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Volumn 8, Issue 4, 2013, Pages

S100A12 Suppresses Pro-inflammatory, but Not Pro-Thrombotic Functions of Serum Amyloid A

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHATASE; PROTEIN S100A12; REACTIVE OXYGEN METABOLITE; SERUM AMYLOID A; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84876523060     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0062372     Document Type: Article
Times cited : (11)

References (101)
  • 1
    • 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, Linke RP, Matzner Y, (2000) Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states. Curr Opin Hema 7: 64-69.
    • (2000) Curr Opin Hema , vol.7 , pp. 64-69
    • Urieli-Shoval, S.1    Linke, R.P.2    Matzner, Y.3
  • 2
    • 0031788669 scopus 로고    scopus 로고
    • Widespread expression of serum amyloid A in histologically normal human tissues: predominant localization to the epithelium
    • Urieli-Shoval S, Cohen P, Eisenberg S, Matzner Y, (1998) Widespread expression of serum amyloid A in histologically normal human tissues: predominant localization to the epithelium. J Histochem Cytochem 46: 1377-1384.
    • (1998) J Histochem Cytochem , vol.46 , pp. 1377-1384
    • Urieli-Shoval, S.1    Cohen, P.2    Eisenberg, S.3    Matzner, Y.4
  • 3
    • 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 RL, Urieli-Shoval S, Benditt EP, (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 U S A 91: 3186-3190.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3186-3190
    • Meek, R.L.1    Urieli-Shoval, S.2    Benditt, E.P.3
  • 4
    • 0033934511 scopus 로고    scopus 로고
    • Serum amyloid A secretion from monocytic leukaemia cell line THP-1 and cultured human peripheral monocytes
    • Yamada T, Wada A, Itoh K, Igari J, (2000) Serum amyloid A secretion from monocytic leukaemia cell line THP-1 and cultured human peripheral monocytes. Scand J Immunol 52: 7-12.
    • (2000) Scand J Immunol , vol.52 , pp. 7-12
    • Yamada, T.1    Wada, A.2    Itoh, K.3    Igari, J.4
  • 6
    • 0028578242 scopus 로고
    • Serum amyloid A protein in patients with non-insulin-dependent diabetes mellitus
    • Kumon Y, Suehiro T, Itahara T, Ikeda Y, Hashimoto K, (1994) Serum amyloid A protein in patients with non-insulin-dependent diabetes mellitus. Clin Biochem 27: 469-473.
    • (1994) Clin Biochem , vol.27 , pp. 469-473
    • Kumon, Y.1    Suehiro, T.2    Itahara, T.3    Ikeda, Y.4    Hashimoto, K.5
  • 7
    • 0034704893 scopus 로고    scopus 로고
    • C-reactive protein and other markers of inflammation in the prediction of cardiovascular disease in women
    • Ridker PM, Hennekens CH, Buring JE, Rifai N, (2000) C-reactive protein and other markers of inflammation in the prediction of cardiovascular disease in women. N Engl J Med 342: 836-843.
    • (2000) N Engl J Med , vol.342 , pp. 836-843
    • Ridker, P.M.1    Hennekens, C.H.2    Buring, J.E.3    Rifai, N.4
  • 9
    • 58149515783 scopus 로고    scopus 로고
    • Serum amyloid A: an acute-phase protein involved in tumour pathogenesis
    • Malle E, Sodin-Semrl S, Kovacevic A, (2009) Serum amyloid A: an acute-phase protein involved in tumour pathogenesis. Cell Mol Life Sci 66: 9-26.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 9-26
    • Malle, E.1    Sodin-Semrl, S.2    Kovacevic, A.3
  • 10
    • 0019165036 scopus 로고
    • Isolation and characterization of the amyloid-related apoprotein (SAA) from human high density lipoprotein
    • Eriksen N, Benditt EP, (1980) Isolation and characterization of the amyloid-related apoprotein (SAA) from human high density lipoprotein. Proc Natl Acad Sci U S A 77: 6860-6864.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 6860-6864
    • Eriksen, N.1    Benditt, E.P.2
  • 11
    • 0020457016 scopus 로고
    • Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture
    • Hoffman JS, Benditt EP, (1982) Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J Biol Chem 257: 10518-10522.
    • (1982) J Biol Chem , vol.257 , pp. 10518-10522
    • Hoffman, J.S.1    Benditt, E.P.2
  • 12
    • 2642570282 scopus 로고    scopus 로고
    • Local expression of the serum amyloid A and formyl peptide receptor-like 1 genes in synovial tissue is associated with matrix metalloproteinase production in patients with inflammatory arthritis
    • O'Hara R, Murphy EP, Whitehead AS, FitzGerald O, Bresnihan B, (2004) Local expression of the serum amyloid A and formyl peptide receptor-like 1 genes in synovial tissue is associated with matrix metalloproteinase production in patients with inflammatory arthritis. Arthritis Rheum 50: 1788-1799.
    • (2004) Arthritis Rheum , vol.50 , pp. 1788-1799
    • O'Hara, R.1    Murphy, E.P.2    Whitehead, A.S.3    FitzGerald, O.4    Bresnihan, B.5
  • 13
    • 0034039716 scopus 로고    scopus 로고
    • Serum amyloid A in Alzheimer's disease brain is predominantly localized to myelin sheaths and axonal membrane
    • Chung TF, Sipe JD, McKee A, Fine RE, Schreiber BM, et al. (2000) Serum amyloid A in Alzheimer's disease brain is predominantly localized to myelin sheaths and axonal membrane. Amyloid 7: 105-110.
    • (2000) Amyloid , vol.7 , pp. 105-110
    • Chung, T.F.1    Sipe, J.D.2    McKee, A.3    Fine, R.E.4    Schreiber, B.M.5
  • 14
    • 82855164033 scopus 로고    scopus 로고
    • Serum amyloid A directly accelerates the progression of atherosclerosis in apolipoprotein E-deficient mice
    • Dong Z, Wu T, Qin W, An C, Wang Z, et al. (2011) Serum amyloid A directly accelerates the progression of atherosclerosis in apolipoprotein E-deficient mice. J Mol Med 17: 1357-1364.
