inhibits expression of endothelial adhesion molecule, E-selectin and ICAM-1, induced by the CD14-lipopolysaccharide complex. Infect Immun 68, 6519 6525. (Pubitemid 32463349)
    • (2000) Infection and Immunity , vol.68 , Issue.12 , pp. 6519-6525
    • Baveye, S.1    Elass, E.2    Fernig, D.G.3    Blanquart, C.4    Mazurier, J.5    Legrand, D.6
  • 16
    • 0028126661 scopus 로고
    • Identification of nucleolin as a binding protein for midkine (MK) and heparin-binding growth associated molecule (HB-GAM)
    • Take M, Tsutsui J, Obama H, Ozawa M, Nakayama T, Maruyama I, Arima T Muramatsu T (1994) Identification of nucleolin as a binding protein for midkine (MK) and heparin-binding growth associated molecule (HB-GAM). J Biochem 116, 1063 1068. (Pubitemid 24354656)
    • (1994) Journal of Biochemistry , vol.116 , Issue.5 , pp. 1063-1068
    • Take, M.1    Tsutsui -i., J.2    Obama, H.3    Ozawa, M.4    Nakayama, T.5    Maruyama, I.6    Arima, T.7    Muramatsu, T.8
  • 17
    • 0037701521 scopus 로고    scopus 로고
    • LDL receptor relatives at the crossroad of endocytosis and signaling
    • DOI 10.1007/s00018-003-2183-Z
    • Schneider WJ Nimpf J (2003) LDL receptor relatives at the crossroad of endocytosis and signaling. Cell Mol Life Sci 60, 892 903. (Pubitemid 36735120)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.5 , pp. 892-903
    • Schneider, W.J.1    Nimpf, J.2
  • 18
    • 0035951070 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human intestinal lactoferrin receptor
    • DOI 10.1021/bi0155899
    • Suzuki YA, Shin K Lönnerdal B (2001) Molecular cloning and functional expression of a human intestinal lactoferrin receptor. Biochemistry 40, 15771 15779. (Pubitemid 34015206)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15771-15779
    • Suzuki, Y.A.1    Shin, K.2    Lonnerdal, B.3
  • 19
    • 28344453346 scopus 로고    scopus 로고
    • Mammalian lactoferrin receptors: Structure and function
    • DOI 10.1007/s00018-005-5371-1
    • Suzuki YA, Lopez V Lönnerdal B (2005) Mammalian lactoferrin receptors: structure and function. Cell Mol Life Sci 62, 2560 2575. (Pubitemid 41721230)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2560-2575
    • Suzuki, Y.A.1    Lopez, V.2    Lonnerdal, B.3
  • 20
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin AS Jr. (1996) The NF-κB and IκB proteins: new discoveries and insights. Annu Rev Immunol 14, 649 681. (Pubitemid 126664210)
    • (1996) Annual Review of Immunology , vol.14 , pp. 649-681
    • Baldwin Jr., A.S.1
  • 21
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden MS Ghosh S (2004) Signaling to NF-κB. Genes Dev 18, 2195 2224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 22
    • 0029997681 scopus 로고    scopus 로고
    • Binding characteristics of human lactoferrin to the human monocytic leukemia cell line THP-1 differentiated into macrophages
    • Eda S, Kikugawa K Beppu M (1996) Binding characteristics of human lactoferrin to the human monocytic leukemia cell line THP-1 differentiated into macrophages. Biol Pharm Bull 19, 167 175. (Pubitemid 26088595)
    • (1996) Biological and Pharmaceutical Bulletin , vol.19 , Issue.2 , pp. 167-175
    • Eda, S.1    Kikugawa, K.2    Beppu, M.3
  • 23
    • 0014339479 scopus 로고
    • Studies on proteolytic enzymes (pronase) of Streptomyces griseus K-1. II. Separation of exo- and endopeptidases of pronase
    • Narahashi Y, Shibuya K Yanagita M (1968) Studies on proteolytic enzymes (pronase) of Streptomyces griseus K-1. II. Separation of exo- and endopeptidases of pronase. J Biochem 64, 427 437.
    • (1968) J Biochem , vol.64 , pp. 427-437
    • Narahashi, Y.1    Shibuya, K.2    Yanagita, M.3
  • 24
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden MS Ghosh S (2008) Shared principles in NF-κB signaling. Cell 132, 344 362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 26
    • 0032530455 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factors (TRAFs) - A family of adapter proteins that regulates life and death
    • Arch RH, Gedrich RW Thompson CB (1998) Tumor necrosis factor receptor-associated factors (TRAFs) - a family of adapter proteins that regulates life and death. Genes Dev 12, 2821 2830.
