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Volumn 194, Issue 10, 2015, Pages 4891-4900

Ex vivo and in vitro effect of serum amyloid a in the induction of macrophage M2 markers and efferocytosis of apoptotic neutrophils

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; ARGINASE 1; CELL PROTEIN; FIZZ 1 PROTEIN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERFERON REGULATORY FACTOR 4; INTERLEUKIN 1 RECEPTOR; INTERLEUKIN 10; INTERLEUKIN 12P40; INTERLEUKIN 23P19; MRC1 PROTEIN; MYELOID DIFFERENTIATION FACTOR 88; RAC1 PROTEIN; SERUM AMYLOID A; SMALL INTERFERING RNA; STAT6 PROTEIN; THYMUS AND ACTIVATION REGULATED CHEMOKINE; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG; YM1 PROTEIN;

EID: 84929095853     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1402164     Document Type: Article
Times cited : (72)

References (50)
  • 1
    • 0037265240 scopus 로고    scopus 로고
    • Alternative activation of macrophages
    • Gordon, S. 2003. Alternative activation of macrophages. Nat. Rev. Immunol. 3: 23-35.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 23-35
    • Gordon, S.1
  • 3
    • 33750813483 scopus 로고    scopus 로고
    • Transcriptional profiling of the human monocyte-to-macrophage differentiation and polarization: New molecules and patterns of gene expression
    • Martinez, F. O., S. Gordon, M. Locati, and A. Mantovani. 2006. Transcriptional profiling of the human monocyte-to-macrophage differentiation and polarization: new molecules and patterns of gene expression. J. Immunol. 177: 7303-7311.
    • (2006) J. Immunol. , vol.177 , pp. 7303-7311
    • Martinez, F.O.1    Gordon, S.2    Locati, M.3    Mantovani, A.4
  • 4
    • 56749174940 scopus 로고    scopus 로고
    • Exploring the full spectrum of macrophage activation
    • Mosser, D. M., and J. P. Edwards. 2008. Exploring the full spectrum of macrophage activation. Nat. Rev. Immunol. 8: 958-969.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 958-969
    • Mosser, D.M.1    Edwards, J.P.2
  • 5
    • 56149103896 scopus 로고    scopus 로고
    • Macrophage polarization in bacterial infections
    • Benoit, M., B. Desnues, and J. L. Mege. 2008. Macrophage polarization in bacterial infections. J. Immunol. 181: 3733-3739.
    • (2008) J. Immunol. , vol.181 , pp. 3733-3739
    • Benoit, M.1    Desnues, B.2    Mege, J.L.3
  • 7
    • 7644231561 scopus 로고    scopus 로고
    • The chemokine system in diverse forms of macrophage activation and polarization
    • Mantovani, A., A. Sica, S. Sozzani, P. Allavena, A. Vecchi, and M. Locati. 2004. The chemokine system in diverse forms of macrophage activation and polarization. Trends Immunol. 25: 677-686.
    • (2004) Trends Immunol. , vol.25 , pp. 677-686
    • Mantovani, A.1    Sica, A.2    Sozzani, S.3    Allavena, P.4    Vecchi, A.5    Locati, M.6
  • 8
    • 84871076444 scopus 로고    scopus 로고
    • Macrophage plasticity and polarization in tissue repair and remodelling
    • Mantovani, A., S. K. Biswas, M. R. Galdiero, A. Sica, and M. Locati. 2013. Macrophage plasticity and polarization in tissue repair and remodelling. J. Pathol. 229: 176-185.
    • (2013) J. Pathol. , vol.229 , pp. 176-185
    • Mantovani, A.1    Biswas, S.K.2    Galdiero, M.R.3    Sica, A.4    Locati, M.5
  • 9
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan, C. 2006. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6: 173-182.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 173-182
    • Nathan, C.1
  • 11
    • 66549126476 scopus 로고    scopus 로고
    • Neutrophil apoptosis and the resolution of infection
    • Kennedy, A. D., and F. R. DeLeo. 2009. Neutrophil apoptosis and the resolution of infection. Immunol. Res. 43: 25-61.