    • (2011) J Mol Med , vol.17 , pp. 1357-1364
    • Dong, Z.1    Wu, T.2    Qin, W.3    An, C.4    Wang, Z.5
  • 15
    • 70450278985 scopus 로고    scopus 로고
    • Serum amyloid A induction of cytokines in monocytes/macrophages and lymphocytes
    • Song C, Hsu K, Yamen E, Yan W, Fock J, et al. (2009) Serum amyloid A induction of cytokines in monocytes/macrophages and lymphocytes. Atherosclerosis 207: 374-383.
    • (2009) Atherosclerosis , vol.207 , pp. 374-383
    • Song, C.1    Hsu, K.2    Yamen, E.3    Yan, W.4    Fock, J.5
  • 16
    • 33846514238 scopus 로고    scopus 로고
    • Serum amyloid A induces monocyte tissue factor
    • Cai H, Song C, Endoh I, Goyette J, Jessup W, et al. (2007) Serum amyloid A induces monocyte tissue factor. J Immunol 178: 1852-1860.
    • (2007) J Immunol , vol.178 , pp. 1852-1860
    • Cai, H.1    Song, C.2    Endoh, I.3    Goyette, J.4    Jessup, W.5
  • 17
    • 57349121095 scopus 로고    scopus 로고
    • Serum amyloid A induces endothelial dysfunction in porcine coronary arteries and human coronary artery endothelial cells
    • Wang X, Chai H, Wang Z, Lin PH, Yao Q, et al. (2008) Serum amyloid A induces endothelial dysfunction in porcine coronary arteries and human coronary artery endothelial cells. Am J Physiol Heart Circ Physiol 295: 2399-2408.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295 , pp. 2399-2408
    • Wang, X.1    Chai, H.2    Wang, Z.3    Lin, P.H.4    Yao, Q.5
  • 18
    • 80052265183 scopus 로고    scopus 로고
    • The acute-phase protein serum amyloid A induces endothelial dysfunction that is inhibited by high-density lipoprotein
    • Witting PK, Song C, Hsu K, Hua S, Parry SN, et al. (2011) The acute-phase protein serum amyloid A induces endothelial dysfunction that is inhibited by high-density lipoprotein. Free Radic Biol Med 51: 1390-1398.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1390-1398
    • Witting, P.K.1    Song, C.2    Hsu, K.3    Hua, S.4    Parry, S.N.5
  • 19
    • 0034673318 scopus 로고    scopus 로고
    • A novel function of serum amyloid A: a potent stimulus for the release of tumor necrosis factor-α, interleukin-1β, and interleukin-8 by human blood neutrophil
    • Furlaneto CJ, Campa A, (2000) A novel function of serum amyloid A: a potent stimulus for the release of tumor necrosis factor-α, 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
  • 20
    • 0037441872 scopus 로고    scopus 로고
    • Serum amyloid A induces IL-8 secretion through a G protein-coupled receptor, FPRL1/LXA4R
    • He R, Sang H, Ye RD, (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
  • 21
    • 0037765331 scopus 로고    scopus 로고
    • mRNA expression and release of interleukin-8 induced by serum amyloid A in neutrophils and monocytes
    • Ribeiro FP, Furlaneto CJ, Hatanaka E, Ribeiro WB, Souza GM, et al. (2003) mRNA expression and release of interleukin-8 induced by serum amyloid A in neutrophils and monocytes. Mediators Inflamm 12: 173-178.
    • (2003) Mediators Inflamm , vol.12 , pp. 173-178
    • Ribeiro, F.P.1    Furlaneto, C.J.2    Hatanaka, E.3    Ribeiro, W.B.4    Souza, G.M.5
  • 22
    • 0034724649 scopus 로고    scopus 로고
    • Serum amyloid A-derived peptides, present in human rheumatic synovial fluids, induce the secretion of interferon-γ by human CD4+ T-lymphocytes
    • Yavin EJ, Preciado-Patt L, Rosen O, Yaron M, Suessmuth RD, et al. (2000) Serum amyloid A-derived peptides, present in human rheumatic synovial fluids, induce the secretion of interferon-γ by human CD4+ T-lymphocytes. FEBS Lett 472: 259-262.
    • (2000) FEBS Lett , vol.472 , pp. 259-262
    • Yavin, E.J.1    Preciado-Patt, L.2    Rosen, O.3    Yaron, M.4    Suessmuth, R.D.5
  • 23
    • 23444460848 scopus 로고
    • Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes
    • Badolato R, Wang JM, Murphy WJ, Lloyd AR, Michiel DF, et al. (1994) Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 180: 203-209.
    • (1994) J Exp Med , vol.180 , pp. 203-209
    • Badolato, R.1    Wang, J.M.2    Murphy, W.J.3    Lloyd, A.R.4    Michiel, D.F.5
  • 24
    • 0033534791 scopus 로고    scopus 로고
    • Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway
    • Olsson N, Siegbahn A, Nilsson G, (1999) Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway. Biochem Biophys Res Commun 254: 143-146.
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 143-146
    • Olsson, N.1    Siegbahn, A.2    Nilsson, G.3
  • 25
    • 44349189334 scopus 로고    scopus 로고
    • Serum amyloid A activates nuclear factor-kappaB in rheumatoid synovial fibroblasts through binding to receptor of advanced glycation end-products
    • Okamoto H, Katagiri Y, Kiire A, Momohara S, Kamatani N, (2008) Serum amyloid A activates nuclear factor-kappaB in rheumatoid synovial fibroblasts through binding to receptor of advanced glycation end-products. J Rheumatol 35: 752-756.
