메뉴 건너뛰기




Volumn 171, Issue 5, 2003, Pages 2602-2609

Blockade of S100A8 and S100A9 suppresses neutrophil migration in response to lipopolysaccharide

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPOLYSACCHARIDE; PROTEIN S 100; PROTEIN S100A8; PROTEIN S100A9; UNCLASSIFIED DRUG;

EID: 0041427762     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.171.5.2602     Document Type: Article
Times cited : (198)

References (48)
  • 1
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi, K., V. Burkart, S. Flohe, and H. Kolb. 2000. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J. Immunol. 164:558.
    • (2000) J. Immunol. , vol.164 , pp. 558
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 2
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • Chen, W., U. Syldath, K. Bellmann, V. Burkart, and H. Kolb. 1999. Human 60-kDa heat-shock protein: a danger signal to the innate immune system. J. Immunol. 162:3212.
    • (1999) J. Immunol. , vol.162 , pp. 3212
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 3
    • 0029982220 scopus 로고    scopus 로고
    • Heat shock protein 65 induces CD62e, CD106, and CD54 on cultured human endothelial cells and increases their adhesiveness for monocytes and granulocytes
    • Verdegaal, M. E., S. T. Zegveld, and R. van Furth. 1996. Heat shock protein 65 induces CD62e, CD106, and CD54 on cultured human endothelial cells and increases their adhesiveness for monocytes and granulocytes. J. Immunol. 157:369.
    • (1996) J. Immunol. , vol.157 , pp. 369
    • Verdegaal, M.E.1    Zegveld, S.T.2    Van Furth, R.3
  • 6
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: A central cell surface receptor for S100/calgranulin polypeptides
    • Hofmann, M. A., S. Drury, C. F. Fu, W. Qu, A. Taguchi, Y. Lu, C. Avila, N. Kambham, A. Bierhaus, P. Nawroth, et al. 1999. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97:889.
    • (1999) Cell , vol.97 , pp. 889
    • Hofmann, M.A.1    Drury, S.2    Fu, C.F.3    Qu, W.4    Taguchi, A.5    Lu, Y.6    Avila, C.7    Kambham, N.8    Bierhaus, A.9    Nawroth, P.10
  • 8
    • 0026699628 scopus 로고
    • Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins
    • Lackmann, M., C. J. Cornish, R. J. Simpson, R. L. Moritz, and C. L. Geczy. 1992. Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins. J. Biol. Chem. 267:7499.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7499
    • Lackmann, M.1    Cornish, C.J.2    Simpson, R.J.3    Moritz, R.L.4    Geczy, C.L.5
  • 10
    • 0025900907 scopus 로고
    • Identification of p8, 14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells
    • Edgeworth, J., M. Gorman, R. Bennett, P. Freemont, and N. Hogg. 1991. Identification of p8, 14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells. J. Biol. Chem. 266:7706.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7706
    • Edgeworth, J.1    Gorman, M.2    Bennett, R.3    Freemont, P.4    Hogg, N.5
  • 11
    • 0026030821 scopus 로고
    • Identification of "cystic fibrosis protein" as a complex of two calcium-binding proteins present in human cells of myeloid origin
    • Barthe, C., C. Figarella, J. Carrere, and O. Guy-Crotte. 1991. Identification of "cystic fibrosis protein" as a complex of two calcium-binding proteins present in human cells of myeloid origin. Biochim. Biophys. Acta 1096:175.
    • (1991) Biochim. Biophys. Acta , vol.1096 , pp. 175
    • Barthe, C.1    Figarella, C.2    Carrere, J.3    Guy-Crotte, O.4
  • 12
    • 0033839581 scopus 로고    scopus 로고
    • Calprotectin (MRP8/14 protein complex) release during mycobacterial infection in vitro and in vivo
    • Pechkovsky, D. V., O. M. Zalutskaya, G. I. Ivanov, and N. I. Misuno. 2000. Calprotectin (MRP8/14 protein complex) release during mycobacterial infection in vitro and in vivo. FEMS Immunol. Med. Microbiol. 29:27.
    • (2000) FEMS Immunol. Med. Microbiol. , vol.29 , pp. 27
    • Pechkovsky, D.V.1    Zalutskaya, O.M.2    Ivanov, G.I.3    Misuno, N.I.4
  • 13
    • 0034089471 scopus 로고    scopus 로고
    • Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis
    • Frosch, M., A. Strey, T. Vogl, N. M. Wulffraat, W. Kuis, C. Sunderkotter, E. Harms, C. Sorg, and J. Roth. 2000. Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis. Arthritis Rheum. 43:628.
