메뉴 건너뛰기




Volumn 177, Issue 6, 2006, Pages 4072-4079

Serum amyloid A is an endogenous ligand that differentially induces IL-12 and IL-23

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; C REACTIVE PROTEIN; CCAAT ENHANCER BINDING PROTEIN; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 12; INTERLEUKIN 12P40; INTERLEUKIN 17; INTERLEUKIN 23; INTERLEUKIN 23P19; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; POLYMYXIN B; SERUM AMYLOID A; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 33748499140     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.6.4072     Document Type: Article
Times cited : (80)

References (64)
  • 1
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay, C., and I. Kushner. 1999. Acute-phase proteins and other systemic responses to inflammation. N. Engl. J. Med. 340: 448-454.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 2
    • 0028095919 scopus 로고
    • The acute phase response
    • Baumann, H., and J. Gauldie. 1994. The acute phase response. Immunol. Today 15: 74-80.
    • (1994) Immunol. Today , vol.15 , pp. 74-80
    • Baumann, H.1    Gauldie, J.2
  • 3
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar, C. M., and A. S. Whitehead. 1999. Serum amyloid A, the major vertebrate acute-phase reactant. Eur. J. Biochem. 265: 501-523.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 501-523
    • Uhlar, C.M.1    Whitehead, A.S.2
  • 4
    • 0033988643 scopus 로고    scopus 로고
    • Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states
    • Urieli-Shoval, S., R. P. Linke, and Y. Matzner. 2000. Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states. Curr. Opin. Hematol. 7: 64-69.
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 64-69
    • Urieli-Shoval, S.1    Linke, R.P.2    Matzner, Y.3
  • 5
    • 0029886548 scopus 로고    scopus 로고
    • Human serum amyloid A (SAA) protein: A prominent acute-phase reactant for clinical practice
    • Malle, E., and F. C. De Beer. 1996. Human serum amyloid A (SAA) protein: a prominent acute-phase reactant for clinical practice. Eur. J. Clin. Invest. 26: 427-435.
    • (1996) Eur. J. Clin. Invest. , vol.26 , pp. 427-435
    • Malle, E.1    De Beer, F.C.2
  • 6
    • 0030685738 scopus 로고    scopus 로고
    • Association between serum amyloid A proteins and coronary artery disease: Evidence from two distinct arteriosclerotic processes
    • Fyfe, A. I., L. S. Rothenberg, F. C. DeBeer, R. M. Cantor, J. I. Rotter, and A. J. Lusis. 1997. Association between serum amyloid A proteins and coronary artery disease: evidence from two distinct arteriosclerotic processes. Circulation 96: 2914-2919.
    • (1997) Circulation , vol.96 , pp. 2914-2919
    • Fyfe, A.I.1    Rothenberg, L.S.2    Debeer, F.C.3    Cantor, R.M.4    Rotter, J.I.5    Lusis, A.J.6
  • 7
    • 0021051914 scopus 로고
    • Serum amyloid-A protein concentration in rheumatoid arthritis and its role in monitoring disease activity
    • Chambers, R. E., D. G. MacFarlane, J. T. Whicher, and P. A. Dieppe. 1983. Serum amyloid-A protein concentration in rheumatoid arthritis and its role in monitoring disease activity. Ann. Rheum. Dis. 42: 665-667.
    • (1983) Ann. Rheum. Dis. , vol.42 , pp. 665-667
    • Chambers, R.E.1    MacFarlane, D.G.2    Whicher, J.T.3    Dieppe, P.A.4
  • 8
    • 0023568036 scopus 로고
    • Serum amyloid A protein compared with C-reactive protein, α1-antichymotrypsin and α1-acid glycoprotein as a monitor of inflammatory bowel disease
    • Chambers, R. E., P. Stross, R. E. Barry, and J. T. Whicher. 1987. Serum amyloid A protein compared with C-reactive protein, α1-antichymotrypsin and α1-acid glycoprotein as a monitor of inflammatory bowel disease. Eur. J. Clin. Invest. 17: 460-467.
    • (1987) Eur. J. Clin. Invest. , vol.17 , pp. 460-467
    • Chambers, R.E.1    Stross, P.2    Barry, R.E.3    Whicher, J.T.4
  • 10
    • 2642535951 scopus 로고    scopus 로고
    • Inflammation as a cardiovascular risk factor
    • Willerson, J. T., and P. M. Ridker. 2004. Inflammation as a cardiovascular risk factor. Circulation 109: 112-10.