    • (2008) J Rheumatol , vol.35 , pp. 752-756
    • Okamoto, H.1    Katagiri, Y.2    Kiire, A.3    Momohara, S.4    Kamatani, N.5
  • 26
    • 84856401514 scopus 로고    scopus 로고
    • Serum amyloid A opposes lipoxin A(4) to mediate glucocorticoid refractory lung inflammation in chronic obstructive pulmonary disease
    • Bozinovski S, Uddin M, Vlahos R, Thompson M, McQualter JL, et al. (2012) Serum amyloid A opposes lipoxin A(4) to mediate glucocorticoid refractory lung inflammation in chronic obstructive pulmonary disease. Proc Natl Acad Sci U S A 109: 935-940.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 935-940
    • Bozinovski, S.1    Uddin, M.2    Vlahos, R.3    Thompson, M.4    McQualter, J.L.5
  • 27
    • 56149092965 scopus 로고    scopus 로고
    • Serum amyloid A induces CCL2 production via formyl peptide receptor-like 1-mediated signaling in human monocytes
    • Lee HY, Kim SD, Shim JW, Lee SY, Lee H, et al. (2008) Serum amyloid A induces CCL2 production via formyl peptide receptor-like 1-mediated signaling in human monocytes. J Immunol 181: 4332-4339.
    • (2008) J Immunol , vol.181 , pp. 4332-4339
    • Lee, H.Y.1    Kim, S.D.2    Shim, J.W.3    Lee, S.Y.4    Lee, H.5
  • 28
    • 0034643268 scopus 로고    scopus 로고
    • Serum amyloid A is a chemotactic agonist at FPR2, a low-affinity N-formylpeptide receptor on mouse neutrophils
    • Liang TS, Wang JM, Murphy PM, Gao JL, (2000) Serum amyloid A is a chemotactic agonist at FPR2, a low-affinity N-formylpeptide receptor on mouse neutrophils. Biochem Biophys Res Commun 270: 331-335.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 331-335
    • Liang, T.S.1    Wang, J.M.2    Murphy, P.M.3    Gao, J.L.4
  • 29
    • 34250872848 scopus 로고    scopus 로고
    • Impact of serum amyloid A on tissue factor and tissue factor pathway inhibitor expression and activity in endothelial cells
    • Zhao Y, Zhou S, Heng CK, (2007) Impact of serum amyloid A on tissue factor and tissue factor pathway inhibitor expression and activity in endothelial cells. Arterioscler Thromb Vasc Biol 27: 1645-1650.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1645-1650
    • Zhao, Y.1    Zhou, S.2    Heng, C.K.3
  • 30
    • 47949085624 scopus 로고    scopus 로고
    • Cutting edge: TLR2 is a functional receptor for acute-phase serum amyloid A
    • Cheng N, He R, Tian J, Ye PP, Ye RD, (2008) Cutting edge: TLR2 is a functional receptor for acute-phase serum amyloid A. J Immunol. 181: 22-26.
    • (2008) J Immunol , vol.181 , pp. 22-26
    • Cheng, N.1    He, R.2    Tian, J.3    Ye, P.P.4    Ye, R.D.5
  • 31
    • 58849134296 scopus 로고    scopus 로고
    • Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2
    • He RL, Zhou J, Hanson CZ, Chen J, Cheng N, et al. (2009) Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2. Blood 113: 429-437.
    • (2009) Blood , vol.113 , pp. 429-437
    • He, R.L.1    Zhou, J.2    Hanson, C.Z.3    Chen, J.4    Cheng, N.5
  • 33
    • 20044367993 scopus 로고    scopus 로고
    • Serum amyloid A binding to CLA-1 (CD36 and LIMPII analogous-1) mediates serum amyloid A protein-induced activation of ERK1/2 and p38 mitogen-activated protein kinases
    • Baranova IN, Vishnyakova TG, Bocharov AV, Kurlander R, Chen Z, et al. (2005) Serum amyloid A binding to CLA-1 (CD36 and LIMPII analogous-1) mediates serum amyloid A protein-induced activation of ERK1/2 and p38 mitogen-activated protein kinases. J Biol Chem 280: 8031-8040.
    • (2005) J Biol Chem , vol.280 , pp. 8031-8040
    • Baranova, I.N.1    Vishnyakova, T.G.2    Bocharov, A.V.3    Kurlander, R.4    Chen, Z.5
  • 34
    • 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, de Beer MC, de Beer FC, van der Westhuyzen DR, (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
  • 35
    • 84866148181 scopus 로고    scopus 로고
    • Acute-phase serum amyloid A regulates tumor necrosis factor alpha and matrix turnover and predicts disease progression in patients with inflammatory arthritis before and after biologic therapy
    • Connolly M, Mullan RH, McCormick J, Matthews C, Sullivan O, et al. (2012) Acute-phase serum amyloid A regulates tumor necrosis factor alpha and matrix turnover and predicts disease progression in patients with inflammatory arthritis before and after biologic therapy. Arthritis Rheum 64: 1035-1045.
    • (2012) Arthritis Rheum , vol.64 , pp. 1035-1045
    • Connolly, M.1    Mullan, R.H.2    McCormick, J.3    Matthews, C.4    Sullivan, O.5
  • 36
    • 77950894882 scopus 로고    scopus 로고
    • CD36 is a novel serum amyloid A (SAA) receptor mediating SAA binding and SAA-induced signaling in human and rodent cells
    • Baranova IN, Bocharov AV, Vishnyakova TG, Kurlander R, Chen Z, et al. (2010) CD36 is a novel serum amyloid A (SAA) receptor mediating SAA binding and SAA-induced signaling in human and rodent cells. J Biol Chem 285: 8492-8506.
    • (2010) J Biol Chem , vol.285 , pp. 8492-8506
    • Baranova, I.N.1    Bocharov, A.V.2    Vishnyakova, T.G.3    Kurlander, R.4    Chen, Z.5
  • 37
    • 2442443134 scopus 로고    scopus 로고
    • Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation
    • Foell D, Frosch M, Sorg C, Roth J, (2004) Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clinica Chimica Acta 344: 37-51.