    • (2000) Arthritis Rheum. , vol.43 , pp. 628
    • Frosch, M.1    Strey, A.2    Vogl, T.3    Wulffraat, N.M.4    Kuis, W.5    Sunderkotter, C.6    Harms, E.7    Sorg, C.8    Roth, J.9
  • 14
    • 0034439034 scopus 로고    scopus 로고
    • Human gingival crevicular fluid contains MRP8 (S100A8) and MRP14 (S100A9), two calcium-binding proteins of the S100 family
    • Kojima, T., E. Andersen, J. C. Sanchez, M. R. Wilkins, D. F. Hochstrasser, W. F. Pralong, and G. Cimasoni. 2000. Human gingival crevicular fluid contains MRP8 (S100A8) and MRP14 (S100A9), two calcium-binding proteins of the S100 family. J. Dent. Res. 79:740.
    • (2000) J. Dent. Res. , vol.79 , pp. 740
    • Kojima, T.1    Andersen, E.2    Sanchez, J.C.3    Wilkins, M.R.4    Hochstrasser, D.F.5    Pralong, W.F.6    Cimasoni, G.7
  • 16
    • 0034194261 scopus 로고    scopus 로고
    • IFN-γ and TNF regulate macrophage expression of the chemotactic S100 protein S100A8
    • Xu, K., and C. L. Geczy. 2000. IFN-γ and TNF regulate macrophage expression of the chemotactic S100 protein S100A8. J. Immunol. 164:4916.
    • (2000) J. Immunol. , vol.164 , pp. 4916
    • Xu, K.1    Geczy, C.L.2
  • 17
    • 0035873775 scopus 로고    scopus 로고
    • IL-10 up-regulates macrophage expression of the S100 protein S100A8
    • Xu, K., T. Yen, and C. L. Geczy. 2001. IL-10 up-regulates macrophage expression of the S100 protein S100A8. J. Immunol. 166:6358.
    • (2001) J. Immunol. , vol.166 , pp. 6358
    • Xu, K.1    Yen, T.2    Geczy, C.L.3
  • 18
    • 0031452336 scopus 로고    scopus 로고
    • Induction of the S100 chemotactic protein, CP-10, in murine microvascular endothelial cells by proinflammatory stimuli
    • Yen, T., C. A. Harrison, J. M. Devery, S. Leong, S. E. Iismaa, T. Yoshimura, and C. L. Geczy. 1997. Induction of the S100 chemotactic protein, CP-10, in murine microvascular endothelial cells by proinflammatory stimuli. Blood. 90:4812.
    • (1997) Blood , vol.90 , pp. 4812
    • Yen, T.1    Harrison, C.A.2    Devery, J.M.3    Leong, S.4    Iismaa, S.E.5    Yoshimura, T.6    Geczy, C.L.7
  • 20
  • 21
    • 0037443667 scopus 로고    scopus 로고
    • Proinflammatory activities of S100 proteins: S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion
    • Ryckman, C., K. Vandal, P. Rouleau, M. Talbot, and P. A. Tessier. 2003. Proinflammatory activities of S100 proteins: S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. J. Immunol. 170:3233.
    • (2003) J. Immunol. , vol.170 , pp. 3233
    • Ryckman, C.1    Vandal, K.2    Rouleau, P.3    Talbot, M.4    Tessier, P.A.5
  • 23
    • 0023815341 scopus 로고
    • Neutrophil death as a defence mechanism against Candida albicans infections
    • McNamara, M. P., J. H. Wiessner, C. Collins-Lech, B. L. Hahn, and P. G. Sohnle. 1988. Neutrophil death as a defence mechanism against Candida albicans infections. Lancet 2:1163.
    • (1988) Lancet , vol.2 , pp. 1163
    • McNamara, M.P.1    Wiessner, J.H.2    Collins-Lech, C.3    Hahn, B.L.4    Sohnle, P.G.5
  • 24
    • 0026059423 scopus 로고
    • The zinc-reversible antimicrobial activity of neutrophil lysates and abscess fluid supernatants
    • Sohnle, P. G., C. Collins-Lech, and J. H. Wiessner. 1991. The zinc-reversible antimicrobial activity of neutrophil lysates and abscess fluid supernatants. J. Infect. Dis. 164:137.
    • (1991) J. Infect. Dis. , vol.164 , pp. 137
    • Sohnle, P.G.1    Collins-Lech, C.2    Wiessner, J.H.3
  • 25
    • 0025965196 scopus 로고
    • Antimicrobial activity of an abundant calcium-binding protein in the cytoplasm of human neutrophils
    • Sohnle, P. G., C. Collins-Lech, and J. H. Wiessner. 1991. Antimicrobial activity of an abundant calcium-binding protein in the cytoplasm of human neutrophils. J. Infect. Dis. 163:187.