    • (2009) Immunol. Res. , vol.43 , pp. 25-61
    • Kennedy, A.D.1    DeLeo, F.R.2
  • 12
    • 78751508599 scopus 로고    scopus 로고
    • Regulation of steady-state neutrophil homeostasis by macrophages
    • Gordy, C., H. Pua, G. D. Sempowski, and Y. W. He. 2011. Regulation of steady-state neutrophil homeostasis by macrophages. Blood 117: 618-629.
    • (2011) Blood , vol.117 , pp. 618-629
    • Gordy, C.1    Pua, H.2    Sempowski, G.D.3    He, Y.W.4
  • 14
    • 78649469767 scopus 로고    scopus 로고
    • PPARγ activation normalizes resolution of acute sterile inflammation in murine chronic granulomatous disease
    • Fernandez-Boyanapalli, R., S. C. Frasch, D. W. Riches, R. W. Vandivier, P. M. Henson, and D. L. Bratton. 2010. PPARγ activation normalizes resolution of acute sterile inflammation in murine chronic granulomatous disease. Blood 116: 4512-4522.
    • (2010) Blood , vol.116 , pp. 4512-4522
    • Fernandez-Boyanapalli, R.1    Frasch, S.C.2    Riches, D.W.3    Vandivier, R.W.4    Henson, P.M.5    Bratton, D.L.6
  • 15
    • 78851471818 scopus 로고    scopus 로고
    • Saturated-efferocytosis generates pro-resolving CD11b low macrophages: Modulation by resolvins and glucocorticoids
    • Schif-Zuck, S., N. Gross, S. Assi, R. Rostoker, C. N. Serhan, and A. Ariel. 2011. Saturated-efferocytosis generates pro-resolving CD11b low macrophages: modulation by resolvins and glucocorticoids. Eur. J. Immunol. 41: 366-379.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 366-379
    • Schif-Zuck, S.1    Gross, N.2    Assi, S.3    Rostoker, R.4    Serhan, C.N.5    Ariel, A.6
  • 16
    • 0002939244 scopus 로고    scopus 로고
    • Acute phase response
    • 3rd Ed. J. I. Gallin, and R. Snyderman, eds. Lippincott Willams & Wilkins, Philadelphia
    • Kushner, I., and D. Rzewnicki. 1999. Acute phase response. In Inflammation: Basic principles and clinical correlates, 3rd Ed. J. I. Gallin, and R. Snyderman, eds. Lippincott Willams & Wilkins, Philadelphia, p. 317-329.
    • (1999) Inflammation: Basic Principles and Clinical Correlates , pp. 317-329
    • Kushner, I.1    Rzewnicki, D.2
  • 17
    • 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
  • 18
    • 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
  • 19
    • 17744373052 scopus 로고    scopus 로고
    • Acute-phase serum amyloid A production by rheumatoid arthritis synovial tissue
    • O'Hara, R., E. P. Murphy, A. S. Whitehead, O. FitzGerald, and B. Bresnihan. 2000. Acute-phase serum amyloid A production by rheumatoid arthritis synovial tissue. Arthritis Res. 2: 142-144.
    • (2000) Arthritis Res. , vol.2 , pp. 142-144
    • O'Hara, R.1    Murphy, E.P.2    Whitehead, A.S.3    FitzGerald, O.4    Bresnihan, B.5
  • 20
    • 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
  • 21
    • 0019969508 scopus 로고
    • Serum amyloid-A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis
    • De Beer, F. C., R. K. Mallya, E. A. Fagan, J. G. Lanham, G. R. Hughes, and M. B. Pepys. 1982. Serum amyloid-A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis. Lancet 2: 231-234.