    • (2004) Clinica Chimica Acta , vol.344 , pp. 37-51
    • Foell, D.1    Frosch, M.2    Sorg, C.3    Roth, J.4
  • 38
    • 0029828512 scopus 로고    scopus 로고
    • Phosphorylation of myeloid-related proteins MRP-14 and MRP-8 during human neutrophil activation
    • Guignard F, Mauel J, Markert M, (1996) Phosphorylation of myeloid-related proteins MRP-14 and MRP-8 during human neutrophil activation. Eur J Biochem 241: 265-271.
    • (1996) Eur J Biochem , vol.241 , pp. 265-271
    • Guignard, F.1    Mauel, J.2    Markert, M.3
  • 40
    • 0344896680 scopus 로고    scopus 로고
    • The regulation of EN-RAGE (S100A12) gene expression in human THP-1 macrophages
    • Hasegawa T, Kosaki A, Kimura T, Matsubara H, Mori Y, et al. (2003) The regulation of EN-RAGE (S100A12) gene expression in human THP-1 macrophages. Atherosclerosis 171: 211-218.
    • (2003) Atherosclerosis , vol.171 , pp. 211-218
    • Hasegawa, T.1    Kosaki, A.2    Kimura, T.3    Matsubara, H.4    Mori, Y.5
  • 41
    • 68949085246 scopus 로고    scopus 로고
    • Pleiotropic roles of S100A12 in coronary atherosclerotic plaque formation and rupture
    • Goyette J, Yan WX, Yamen E, Chung YM, Lim SY, et al. (2009) Pleiotropic roles of S100A12 in coronary atherosclerotic plaque formation and rupture. J Immunol 183: 593-603.
    • (2009) J Immunol , vol.183 , pp. 593-603
    • Goyette, J.1    Yan, W.X.2    Yamen, E.3    Chung, Y.M.4    Lim, S.Y.5
  • 42
    • 33845948230 scopus 로고    scopus 로고
    • S100A12 provokes mast cell activation: a potential amplification pathway in asthma and innate immunity
    • Yang Z, Yan WX, Cai H, Tedla N, Armishaw C, et al. (2007) S100A12 provokes mast cell activation: a potential amplification pathway in asthma and innate immunity. J Allergy Clin Immunol 119: 106-114.
    • (2007) J Allergy Clin Immunol , vol.119 , pp. 106-114
    • Yang, Z.1    Yan, W.X.2    Cai, H.3    Tedla, N.4    Armishaw, C.5
  • 43
    • 0038576426 scopus 로고    scopus 로고
    • Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease
    • Foell D, Kucharzik T, Kraft M, Vogl T, Sorg C, et al. (2003) Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease. Gut 52: 847-853.
    • (2003) Gut , vol.52 , pp. 847-853
    • Foell, D.1    Kucharzik, T.2    Kraft, M.3    Vogl, T.4    Sorg, C.5
  • 44
    • 35148869758 scopus 로고    scopus 로고
    • Serum and mucosal S100 proteins, calprotectin (S100A8/S100A9) and S100A12, are elevated at diagnosis in children with inflammatory bowel disease
    • Leach ST, Yang Z, Messina I, Song C, Geczy CL, et al. (2007) Serum and mucosal S100 proteins, calprotectin (S100A8/S100A9) and S100A12, are elevated at diagnosis in children with inflammatory bowel disease. Scand J Gastroenterol 42: 1321-1331.
    • (2007) Scand J Gastroenterol , vol.42 , pp. 1321-1331
    • Leach, S.T.1    Yang, Z.2    Messina, I.3    Song, C.4    Geczy, C.L.5
  • 45
    • 10444270993 scopus 로고    scopus 로고
    • Proinflammatory S100 proteins in arthritis and autoimmune disease
    • Foell D, Roth J, (2004) Proinflammatory S100 proteins in arthritis and autoimmune disease. Arthritis Rheum 50: 3762-3771.
    • (2004) Arthritis Rheum , vol.50 , pp. 3762-3771
    • Foell, D.1    Roth, J.2
  • 46
    • 0242500281 scopus 로고    scopus 로고
    • S100A12 (EN-RAGE) in monitoring Kawasaki disease
    • Foell D, Ichida F, Vogl T, Yu X, Chen R, et al. (2003) S100A12 (EN-RAGE) in monitoring Kawasaki disease. Lancet 361: 1270-1272.
    • (2003) Lancet , vol.361 , pp. 1270-1272
    • Foell, D.1    Ichida, F.2    Vogl, T.3    Yu, X.4    Chen, R.5
  • 47
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides
    • Hofmann MA, Drury S, Fu C, Qu W, Taguchi A, et al. (1999) RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97: 889-901.
    • (1999) Cell , vol.97 , pp. 889-901
    • Hofmann, M.A.1    Drury, S.2    Fu, C.3    Qu, W.4    Taguchi, A.5
  • 48
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar CM, Whitehead AS, (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
  • 49
    • 45149117428 scopus 로고    scopus 로고
    • Mast cell and monocyte recruitment by S100A12 and its hinge domain
    • Yan WX, Armishaw C, Goyette J, Yang Z, Cai H, et al. (2008) Mast cell and monocyte recruitment by S100A12 and its hinge domain. J Biol Chem 283: 13035-13043.
    • (2008) J Biol Chem , vol.283 , pp. 13035-13043
    • Yan, W.X.1    Armishaw, C.2    Goyette, J.3    Yang, Z.4    Cai, H.5
  • 50
    • 79955760681 scopus 로고    scopus 로고
    • Transgenic expression of human S100A12 induces structural airway abnormalities and limited lung inflammation in a mouse model of allergic inflammation
    • Hofmann Bowman MA, Heydemann A, Gawdzik J, Shilling RA, Camoretti-Mercado B, (2011) Transgenic expression of human S100A12 induces structural airway abnormalities and limited lung inflammation in a mouse model of allergic inflammation. Clin Exp Allergy 41: 878-889.