    • (1991) J. Infect. Dis. , vol.163 , pp. 187
    • Sohnle, P.G.1    Collins-Lech, C.2    Wiessner, J.H.3
  • 26
    • 0028929257 scopus 로고
    • Resistance of zinc-supplemented Candida albicans cells to the growth inhibitory effect of calprotectin
    • Santhanagopalan, V., B. L. Hahn, and P. G. Sohnle. 1995. Resistance of zinc-supplemented Candida albicans cells to the growth inhibitory effect of calprotectin. J. Infect. Dis. 171:1289.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1289
    • Santhanagopalan, V.1    Hahn, B.L.2    Sohnle, P.G.3
  • 27
    • 0029828249 scopus 로고    scopus 로고
    • Inhibition of Candida albicans growth by calprotectin in the absence of direct contact with the organisms
    • Sohnle, P. G., B. L. Hahn, and V. Santhanagopalan. 1996. Inhibition of Candida albicans growth by calprotectin in the absence of direct contact with the organisms. J. Infect. Dis. 174:1369.
    • (1996) J. Infect. Dis. , vol.174 , pp. 1369
    • Sohnle, P.G.1    Hahn, B.L.2    Santhanagopalan, V.3
  • 28
    • 0031934940 scopus 로고    scopus 로고
    • Histidine-based zinc-binding sequences and the antimicrobial activity of calprotectin
    • Loomans, H. J., B. L. Hahn, Q. Q. Li, S. H. Phadnis, and P. G. Sohnle. 1998. Histidine-based zinc-binding sequences and the antimicrobial activity of calprotectin. J. Infect. Dis. 177:812.
    • (1998) J. Infect. Dis. , vol.177 , pp. 812
    • Loomans, H.J.1    Hahn, B.L.2    Li, Q.Q.3    Phadnis, S.H.4    Sohnle, P.G.5
  • 29
    • 0033796465 scopus 로고    scopus 로고
    • Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14)
    • Sohnle, P. G., M. J. Hunter, B. Hahn, and W. J. Chazin. 2000. Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14). J. Infect. Dis. 182:1272.
    • (2000) J. Infect. Dis. , vol.182 , pp. 1272
    • Sohnle, P.G.1    Hunter, M.J.2    Hahn, B.3    Chazin, W.J.4
  • 32
    • 0033791974 scopus 로고    scopus 로고
    • Human neutrophil-mediated nonoxidative antifungal activity against Cryptococcus neoformans
    • Mambula, S. S., E. R. Simons, R. Hastey, M. E. Selsted, and S. M. Levitz. 2000. Human neutrophil-mediated nonoxidative antifungal activity against Cryptococcus neoformans. Infect. Immun. 68:6257.
    • (2000) Infect. Immun. , vol.68 , pp. 6257
    • Mambula, S.S.1    Simons, E.R.2    Hastey, R.3    Selsted, M.E.4    Levitz, S.M.5
  • 33
    • 0034978030 scopus 로고    scopus 로고
    • Calprotectin expression in vitro by oral epithelial cells confers resistance to infection by Porphyromonas gingivalis
    • Nisapakultorn, K., K. F. Ross, and M. C. Herzberg. 2001. Calprotectin expression in vitro by oral epithelial cells confers resistance to infection by Porphyromonas gingivalis. Infect. Immun. 69:4242.
    • (2001) Infect. Immun. , vol.69 , pp. 4242
    • Nisapakultorn, K.1    Ross, K.F.2    Herzberg, M.C.3
  • 34
    • 0034997757 scopus 로고    scopus 로고
    • Calprotectin expression inhibits bacterial binding to mucosal epithelial cells
    • Nisapakultorn, K., K. F. Ross, and M. C. Herzberg. 2001. Calprotectin expression inhibits bacterial binding to mucosal epithelial cells. Infect. Immun. 69:3692.
    • (2001) Infect. Immun. , vol.69 , pp. 3692
    • Nisapakultorn, K.1    Ross, K.F.2    Herzberg, M.C.3
  • 35
    • 0026652590 scopus 로고
    • Calprotectin in patients with rheumatoid arthritis: Relation to clinical and laboratory variables of disease activity
    • Brun, J. G., H. J. Haga, E. Boe, I. Kallay, C. Lekven, H. B. Berntzen, and M. K. Fagerhol. 1992. Calprotectin in patients with rheumatoid arthritis: relation to clinical and laboratory variables of disease activity. J. Rheumatol. 19:859.