    • (2004) Circulation , vol.109 , pp. 112-210
    • Willerson, J.T.1    Ridker, P.M.2
  • 12
    • 2642579895 scopus 로고    scopus 로고
    • CRP as a mediator of disease
    • Yeh, E. T. 2004. CRP as a mediator of disease. Circulation 109: II11-14.
    • (2004) Circulation , vol.109
    • Yeh, E.T.1
  • 13
    • 0032530560 scopus 로고    scopus 로고
    • Regulation of serum amyloid A protein expression during the acute-phase response
    • Jensen, L. E., and A. S. Whitehead. 1998. Regulation of serum amyloid A protein expression during the acute-phase response. Biochem. J. 334: 489-503.
    • (1998) Biochem. J. , vol.334 , pp. 489-503
    • Jensen, L.E.1    Whitehead, A.S.2
  • 14
    • 0345299157 scopus 로고
    • Amyloid protein SAA is associated with high density lipoprotein from human serum
    • Benditt, E. P., and N. Eriksen. 1977. Amyloid protein SAA is associated with high density lipoprotein from human serum. Proc. Natl. Acad. Sci. USA 74: 4025-4028.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4025-4028
    • Benditt, E.P.1    Eriksen, N.2
  • 15
  • 16
    • 0032933232 scopus 로고    scopus 로고
    • Expression of serum amyloid A protein in the absence of the acute phase response does not reduce HDL cholesterol or apoA-I levels in human apoA-I transgenic mice
    • Hosoai, H., N. R. Webb, J. M. Glick, U. J. Tietge, M. S. Purdom, F. C. de Beer, and D. J. Rader. 1999. Expression of serum amyloid A protein in the absence of the acute phase response does not reduce HDL cholesterol or apoA-I levels in human apoA-I transgenic mice. J. Lipid Res. 40: 648-653.
    • (1999) J. Lipid Res. , vol.40 , pp. 648-653
    • Hosoai, H.1    Webb, N.R.2    Glick, J.M.3    Tietge, U.J.4    Purdom, M.S.5    De Beer, F.C.6    Rader, D.J.7
  • 17
    • 0028202075 scopus 로고
    • Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: Implications for serum amyloid A function
    • Meek, R. L., S. Urieli-Shoval, and E. P. Benditt. 1994. Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. Proc. Natl. Acad. Sci. USA 91: 3186-3190.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3186-3190
    • Meek, R.L.1    Urieli-Shoval, S.2    Benditt, E.P.3
  • 18
    • 0032916193 scopus 로고    scopus 로고
    • Local expression of acute phase serum amyloid A mRNA in rheumatoid arthritis synovial tissue and cells
    • Kumon, Y., T. Suehiro, K. Hashimoto, K. Nakatani, and J. D. Sipe. 1999. Local expression of acute phase serum amyloid A mRNA in rheumatoid arthritis synovial tissue and cells. J. Rheumatol. 26: 785-790.
    • (1999) J. Rheumatol. , vol.26 , pp. 785-790
    • Kumon, Y.1    Suehiro, T.2    Hashimoto, K.3    Nakatani, K.4    Sipe, J.D.5
  • 19
    • 0035164775 scopus 로고    scopus 로고
    • Amyloid precursors and amyloidosis in inflammatory arthritis
    • Cunnane, G. 2001. Amyloid precursors and amyloidosis in inflammatory arthritis. Curr. Opin. Rheumatol. 13: 67-73.
    • (2001) Curr. Opin. Rheumatol. , vol.13 , pp. 67-73
    • Cunnane, G.1
  • 20
    • 0000485181 scopus 로고    scopus 로고
    • A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells
    • Su, S. B., W. Gong, J. L. Gao, W. Shen, P. M. Murphy, J. J. Oppenheim, and J. M. Wang. 1999. A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells. J. Exp. Med. 189: 395-402.
    • (1999) J. Exp. Med. , vol.189 , pp. 395-402
    • Su, S.B.1    Gong, W.2    Gao, J.L.3    Shen, W.4    Murphy, P.M.5    Oppenheim, J.J.6    Wang, J.M.7
  • 22
    • 13244251233 scopus 로고    scopus 로고
    • Serum amyloid A is a ligand for scavenger receptor class B type I and inhibits high density lipoprotein binding and selective lipid uptake
    • Cai, L., M. C. de Beer, F. C. de Beer, and D. R. van der Westhuyzen. 2005. Serum amyloid A is a ligand for scavenger receptor class B type I and inhibits high density lipoprotein binding and selective lipid uptake. J. Biol. Chem. 280: 2954-2961.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2954-2961
    • Cai, L.1    De Beer, M.C.2    De Beer, F.C.3    Van Der Westhuyzen, D.R.4
  • 27
    • 0029987839 scopus 로고    scopus 로고
    • The instructive role of innate immunity in the acquired immune response
    • Fearon, D. T., and R. M. Locksley. 1996. The instructive role of innate immunity in the acquired immune response. Science 272: 50-53.