    • (2011) Clin Exp Allergy , vol.41 , pp. 878-889
    • Hofmann Bowman, M.A.1    Heydemann, A.2    Gawdzik, J.3    Shilling, R.A.4    Camoretti-Mercado, B.5
  • 51
    • 38149083650 scopus 로고    scopus 로고
    • Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1
    • Bjorkman L, Karlsson J, Karlsson A, Rabiet MJ, Boulay F, et al. (2008) Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1. J Leukoc Biol 83: 245-253.
    • (2008) J Leukoc Biol , vol.83 , pp. 245-253
    • Bjorkman, L.1    Karlsson, J.2    Karlsson, A.3    Rabiet, M.J.4    Boulay, F.5
  • 53
    • 29244446785 scopus 로고    scopus 로고
    • S100A8 and S100A9 in human arterial wall: implications for atherogenesis
    • McCormick MM, Rahimi F, Bobryshev YV, Gaus K, Zreiqat H, et al. (2005) S100A8 and S100A9 in human arterial wall: implications for atherogenesis. J Biol Chem 280: 41521-41529.
    • (2005) J Biol Chem , vol.280 , pp. 41521-41529
    • McCormick, M.M.1    Rahimi, F.2    Bobryshev, Y.V.3    Gaus, K.4    Zreiqat, H.5
  • 54
    • 0031455120 scopus 로고    scopus 로고
    • On the cytoprotective role of ferritin in macrophages and its ability to enhance lysosomal stability
    • Garner B, Li W, Roberg K, Brunk UT, (1997) On the cytoprotective role of ferritin in macrophages and its ability to enhance lysosomal stability. Free Radic Res 27: 487-500.
    • (1997) Free Radic Res , vol.27 , pp. 487-500
    • Garner, B.1    Li, W.2    Roberg, K.3    Brunk, U.T.4
  • 56
    • 63849227423 scopus 로고    scopus 로고
    • Serum amyloid A may potentiate prothrombotic and proinflammatory events in acute coronary syndromes
    • Song C, Shen Y, Yamen E, Hsu K, Yan W, et al. (2009) Serum amyloid A may potentiate prothrombotic and proinflammatory events in acute coronary syndromes. Atherosclerosis 202: 596-604.
    • (2009) Atherosclerosis , vol.202 , pp. 596-604
    • Song, C.1    Shen, Y.2    Yamen, E.3    Hsu, K.4    Yan, W.5
  • 57
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M, (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 58
    • 33746215231 scopus 로고    scopus 로고
    • Active ERK contributes to protein translation by preventing JNK-dependent inhibition of protein Phosphatase 1
    • Monick MM, Powers LS, Gross TJ, Flaherty DM, Barrett CW, et al. (2006) Active ERK contributes to protein translation by preventing JNK-dependent inhibition of protein Phosphatase 1. J Immunol 177: 1636-1645.
    • (2006) J Immunol , vol.177 , pp. 1636-1645
    • Monick, M.M.1    Powers, L.S.2    Gross, T.J.3    Flaherty, D.M.4    Barrett, C.W.5
  • 59
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K, Krause KH, (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87: 245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 60
    • 0038362437 scopus 로고    scopus 로고
    • Superoxide dismutases from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity
    • Ahmed H, Schott EJ, Gauthier JD, Vasta GR, (2003) Superoxide dismutases from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity. Anal Biochem 318: 132-141.
    • (2003) Anal Biochem , vol.318 , pp. 132-141
    • Ahmed, H.1    Schott, E.J.2    Gauthier, J.D.3    Vasta, G.R.4
  • 61
    • 0025947544 scopus 로고
    • Discordant expression of tissue factor antigen and procoagulant activity on human monocytes activated with LPS and low dose cycloheximide
    • Walsh JD, Geczy CL, (1991) Discordant expression of tissue factor antigen and procoagulant activity on human monocytes activated with LPS and low dose cycloheximide. Thromb Haemost 66: 552-558.
    • (1991) Thromb Haemost , vol.66 , pp. 552-558
    • Walsh, J.D.1    Geczy, C.L.2
  • 62
    • 0028322179 scopus 로고
    • Cellular mechanisms for the activation of blood coagulation
    • Geczy CL, (1994) Cellular mechanisms for the activation of blood coagulation. Int Rev Cytol 152: 49-108.
    • (1994) Int Rev Cytol , vol.152 , pp. 49-108
    • Geczy, C.L.1
  • 63
    • 2942622299 scopus 로고    scopus 로고
    • Probing the S100 protein family through genomic and functional analysis
    • Ravasi T, Hsu K, Goyette J, Schroder K, Yang Z, et al. (2004) Probing the S100 protein family through genomic and functional analysis. Genomics 84: 10-22.
    • (2004) Genomics , vol.84 , pp. 10-22
    • Ravasi, T.1    Hsu, K.2    Goyette, J.3    Schroder, K.4    Yang, Z.5
  • 64
    • 78249268525 scopus 로고    scopus 로고
    • S100A8 causes a shift toward expression of activatory Fcγ receptors on macrophages via toll-like receptor 4 and regulates Fcγ receptor expression in synovium during chronic experimental arthritis
    • van Lent PL, Grevers LC, Schelbergen R, Blom A, Geurts J, et al. (2010) S100A8 causes a shift toward expression of activatory Fcγ receptors on macrophages via toll-like receptor 4 and regulates Fcγ receptor expression in synovium during chronic experimental arthritis. Arthritis Rheum 62: 3353-3364.
    • (2010) Arthritis Rheum , vol.62 , pp. 3353-3364
    • van Lent, P.L.1    Grevers, L.C.2    Schelbergen, R.3    Blom, A.4    Geurts, J.5
  • 65
    • 65949111512 scopus 로고    scopus 로고
    • Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides
    • Bjork P, Bjork A, Vogl T, Stenstrom M, Liberg D, et al. (2009) Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides. PLoS Biol 7: 800-812.