    • (1982) Lancet , vol.2 , pp. 231-234
    • De Beer, F.C.1    Mallya, R.K.2    Fagan, E.A.3    Lanham, J.G.4    Hughes, G.R.5    Pepys, M.B.6
  • 22
    • 0028578242 scopus 로고
    • Serum amyloid A protein in patients with non-insulin-dependent diabetes mellitus
    • Kumon, Y., T. Suehiro, T. Itahara, Y. Ikeda, and K. Hashimoto. 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
  • 23
    • 23444460848 scopus 로고
    • Serum amyloid A is a chemoattractant: Induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes
    • Badolato, R., J. M. Wang, W. J. Murphy, A. R. Lloyd, D. F. Michiel, L. L. Bausserman, D. J. Kelvin, and J. J. Oppenheim. 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    Bausserman, L.L.6    Kelvin, D.J.7    Oppenheim, J.J.8
  • 24
    • 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
  • 25
    • 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
  • 26
    • 33748499140 scopus 로고    scopus 로고
    • Serum amyloid A is an endogenous ligand that differentially induces IL-12 and IL-23
    • He, R., L. W. Shepard, J. Chen, Z. K. Pan, and R. D. Ye. 2006. Serum amyloid A is an endogenous ligand that differentially induces IL-12 and IL-23. J. Immunol. 177: 4072-4079.
    • (2006) J. Immunol. , vol.177 , pp. 4072-4079
    • He, R.1    Shepard, L.W.2    Chen, J.3    Pan, Z.K.4    Ye, R.D.5
  • 27
    • 58849134296 scopus 로고    scopus 로고
    • Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2
    • He, R. L., J. Zhou, C. Z. Hanson, J. Chen, N. Cheng, and R. D. Ye. 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    Ye, R.D.6
  • 28
    • 47949085624 scopus 로고    scopus 로고
    • Cutting edge: TLR2 is a functional receptor for acute-phase serum amyloid A
    • Cheng, N., R. He, J. Tian, P. P. Ye, and R. D. Ye. 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
    • 84881593949 scopus 로고    scopus 로고
    • Endogenous acute phase serum amyloid A lacks proinflammatory activity, contrasting the two recombinant variants that activate human neutrophils through different receptors
    • Christenson, K., L. Björkman, S. Ahlin, M. Olsson, K. Sjöholm, A. Karlsson, and J. Bylund. 2013. Endogenous acute phase serum amyloid A lacks proinflammatory activity, contrasting the two recombinant variants that activate human neutrophils through different receptors. Front. Immunol. 4: 92.
    • (2013) Front. Immunol. , vol.4 , pp. 92
    • Christenson, K.1    Björkman, L.2    Ahlin, S.3    Olsson, M.4    Sjöholm, K.5    Karlsson, A.6    Bylund, J.7
  • 32
    • 84873101814 scopus 로고    scopus 로고
    • SAA does not induce cytokine production in physiological conditions
    • Kim, M. H., M. C. de Beer, J. M. Wroblewski, N. R. Webb, and F. C. de Beer. 2013. SAA does not induce cytokine production in physiological conditions. Cytokine 61: 506-512.
    • (2013) Cytokine , vol.61 , pp. 506-512
    • Kim, M.H.1    De Beer, M.C.2    Wroblewski, J.M.3    Webb, N.R.4    De Beer, F.C.5
  • 33
    • 77951644229 scopus 로고    scopus 로고
    • A critical role for the g protein-coupled receptor mFPR2 in airway inflammation and immune responses
    • Chen, K., Y. Le, Y. Liu, W. Gong, G. Ying, J. Huang, T. Yoshimura, L. Tessarollo, and J. M. Wang. 2010. A critical role for the g protein-coupled receptor mFPR2 in airway inflammation and immune responses. J. Immunol. 184: 3331-3335.
    • (2010) J. Immunol. , vol.184 , pp. 3331-3335
    • Chen, K.1    Le, Y.2    Liu, Y.3    Gong, W.4    Ying, G.5    Huang, J.6    Yoshimura, T.7    Tessarollo, L.8    Wang, J.M.9
  • 34
    • 58849167699 scopus 로고    scopus 로고
    • The isolation and characterization of murine macrophages
    • Chapter 14: Unit 14.1
    • Zhang, X., R. Goncalves, and D. M. Mosser. 2008. The isolation and characterization of murine macrophages. Curr. Protoc. Immunol. Chapter 14: Unit 14.1. doi:10.1002/0471142735.im1401s83.