    • (1996) Science , vol.272 , pp. 50-53
    • Fearon, D.T.1    Locksley, R.M.2
  • 28
    • 0037441872 scopus 로고    scopus 로고
    • Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R
    • He, R., H. Sang, and R. D. Ye. 2003. Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R. Blood 101: 1572-1581.
    • (2003) Blood , vol.101 , pp. 1572-1581
    • He, R.1    Sang, H.2    Ye, R.D.3
  • 29
    • 0034673318 scopus 로고    scopus 로고
    • A novel function of serum amyloid A: A potent stimulus for the release of tumor necrosis factor-1β, interleukin-1β, and interleukin-8 by human blood neutrophil
    • Furlaneto, C. J., and A. Campa. 2000. A novel function of serum amyloid A: a potent stimulus for the release of tumor necrosis factor-1β, interleukin-1β, and interleukin-8 by human blood neutrophil. Biochem. Biophys. Res. Commun. 268: 405-408.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 405-408
    • Furlaneto, C.J.1    Campa, A.2
  • 31
    • 0031754163 scopus 로고    scopus 로고
    • Human serum amyloid A has cytokine-like properties
    • Patel, H., R. Fellowes, S. Coade, and P. Woo. 1998. Human serum amyloid A has cytokine-like properties. Scand. J. Immunol. 48: 410-418.
    • (1998) Scand. J. Immunol. , vol.48 , pp. 410-418
    • Patel, H.1    Fellowes, R.2    Coade, S.3    Woo, P.4
  • 33
  • 35
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • Gingras, A. C., S. G. Kennedy, M. A. O'Leary, N. Sonenberg, and N. Hay. 1998. 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway. Genes Dev. 12: 502-513.
    • (1998) Genes Dev. , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 36
    • 0030812347 scopus 로고    scopus 로고
    • Apoptosis signaling pathway in T cells is composed of ICE/Ced-3 family proteases and MAP kinase kinase 6b
    • Huang, S., Y. Jiang, Z. Li, E. Nishida, P. Mathias, S. Lin, R. J. Ulevitch, G. R. Nemerow, and J. Han. 1997. Apoptosis signaling pathway in T cells is composed of ICE/Ced-3 family proteases and MAP kinase kinase 6b. Immunity 6: 739-749.
    • (1997) Immunity , vol.6 , pp. 739-749
    • Huang, S.1    Jiang, Y.2    Li, Z.3    Nishida, E.4    Mathias, P.5    Lin, S.6    Ulevitch, R.J.7    Nemerow, G.R.8    Han, J.9
  • 37
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J, D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11: 1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 38
    • 0029031505 scopus 로고
    • Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway
    • Kravchenko, V. V., Z. Pan, J. Han, J. M. Herbert, R. J. Ulevitch, and R. D. Ye. 1995. Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway. J. Biol. Chem. 25: 14928-14934.
    • (1995) J. Biol. Chem. , vol.25 , pp. 14928-14934
    • Kravchenko, V.V.1    Pan, Z.2    Han, J.3    Herbert, J.M.4    Ulevitch, R.J.5    Ye, R.D.6
  • 39
    • 0034763143 scopus 로고    scopus 로고
    • Regulation of interleukin-12 production in antigen-presenting cells
    • Ma, X., and G. Trinchieri. 2001. Regulation of interleukin-12 production in antigen-presenting cells. Adv. Immunol. 79: 55-92.
    • (2001) Adv. Immunol. , vol.79 , pp. 55-92
    • Ma, X.1    Trinchieri, G.2
  • 40
    • 0024340980 scopus 로고
    • Polymyxin B prevents lipopolysaccharide-induced release of tumor necrosis factor-α from alveolar macrophages
    • Stokes, D. C., J. L. Shenep, M. Fishman, W. K. Hildner, G. K. Bysani, and K. Rufus. 1989. Polymyxin B prevents lipopolysaccharide-induced release of tumor necrosis factor-α from alveolar macrophages. J. Infect. Dis. 160: 52-57.
    • (1989) J. Infect. Dis. , vol.160 , pp. 52-57
    • Stokes, D.C.1    Shenep, J.L.2    Fishman, M.3    Hildner, W.K.4    Bysani, G.K.5    Rufus, K.6
  • 41
    • 0014077554 scopus 로고
    • Prevention by polymyxin B of endotoxin lethality in mice
    • Rifkind, D. 1967. Prevention by polymyxin B of endotoxin lethality in mice. J. Bacteriol 93: 1463-1464.