    • (1998) Genes Dev , vol.12 , pp. 2821-2830
    • Arch, R.H.1    Gedrich, R.W.2    Thompson, C.B.3
  • 27
    • 36049033394 scopus 로고    scopus 로고
    • Signaling to NF-κB by Toll-like receptors
    • Kawai T Akira S (2007) Signaling to NF-κB by Toll-like receptors. TRENDS Mol Med 13, 460 469.
    • (2007) TRENDS Mol Med , vol.13 , pp. 460-469
    • Kawai, T.1    Akira, S.2
  • 28
    • 0141923690 scopus 로고    scopus 로고
    • Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the toll-like receptor signaling
    • Sato S, Sugiyama M, Yamamoto M, Watanabe Y, Kawai T, Takeda K Akira S (2003) Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the Toll-like receptor signaling. J Immunol 171, 4304 4310. (Pubitemid 37238709)
    • (2003) Journal of Immunology , vol.171 , Issue.8 , pp. 4304-4310
    • Sato, S.1    Sugiyama, M.2    Yamamoto, M.3    Watanabe, Y.4    Kawai, T.5    Takeda, K.6    Akira, S.7
  • 29
    • 1542723466 scopus 로고    scopus 로고
    • Toll-like receptor 3-mediated activation of NF-κB and IRF3 diverges at Toll-IL-1 receptor domain-containing adapter inducing IFN-β
    • DOI 10.1073/pnas.0308496101
    • Jiang Z, Mak TW, Sen G Li X (2004) Toll-like receptor 3-mediated activation of NF-κB and IRF3 diverges at Toll-IL-1 receptor domain-containing adapter inducing IFN-β. Proc Natl Acad Sci USA 101, 3533 3538. (Pubitemid 38338230)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.10 , pp. 3533-3538
    • Jiang, Z.1    Mak, T.W.2    Sen, G.3    Li, X.4
  • 30
    • 4344613405 scopus 로고    scopus 로고
    • Cutting edge: TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent pathway but not Toll/IL-1 receptor domain-containing adaptor-inducing IFN-β (TRIF)-dependent pathway in TLR signaling
    • Gohda J, Matsumura T Inoue J (2004) TNFR-associated factor (TRAF) 6 is essential for MyD88-dependent pathway but not Toll/IL-1 receptor domain-containing adaptor-inducing IFN-β (TRIF)-dependent pathway in TLR signaling. J Immunol 173, 2913 2917. (Pubitemid 39141993)
    • (2004) Journal of Immunology , vol.173 , Issue.5 , pp. 2913-2917
    • Gohda, J.1    Matsumura, T.2    Inoue, J.-I.3
  • 31
    • 0024119835 scopus 로고
    • Comparative study of the primary structures of sero-, lacto-, and ovotransferrin glycans from different species
    • Spik G, Coddeville B Montreuil J (1988) Comparative study of the primary structures of sero-, lacto-, and ovotransferrin glycans from different species. Biochimie 70, 1459 1469.
    • (1988) Biochimie , vol.70 , pp. 1459-1469
    • Spik, G.1    Coddeville, B.2    Montreuil, J.3
  • 32
    • 0021265108 scopus 로고
    • Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes
    • Fukuda M, Dell A, Oates JE Fukuda MN (1984) Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes. J Biol Chem 259, 8260 8273. (Pubitemid 14090574)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.13 , pp. 8260-8273
    • Fukuda, M.1    Dell, A.2    Oates, J.E.3    Fukuda, M.N.4
  • 33
    • 0026636590 scopus 로고
    • Antigenic determinants of senescent antigen of human erythrocytes are located in sialylated carbohydrate chains of band 3 glycoprotein
    • Beppu M, Mizukami A, Ando K Kikugawa K (1992) Antigenic determinants of senescent antigen of human erythrocytes are located in sialylated carbohydrate chains of band 3 glycoprotein. J Biol Chem 267, 14691 14696.