    • (2009) PLoS Biol , vol.7 , pp. 800-812
    • Bjork, P.1    Bjork, A.2    Vogl, T.3    Stenstrom, M.4    Liberg, D.5
  • 66
    • 34948900275 scopus 로고    scopus 로고
    • Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock
    • Vogl T, Tenbrock K, Ludwig S, Leukert N, Ehrhardt C, et al. (2007) Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock. Nat Med 13: 1042-1049.
    • (2007) Nat Med , vol.13 , pp. 1042-1049
    • Vogl, T.1    Tenbrock, K.2    Ludwig, S.3    Leukert, N.4    Ehrhardt, C.5
  • 67
    • 34548036986 scopus 로고    scopus 로고
    • The S100A8/A9 heterodimer amplifies proinflammatory cytokine production by macrophages via activation of nuclear factor kappa B and p38 mitogen-activated protein kinase in rheumatoid arthritis
    • Sunahori K, Yamamura M, Yamana J, Takasugi K, Kawashima M, et al. (2006) The S100A8/A9 heterodimer amplifies proinflammatory cytokine production by macrophages via activation of nuclear factor kappa B and p38 mitogen-activated protein kinase in rheumatoid arthritis. Arthritis Res Ther 8: R69.
    • (2006) Arthritis Res Ther , vol.8
    • Sunahori, K.1    Yamamura, M.2    Yamana, J.3    Takasugi, K.4    Kawashima, M.5
  • 68
    • 0033952703 scopus 로고    scopus 로고
    • TLR4: central component of the sole mammalian LPS sensor
    • Beutler B, (2000) TLR4: central component of the sole mammalian LPS sensor. Curr Opin Immunol 12: 20-26.
    • (2000) Curr Opin Immunol , vol.12 , pp. 20-26
    • Beutler, B.1
  • 69
    • 55549128598 scopus 로고    scopus 로고
    • The S100A8-serum amyloid A3-TLR4 paracrine cascade establishes a pre-metastatic phase
    • Hiratsuka S, Watanabe A, Sakurai Y, Akashi-Takamura S, Ishibashi S, et al. (2008) The S100A8-serum amyloid A3-TLR4 paracrine cascade establishes a pre-metastatic phase. Nat Cell Biol 10: 1349-1355.
    • (2008) Nat Cell Biol , vol.10 , pp. 1349-1355
    • Hiratsuka, S.1    Watanabe, A.2    Sakurai, Y.3    Akashi-Takamura, S.4    Ishibashi, S.5
  • 70
    • 22844449992 scopus 로고    scopus 로고
    • Differential involvement of calmodulin-dependent protein kinase II-activated AP-1 and c-Jun N-terminal kinase-activated EGR-1 signaling pathways in tumor necrosis factor-α and lipopolysaccharide-induced CD44 expression in human monocytic cells
    • Mishra JP, Mishra S, Gee K, Kumar A, (2005) Differential involvement of calmodulin-dependent protein kinase II-activated AP-1 and c-Jun N-terminal kinase-activated EGR-1 signaling pathways in tumor necrosis factor-α and lipopolysaccharide-induced CD44 expression in human monocytic cells. J Biol Chem 280: 26825-26837.
    • (2005) J Biol Chem , vol.280 , pp. 26825-26837
    • Mishra, J.P.1    Mishra, S.2    Gee, K.3    Kumar, A.4
  • 71
    • 33745230802 scopus 로고    scopus 로고
    • Serum amyloid A induces contrary immune responses via formyl peptide receptor-like 1 in human monocytes
    • Lee HY, Kim MK, Park KS, Shin EH, Jo SH, et al. (2006) Serum amyloid A induces contrary immune responses via formyl peptide receptor-like 1 in human monocytes. Molecular Pharmacology 70: 241-248.
    • (2006) Molecular Pharmacology , vol.70 , pp. 241-248
    • Lee, H.Y.1    Kim, M.K.2    Park, K.S.3    Shin, E.H.4    Jo, S.H.5
  • 72
    • 0027933081 scopus 로고
    • The prognostic value of C-reactive protein and serum amyloid A protein in severe unstable angina
    • Liuzzo G, Biasucci LM, Gallimore JR, Grillo RL, Rebuzzi AG, et al. (1994) The prognostic value of C-reactive protein and serum amyloid A protein in severe unstable angina. N Engl J Med 331: 417-424.
    • (1994) N Engl J Med , vol.331 , pp. 417-424
    • Liuzzo, G.1    Biasucci, L.M.2    Gallimore, J.R.3    Grillo, R.L.4    Rebuzzi, A.G.5
  • 73
    • 84859093135 scopus 로고    scopus 로고
    • High-density lipoprotein loses its anti-inflammatory capacity by accumulation of pro-inflammatory-serum amyloid A
    • Tolle M, Huang T, Schuchardt M, Jankowski V, Prufer N, et al. (2012) High-density lipoprotein loses its anti-inflammatory capacity by accumulation of pro-inflammatory-serum amyloid A. Cardiovasc Res. 94: 154-162.
    • (2012) Cardiovasc Res , vol.94 , pp. 154-162
    • Tolle, M.1    Huang, T.2    Schuchardt, M.3    Jankowski, V.4    Prufer, N.5
  • 74
    • 84865308706 scopus 로고    scopus 로고
    • Local production of serum amyloid a is implicated in the induction of macrophage chemoattractants in Schwann cells during wallerian degeneration of peripheral nerves
    • Jang SY, Shin YK, Lee HY, Park JY, Suh DJ, et al. (2012) Local production of serum amyloid a is implicated in the induction of macrophage chemoattractants in Schwann cells during wallerian degeneration of peripheral nerves. Glia 60: 1619-1628.
    • (2012) Glia , vol.60 , pp. 1619-1628
    • Jang, S.Y.1    Shin, Y.K.2    Lee, H.Y.3    Park, J.Y.4    Suh, D.J.5
  • 75
    • 79960386345 scopus 로고    scopus 로고
    • Serum amyloid A activates the NLRP3 inflammasome and promotes Th17 allergic asthma in mice
    • Ather JL, Ckless K, Martin R, Foley KL, Suratt BT, et al. (2011) Serum amyloid A activates the NLRP3 inflammasome and promotes Th17 allergic asthma in mice. J Immunol 187: 64-73.