    • (1967) J. Bacteriol. , vol.93 , pp. 1463-1464
    • Rifkind, D.1
  • 42
    • 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., J. H. Gemberling, S. Hsu, A. J. Dorner, and S. T. Smale. 1997. 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. 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
  • 44
    • 15844411922 scopus 로고    scopus 로고
    • Serum amyloid A activates NF-κB and proinflammatory gene expression in human and murine intestinal epithelial cells
    • Jijon, H. B., K. L. Madsen, J. W. Walker, B. Allard, and C. Jobin. 2005. Serum amyloid A activates NF-κB and proinflammatory gene expression in human and murine intestinal epithelial cells. Eur. J. Immunol. 35: 718-726.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 718-726
    • Jijon, H.B.1    Madsen, K.L.2    Walker, J.W.3    Allard, B.4    Jobin, C.5
  • 46
    • 16244412633 scopus 로고    scopus 로고
    • Serum amyloid A stimulates matrix-metalloproteinase-9 upregulation via formyl peptide receptor like-1-mediated signaling in human monocytic cells
    • Lee, H. Y., M. K. Kim, K. S. Park, Y. H. Bae, J. Yun, J. I. Park, J. Y. Kwak, and Y. S. Bae. 2005. Serum amyloid A stimulates matrix-metalloproteinase-9 upregulation via formyl peptide receptor like-1-mediated signaling in human monocytic cells. Biochem. Biophys. Res. Commun. 330: 989-998.
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 989-998
    • Lee, H.Y.1    Kim, M.K.2    Park, K.S.3    Bae, Y.H.4    Yun, J.5    Park, J.I.6    Kwak, J.Y.7    Bae, Y.S.8
  • 47
    • 0033775754 scopus 로고    scopus 로고
    • NF-κB regulates the LPS-induced expression of interleukin 12 p40 in murine peritoneal macrophages: Roles of PKC, PKA, ERK, p38 MAPK, and proteasome
    • Zhang, J. S., W. G. Feng, C. L. Li, X. Y. Wang, and Z. L. Chang. 2000. NF-κB regulates the LPS-induced expression of interleukin 12 p40 in murine peritoneal macrophages: roles of PKC, PKA, ERK, p38 MAPK, and proteasome. Cell. Immunol. 204: 38-45.
    • (2000) Cell. Immunol. , vol.204 , pp. 38-45
    • Zhang, J.S.1    Feng, W.G.2    Li, C.L.3    Wang, X.Y.4    Chang, Z.L.5
  • 48
    • 0038127035 scopus 로고    scopus 로고
    • Differential regulation of interleukin-12 p40 and p35 induction via Erk mitogen-activated protein kinase-dependent and -independent mechanisms and the implications for bioactive IL-12 and IL-23 responses
    • Goodridge, H. S., W. Harnett, F. Y. Liew, and M. M. Harnett. 2003. Differential regulation of interleukin-12 p40 and p35 induction via Erk mitogen-activated protein kinase-dependent and -independent mechanisms and the implications for bioactive IL-12 and IL-23 responses. Immunology 109: 415-425.
    • (2003) Immunology , vol.109 , pp. 415-425
    • Goodridge, H.S.1    Harnett, W.2    Liew, F.Y.3    Harnett, M.M.4
  • 49
    • 0037629646 scopus 로고    scopus 로고
    • PI3K and negative regulation of TLR signaling
    • Fukao, T., and S. Koyasu. 2003. PI3K and negative regulation of TLR signaling. Trends Immunol. 24: 358-363.
    • (2003) Trends Immunol. , vol.24 , pp. 358-363
    • Fukao, T.1    Koyasu, S.2
  • 51
    • 0038446051 scopus 로고    scopus 로고
    • Role of the phosphatidylinositol 3 kinase-Akt pathway in the regulation of IL-10 and IL-12 by Porphyromonas gingivalis lipopolysaccharide
    • Martin, M., R. E. Schifferle, N. Cuesta, S. N. Vogel, J. Katz, and S. M. Michalek. 2003. Role of the phosphatidylinositol 3 kinase-Akt pathway in the regulation of IL-10 and IL-12 by Porphyromonas gingivalis lipopolysaccharide. J. Immunol. 171: 717-725.