    • (1992) J Biol Chem , vol.267 , pp. 14691-14696
    • Beppu, M.1    Mizukami, A.2    Ando, K.3    Kikugawa, K.4
  • 35
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide evidence for TLR4 as the Lps gene product
    • Hoshino K, Takeuchi O, Kawai T, Sanjo H, Ogawa T, Takeda Y, Takeda K Akira S (1999) Cutting Edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccaride: evidence for TLR4 as the Lps gene product. J Immunol 162, 3749 3752. (Pubitemid 29314747)
    • (1999) Journal of Immunology , vol.162 , Issue.7 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3    Sanjo, H.4    Ogawa, T.5    Takeda, Y.6    Takeda, K.7    Akira, S.8
  • 36
    • 0034857271 scopus 로고    scopus 로고
    • The role of MyD88 and TLR4 in the LPS-mimetic activity of Taxol
    • DOI 10.1002/1521-4141(200108)31:8<2448::AID-IMMU2448>3.0.CO;2-N
    • Byrd-Leifer CA, Block EF, Takeda K, Akira S Ding A (2001) The role of MyD88 and TLR4 in the LPS-mimetic activities of Taxol. Eur J Immunol 31, 2448 2457. (Pubitemid 32785364)
    • (2001) European Journal of Immunology , vol.31 , Issue.8 , pp. 2448-2457
    • Byrd-Leifer, C.A.1    Block, E.F.2    Takeda, K.3    Akira, S.4    Ding, A.5
  • 37
    • 0034723186 scopus 로고    scopus 로고
    • Mouse toll-like receptor 4·MD-2 complex mediates lipopolysaccharide- mimetic signal transduction by Taxol
    • DOI 10.1074/jbc.275.4.2251
    • Kawasaki K, Akashi S, Shimazu R, Yoshida T, Miyake K Nishijima M (2000) Mouse Toll-like receptor 4/MD-2 complex mediates lipopolysaccharide-mimetic signal transduction by Taxol. J Biol Chem 275, 2251 2254. (Pubitemid 30081977)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2251-2254
    • Kawasaki, K.1    Akashi, S.2    Shimazu, R.3    Yoshida, T.4    Miyake, K.5    Nishijima, M.6
  • 38
    • 12444341944 scopus 로고    scopus 로고
    • Toll-like receptors in innate immunity
    • Takeda K Akira S (2005) Toll-like receptors in innate immunity. Int Immunol 17, 1 14.
    • (2005) Int Immunol , vol.17 , pp. 1-14
    • Takeda, K.1    Akira, S.2
  • 39
    • 0037414787 scopus 로고    scopus 로고
    • Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages
    • DOI 10.1074/jbc.M208742200
    • Gao B Tsan M-F (2003) Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages. J Biol Chem 278, 174 179. (Pubitemid 36043559)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 174-179
    • Gao, B.1    Tsan, M.-F.2
  • 41
    • 34547510802 scopus 로고    scopus 로고
    • Structural biology of the LPS recognition
    • DOI 10.1016/j.ijmm.2007.04.001, PII S1438422107000689
    • Jerala R (2007) Structural biology of the LPS recognition. Int J Med Microbiol 297, 353 363. (Pubitemid 47188054)
    • (2007) International Journal of Medical Microbiology , vol.297 , Issue.5 , pp. 353-363
    • Jerala, R.1
  • 42
    • 33845464963 scopus 로고    scopus 로고
    • Lactoferrin activates macrophages via TLR4-dependent and -independent signaling pathways
    • DOI 10.1016/j.cellimm.2006.08.006, PII S0008874906001523
    • Curran CS, Demick KP Mansfield JM (2006) Lactoferrin activates macrophages via TLR4-dependent and -independent signaling pathways. Cell Immunol 242, 23 30. (Pubitemid 44894393)
    • (2006) Cellular Immunology , vol.242 , Issue.1 , pp. 23-30
    • Curran, C.S.1    Demick, K.P.2    Mansfield, J.M.3
  • 44
    • 33846829418 scopus 로고    scopus 로고
    • Advances in our understanding of the biology of human milk and its effects on the offspring
    • Schack-Nielsen L Michaelsen KF (2007) Advances in our understanding of the biology of human milk and its effects on the offspring. J Nutr 137, 503S 510S. (Pubitemid 46213473)
    • (2007) Journal of Nutrition , vol.137 , Issue.2
    • Schack-Nielsen, L.1    Michaelsen, K.F.2
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 33749946901 scopus 로고
    • Colorimetric method of determination of sugars and related substances
    • Dubois M, Gilles KA, Hamilton JK, Rebers PA Smith F (1956) Colorimetric method of determination of sugars and related substances. Anal Chem 28, 350 356.
    • (1956) Anal Chem , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 48
    • 0035168317 scopus 로고    scopus 로고
    • Acholeplasma laidlawii up-regulates granulysin gene expression via transcription factor activator protein-1 in a human monocytic cell line, THP-1
    • DOI 10.1046/j.1365-2567.2001.01310.x
    • Kida Y, Kuwano K, Zhang Y Arai S (2001) Acholeplasma laidlawii up-regulates granulysin gene expression via transcription factor protein-1 in a human monocytic cell line, THP-1. Immunology 104, 324 332. (Pubitemid 33064458)
    • (2001) Immunology , vol.104 , Issue.3 , pp. 324-332
    • Kida, Y.1    Kuwano, K.2    Zhang, Y.3    Arai, S.4
  • 49
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-B transcription factor and HIV-1
    • Schreck R, Rieber P Baeuerle PA (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J 10, 2247 2258. (Pubitemid 21905698)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 50
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DOI 10.1038/41493
    • DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E Karin M (1997) A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388, 548 554. (Pubitemid 27339997)
    • (1997) Nature , vol.388 , Issue.6642 , pp. 548-554
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.