    • (2011) J Immunol , vol.187 , pp. 64-73
    • Ather, J.L.1    Ckless, K.2    Martin, R.3    Foley, K.L.4    Suratt, B.T.5
  • 76
    • 77952721659 scopus 로고    scopus 로고
    • Carboxylated N-glycans on RAGE promote S100A12 binding and signaling
    • Srikrishna G, Nayak J, Weigle B, Temme A, Foell D, et al. (2010) Carboxylated N-glycans on RAGE promote S100A12 binding and signaling. J Cell Biochem 110: 645-659.
    • (2010) J Cell Biochem , vol.110 , pp. 645-659
    • Srikrishna, G.1    Nayak, J.2    Weigle, B.3    Temme, A.4    Foell, D.5
  • 77
    • 77649180564 scopus 로고    scopus 로고
    • Scavenger receptors are associated with cellular interactions of S100A12 in vitro and in vivo
    • Hoppmann S, Steinbach J, Pietzsch J, (2010) Scavenger receptors are associated with cellular interactions of S100A12 in vitro and in vivo. Int J Biochem Cell Biol 42: 651-661.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 651-661
    • Hoppmann, S.1    Steinbach, J.2    Pietzsch, J.3
  • 78
    • 79551504491 scopus 로고    scopus 로고
    • S100A12 in vascular smooth muscle accelerates vascular calcification in apolipoprotein E-null mice by activating an osteogenic gene regulatory program
    • Hofmann Bowman MA, Gawdzik J, Bukhari U, Husain AN, Toth PT, et al. (2011) S100A12 in vascular smooth muscle accelerates vascular calcification in apolipoprotein E-null mice by activating an osteogenic gene regulatory program. Arterioscler Thromb Vasc Biol 31: 337-344.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , pp. 337-344
    • Hofmann Bowman, M.A.1    Gawdzik, J.2    Bukhari, U.3    Husain, A.N.4    Toth, P.T.5
  • 79
    • 67349129131 scopus 로고    scopus 로고
    • S100B's double life: intracellular regulator and extracellular signal
    • Donato R, Sorci G, Riuzzi F, Arcuri C, Bianchi R, et al. (2009) S100B's double life: intracellular regulator and extracellular signal. Biochim Biophys Acta 1793: 1008-1022.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1008-1022
    • Donato, R.1    Sorci, G.2    Riuzzi, F.3    Arcuri, C.4    Bianchi, R.5
  • 80
    • 81555205312 scopus 로고    scopus 로고
    • Inflammation-associated S100 proteins: new mechanisms that regulate function
    • Goyette J, Geczy CL, (2011) Inflammation-associated S100 proteins: new mechanisms that regulate function. Amino Acids 41: 821-842.
    • (2011) Amino Acids , vol.41 , pp. 821-842
    • Goyette, J.1    Geczy, C.L.2
  • 81
    • 67651160306 scopus 로고    scopus 로고
    • The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation
    • Moroz OV, Blagova EV, Wilkinson AJ, Wilson KS, Bronstein IB, (2009) The crystal structures of human S100A12 in apo form and in complex with zinc: new insights into S100A12 oligomerisation. J Mol Biol 391: 536-551.
    • (2009) J Mol Biol , vol.391 , pp. 536-551
    • Moroz, O.V.1    Blagova, E.V.2    Wilkinson, A.J.3    Wilson, K.S.4    Bronstein, I.B.5
  • 82
    • 34248165082 scopus 로고    scopus 로고
    • Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A
    • Wang L, Colon W, (2007) Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry. 46: 5562-5569.
    • (2007) Biochemistry , vol.46 , pp. 5562-5569
    • Wang, L.1    Colon, W.2
  • 83
    • 0032453876 scopus 로고    scopus 로고
    • New perspectives on S100 proteins: a multi-functional Ca2+-, Zn2+- and Cu2+-binding protein family
    • Heizmann CW, Cox JA, (1998) New perspectives on S100 proteins: a multi-functional Ca2+-, Zn2+- and Cu2+-binding protein family. Biometals 11: 383-397.
    • (1998) Biometals , vol.11 , pp. 383-397
    • Heizmann, C.W.1    Cox, J.A.2
  • 84
    • 70349767925 scopus 로고    scopus 로고
    • Defining lipid-binding regions of human serum amyloid A using its fragment peptides
    • Ohta S, Tanaka M, Sakakura K, Kawakami T, Aimoto S, et al. (2009) Defining lipid-binding regions of human serum amyloid A using its fragment peptides. Chem Phys Lipids 162: 62-68.
    • (2009) Chem Phys Lipids , vol.162 , pp. 62-68
    • Ohta, S.1    Tanaka, M.2    Sakakura, K.3    Kawakami, T.4    Aimoto, S.5
  • 85
    • 33847296039 scopus 로고    scopus 로고
    • Posttranslationally modified proteins as mediators of sustained intestinal inflammation
    • Andrassy M, Igwe J, Autschbach F, Volz C, Remppis A, et al. (2006) Posttranslationally modified proteins as mediators of sustained intestinal inflammation. Am J Pathol 169: 1223-1237.
    • (2006) Am J Pathol , vol.169 , pp. 1223-1237
    • Andrassy, M.1    Igwe, J.2    Autschbach, F.3    Volz, C.4    Remppis, A.5
  • 86
    • 45149098188 scopus 로고    scopus 로고
    • S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products
    • Boyd JH, Kan B, Roberts H, Wang Y, Walley KR, (2008) S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products. Circ Res 102: 1239-1246.