    • (2003) J. Immunol. , vol.171 , pp. 717-725
    • Martin, M.1    Schifferle, R.E.2    Cuesta, N.3    Vogel, S.N.4    Katz, J.5    Michalek, S.M.6
  • 53
    • 25444465640 scopus 로고    scopus 로고
    • Clq receptor ligation selectively down-regulates human IL-12 production through activation of the phosphoinositide 3-kinase pathway
    • Waggoner, S. N., M. W. Cruise, R. Kassel, and Y. S. Hahn. 2005. gClq receptor ligation selectively down-regulates human IL-12 production through activation of the phosphoinositide 3-kinase pathway. J. Immunol. 175: 4706-4714.
    • (2005) J. Immunol. , vol.175 , pp. 4706-4714
    • Waggoner, S.N.1    Cruise, M.W.2    Kassel, R.3    Hahn, Y.S.4
  • 54
    • 0142156744 scopus 로고    scopus 로고
    • Differential regulation of interleukin (IL)-12 p35 and p40 gene expression and interferon (IFN)-γ-primed IL-12 production by IFN regulatory factor 1
    • Liu, I., S. Cao, L. M. Herman, and X. Ma. 2003. Differential regulation of interleukin (IL)-12 p35 and p40 gene expression and interferon (IFN)-γ-primed IL-12 production by IFN regulatory factor 1. J. Exp. Med. 198: 1265-1276.
    • (2003) J. Exp. Med. , vol.198 , pp. 1265-1276
    • Liu, I.1    Cao, S.2    Herman, L.M.3    Ma, X.4
  • 55
  • 56
    • 0035383783 scopus 로고    scopus 로고
    • 2 is a selective inducer of interleukin-12 p40 (IL-12p40) production and an inhibitor of bioactive IL-12p70 heterodimer
    • 2 is a selective inducer of interleukin-12 p40 (IL-12p40) production and an inhibitor of bioactive IL-12p70 heterodimer. Blood 97: 3466-3469.
    • (2001) Blood , vol.97 , pp. 3466-3469
    • Kalinski, P.1    Vieira, P.L.2    Schuitemaker, J.H.3    De Jong, E.C.4    Kapsenberg, M.L.5
  • 57
    • 0025819340 scopus 로고
    • Induction of interferon γ production by natural killer cell stimulatory factor: Characterization of the responder cells and synergy with other inducers
    • Chan, S. H., B. Perussia, J. W. Gupta. M. Kobayashi, M. Pospisil, H. A. Young, S. F. Wolf, D. Young, S. C. Clark, and G. Trinchieri. 1991. Induction of interferon γ production by natural killer cell stimulatory factor: characterization of the responder cells and synergy with other inducers. J. Exp. Med. 173: 869-879.
    • (1991) J. Exp. Med. , vol.173 , pp. 869-879
    • Chan, S.H.1    Perussia, B.2    Gupta, J.W.3    Kobayashi, M.4    Pospisil, M.5    Young, H.A.6    Wolf, S.F.7    Young, D.8    Clark, S.C.9    Trinchieri, G.10
  • 59
    • 0037449737 scopus 로고    scopus 로고
    • Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17
    • Aggarwal, S., N. Ghilardi, M. H. Xie, F. J. de Sauvage, and A. L. Gurney. 2003. Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17. J. Biol. Chem. 278: 1910-1914.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1910-1914
    • Aggarwal, S.1    Ghilardi, N.2    Xie, M.H.3    De Sauvage, F.J.4    Gurney, A.L.5
  • 61
  • 63
    • 15244344110 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic neutrophils regulates granulopoiesis via IL-23 and IL-17
    • Stark, M. A., Y. Huo, T. L. Burcin, M. A. Morris, T. S. Olson, and K. Ley. 2005. Phagocytosis of apoptotic neutrophils regulates granulopoiesis via IL-23 and IL-17. Immunity 22: 285-294.
    • (2005) Immunity , vol.22 , pp. 285-294
    • Stark, M.A.1    Huo, Y.2    Burcin, T.L.3    Morris, M.A.4    Olson, T.S.5    Ley, K.6
  • 64
    • 20444389826 scopus 로고    scopus 로고
    • Serum amyloid A-luciferase transgenic mice: Response to sepsis, acute arthritis, and contact hypersensitivity and the effects of proteasome inhibition
    • Zhang, N., M. H. Ahsan, A. F. Purchio, and D. B. West. 2005. Serum amyloid A-luciferase transgenic mice: response to sepsis, acute arthritis, and contact hypersensitivity and the effects of proteasome inhibition. J. Immunol. 174: 8125-8134.
    • (2005) J. Immunol. , vol.174 , pp. 8125-8134
    • Zhang, N.1    Ahsan, M.H.2    Purchio, A.F.3    West, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.