    • (2008) Curr. Protoc. Immunol.
    • Zhang, X.1    Goncalves, R.2    Mosser, D.M.3
  • 37
    • 77952865796 scopus 로고    scopus 로고
    • Phagocyte partnership during the onset and resolution of inflammation
    • Soehnlein, O., and L. Lindbom. 2010. Phagocyte partnership during the onset and resolution of inflammation. Nat. Rev. Immunol. 10: 427-439.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 427-439
    • Soehnlein, O.1    Lindbom, L.2
  • 38
    • 0035128074 scopus 로고    scopus 로고
    • Requirement for Rho GTPases and PI 3-kinases during apoptotic cell phagocytosis by macrophages
    • Leverrier, Y., and A. J. Ridley. 2001. Requirement for Rho GTPases and PI 3-kinases during apoptotic cell phagocytosis by macrophages. Curr. Biol. 11: 195-199.
    • (2001) Curr. Biol. , vol.11 , pp. 195-199
    • Leverrier, Y.1    Ridley, A.J.2
  • 41
    • 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
  • 43
    • 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
  • 45
    • 84901775237 scopus 로고    scopus 로고
    • Jmjd3-mediated epigenetic regulation of inflammatory cytokine gene expression in serum amyloid A-stimulated macrophages
    • Yan, Q., L. Sun, Z. Zhu, L. Wang, S. Li, and R. D. Ye. 2014. Jmjd3-mediated epigenetic regulation of inflammatory cytokine gene expression in serum amyloid A-stimulated macrophages. Cell. Signal. 26: 1783-1791.
    • (2014) Cell. Signal. , vol.26 , pp. 1783-1791
    • Yan, Q.1    Sun, L.2    Zhu, Z.3    Wang, L.4    Li, S.5    Ye, R.D.6
  • 46
    • 77956962267 scopus 로고    scopus 로고
    • Regulation of alternative macrophage activation by chromatin remodeling
    • Bowdridge, S., and W. C. Gause. 2010. Regulation of alternative macrophage activation by chromatin remodeling. Nat. Immunol. 11: 879-881.
    • (2010) Nat. Immunol. , vol.11 , pp. 879-881
    • Bowdridge, S.1    Gause, W.C.2
  • 47
    • 77958145336 scopus 로고    scopus 로고
    • Invariant NKT cells modulate the suppressive activity of IL-10-secreting neutrophils differentiated with serum amyloid A
    • De Santo, C., R. Arscott, S. Booth, I. Karydis, M. Jones, R. Asher, M. Salio, M. Middleton, and V. Cerundolo. 2010. Invariant NKT cells modulate the suppressive activity of IL-10-secreting neutrophils differentiated with serum amyloid A. Nat. Immunol. 11: 1039-1046.
    • (2010) Nat. Immunol. , vol.11 , pp. 1039-1046
    • De Santo, C.1    Arscott, R.2    Booth, S.3    Karydis, I.4    Jones, M.5    Asher, R.6    Salio, M.7    Middleton, M.8    Cerundolo, V.9
  • 49
    • 0027977021 scopus 로고
    • Evolution of the serum amyloid A (SAA) protein superfamily
    • Uhlar, C. M., C. J. Burgess, P. M. Sharp, and A. S. Whitehead. 1994. Evolution of the serum amyloid A (SAA) protein superfamily. Genomics 19: 228-235.
    • (1994) Genomics , vol.19 , pp. 228-235
    • Uhlar, C.M.1    Burgess, C.J.2    Sharp, P.M.3    Whitehead, A.S.4
  • 50
    • 33748136434 scopus 로고    scopus 로고
    • Serum amyloid A is an innate immune opsonin for gram-negative bacteria
    • Shah, C., R. Hari-Dass, and J. G. Raynes. 2006. Serum amyloid A is an innate immune opsonin for Gram-negative bacteria. Blood 108: 1751-1757.
    • (2006) Blood , vol.108 , pp. 1751-1757
    • Shah, C.1    Hari-Dass, R.2    Raynes, J.G.3


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