    • (2008) Circ Res , vol.102 , pp. 1239-1246
    • Boyd, J.H.1    Kan, B.2    Roberts, H.3    Wang, Y.4    Walley, K.R.5
  • 87
    • 38349052450 scopus 로고    scopus 로고
    • S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway
    • Ghavami S, Rashedi I, Dattilo BM, Eshraghi M, Chazin WJ, et al. (2008) S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway. J Leukoc Biol 83: 1484-1492.
    • (2008) J Leukoc Biol , vol.83 , pp. 1484-1492
    • Ghavami, S.1    Rashedi, I.2    Dattilo, B.M.3    Eshraghi, M.4    Chazin, W.J.5
  • 88
    • 67649208478 scopus 로고    scopus 로고
    • The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer
    • Ehrchen JM, Sunderkotter C, Foell D, Vogl T, Roth J, (2009) The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer. J Leukoc Biol 86: 557-566.
    • (2009) J Leukoc Biol , vol.86 , pp. 557-566
    • Ehrchen, J.M.1    Sunderkotter, C.2    Foell, D.3    Vogl, T.4    Roth, J.5
  • 89
    • 77953233075 scopus 로고    scopus 로고
    • The Toll-like receptor 4 ligands Mrp8 and Mrp14 are crucial in the development of autoreactive CD8+ T cells
    • Loser K, Vogl T, Voskort M, Lueken A, Kupas V, et al. (2010) The Toll-like receptor 4 ligands Mrp8 and Mrp14 are crucial in the development of autoreactive CD8+ T cells. Nat Med 16: 713-717.
    • (2010) Nat Med , vol.16 , pp. 713-717
    • Loser, K.1    Vogl, T.2    Voskort, M.3    Lueken, A.4    Kupas, V.5
  • 90
    • 0035830423 scopus 로고    scopus 로고
    • Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells
    • Kerkhoff C, Sorg C, Tandon NN, Nacken W, (2001) Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry 40: 241-248.
    • (2001) Biochemistry , vol.40 , pp. 241-248
    • Kerkhoff, C.1    Sorg, C.2    Tandon, N.N.3    Nacken, W.4
  • 91
    • 0034746919 scopus 로고    scopus 로고
    • NF-κB: a key role in inflammatory diseases
    • Tak PP, Firestein GS, (2001) NF-κB: a key role in inflammatory diseases. J Clin Invest 107: 7-11.
    • (2001) J Clin Invest , vol.107 , pp. 7-11
    • Tak, P.P.1    Firestein, G.S.2
  • 92
    • 11144252845 scopus 로고    scopus 로고
    • PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway
    • Dokladda K, Green KA, Pan DA, Hardie DG, (2005) PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway. FEBS Lett 579: 236-240.
    • (2005) FEBS Lett , vol.579 , pp. 236-240
    • Dokladda, K.1    Green, K.A.2    Pan, D.A.3    Hardie, D.G.4
  • 93
    • 0038304819 scopus 로고    scopus 로고
    • The Raf/MEK inhibitor PD98059 enhances ERK1/2 phosphorylation mediated by peroxynitrite via enforced mitochondrial formation of reactive oxygen species
    • Cerioni L, Palomba L, Cantoni O, (2003) The Raf/MEK inhibitor PD98059 enhances ERK1/2 phosphorylation mediated by peroxynitrite via enforced mitochondrial formation of reactive oxygen species. FEBS Lett 547: 92-96.
    • (2003) FEBS Lett , vol.547 , pp. 92-96
    • Cerioni, L.1    Palomba, L.2    Cantoni, O.3
  • 94
    • 61849153316 scopus 로고    scopus 로고
    • SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels
    • Lorenz U, (2009) SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels. Immunol Rev 228: 342-359.
    • (2009) Immunol Rev , vol.228 , pp. 342-359
    • Lorenz, U.1
  • 95
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: a gene family for control of MAP kinase function
    • Camps M, Nichols A, Arkinstall S, (2000) Dual specificity phosphatases: a gene family for control of MAP kinase function. The FASEB J 14: 6-16.
    • (2000) The FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 96
    • 0032557632 scopus 로고    scopus 로고
    • Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
    • Camps M, Nichols A, Gillieron C, Antonsson B, Muda M, et al. (1998) Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 280: 1262-1265.
    • (1998) Science , vol.280 , pp. 1262-1265
    • Camps, M.1    Nichols, A.2    Gillieron, C.3    Antonsson, B.4    Muda, M.5
  • 97
    • 0032534791 scopus 로고    scopus 로고
    • PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
    • Pulido R, Zuniga A, Ullrich A, (1998) PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J 17: 7337-7350.
    • (1998) EMBO J , vol.17 , pp. 7337-7350
    • Pulido, R.1    Zuniga, A.2    Ullrich, A.3
  • 98
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, Honda SI, Maeda S, Chang L, Hirata H, et al. (2005) Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120: 649-661.
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.I.2    Maeda, S.3    Chang, L.4    Hirata, H.5
  • 99
    • 44449086957 scopus 로고    scopus 로고
    • Redox-regulation of Erk1/2-directed phosphatase by reactive oxygen species: Role in signaling TPA-induced growth arrest in ML-1 cells
    • Traore K, Sharma R, Thimmulappa RK, Watson WH, Biswal S, et al. (2008) Redox-regulation of Erk1/2-directed phosphatase by reactive oxygen species: Role in signaling TPA-induced growth arrest in ML-1 cells. J Cell Physiol 216: 276-285.
    • (2008) J Cell Physiol , vol.216 , pp. 276-285
    • Traore, K.1    Sharma, R.2    Thimmulappa, R.K.3    Watson, W.H.4    Biswal, S.5
  • 101
    • 0032213207 scopus 로고    scopus 로고
    • Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils
    • Gatt ME, Urieli-Shoval S, Preciado-Patt L, Fridkin M, Calco S, et al. (1998) Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils. J Lab Clin Med 132: 414-420.
    • (1998) J Lab Clin Med , vol.132 , pp. 414-420
    • Gatt, M.E.1    Urieli-Shoval, S.2    Preciado-Patt, L.3    Fridkin, M.4    Calco, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.