    • (1992) J. Rheumatol. , vol.19 , pp. 859
    • Brun, J.G.1    Haga, H.J.2    Boe, E.3    Kallay, I.4    Lekven, C.5    Berntzen, H.B.6    Fagerhol, M.K.7
  • 36
    • 0029090604 scopus 로고
    • The myeloic related protein MRP8/14 (27E10 antigen) - Usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function
    • Lugering, N., R. Stoll, K. W. Schmid, T. Kucharzik, H. Stein, G. Burmeister, C. Sorg, and W. Domschke. 1995. The myeloic related protein MRP8/14 (27E10 antigen) - usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function. Eur. J. Clin. Invest. 25:659.
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 659
    • Lugering, N.1    Stoll, R.2    Schmid, K.W.3    Kucharzik, T.4    Stein, H.5    Burmeister, G.6    Sorg, C.7    Domschke, W.8
  • 37
    • 0026474831 scopus 로고
    • Complex pattern of the myelo-monocytic differentiation antigens MRP8 and MRP14 during chronic airway inflammation
    • Roth, J., S. Teigelkamp, M. Wilke, L. Grun, B. Tummler, and C. Sorg. 1992. Complex pattern of the myelo-monocytic differentiation antigens MRP8 and MRP14 during chronic airway inflammation. Immunobiology 186:304.
    • (1992) Immunobiology , vol.186 , pp. 304
    • Roth, J.1    Teigelkamp, S.2    Wilke, M.3    Grun, L.4    Tummler, B.5    Sorg, C.6
  • 38
    • 0032891539 scopus 로고    scopus 로고
    • CP-10, a chemotactic peptide, is expressed in lesions of experimental autoimmune encephalomyelitis, neuritis, uveitis and in C6 gliomas
    • Deininger, M. H., Y. Zhao, and H. J. Schluesener. 1999. CP-10, a chemotactic peptide, is expressed in lesions of experimental autoimmune encephalomyelitis, neuritis, uveitis and in C6 gliomas. J. Neuroimmunol. 93:156.
    • (1999) J. Neuroimmunol. , vol.93 , pp. 156
    • Deininger, M.H.1    Zhao, Y.2    Schluesener, H.J.3
  • 40
    • 0031253960 scopus 로고    scopus 로고
    • Chemokine networks in vivo: Involvement of C-X-C and C-C chemokines in neutrophil extravasation in vivo in response to TNF-α
    • Tessier, P. A., P. H. Naccache, I. Clark-Lewis, R. P. Gladue, K. S. Neote, and S. R. McColl. 1997. Chemokine networks in vivo: involvement of C-X-C and C-C chemokines in neutrophil extravasation in vivo in response to TNF-α. J. Immunol. 159:3595.
    • (1997) J. Immunol. , vol.159 , pp. 3595
    • Tessier, P.A.1    Naccache, P.H.2    Clark-Lewis, I.3    Gladue, R.P.4    Neote, K.S.5    McColl, S.R.6
  • 41
    • 0028293840 scopus 로고
    • Removal of blood from laboratory mammals and birds
    • Evans, G. O. 1994. Removal of blood from laboratory mammals and birds. Lab. Anim. 28:178.
    • (1994) Lab. Anim. , vol.28 , pp. 178
    • Evans, G.O.1
  • 42
    • 0028268514 scopus 로고
    • Acute inflammatory activity of the S100 protein CP-10: Activation of neutrophils in vivo and in vitro
    • Devery, J. M., N. J. King, and C. L. Geczy. 1994. Acute inflammatory activity of the S100 protein CP-10: activation of neutrophils in vivo and in vitro. J. Immunol. 152:1888.
    • (1994) J. Immunol. , vol.152 , pp. 1888
    • Devery, J.M.1    King, N.J.2    Geczy, C.L.3
  • 43
    • 0024411402 scopus 로고
    • Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro
    • Smith, W. C., S. D. Marlin, R. Rothlein, C. Toman, and D. C. Anderson. 1989. Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro. J. Clin. Invest. 83:2008.
    • (1989) J. Clin. Invest. , vol.83 , pp. 2008
    • Smith, W.C.1    Marlin, S.D.2    Rothlein, R.3    Toman, C.4    Anderson, D.C.5
  • 45
    • 0030015924 scopus 로고    scopus 로고
    • Contribution of LFA-1 and Mac-1 to CD18-dependent neutrophil emigration in a neonatal rabbit model
    • Graf, J. M., C. W. Smith, and M. M. Mariscalco. 1996. Contribution of LFA-1 and Mac-1 to CD18-dependent neutrophil emigration in a neonatal rabbit model. J. Appl. Physiol. 80:1984.
    • (1996) J. Appl. Physiol. , vol.80 , pp. 1984
    • Graf, J.M.1    Smith, C.W.2    Mariscalco, M.M.3
  • 47
    • 0024390899 scopus 로고
    • Monoclonal antibody 5.5 reacts with p8, 14, a myeloid molecule associated with some vascular endothelium
    • Hogg, N., C. Allen, and J. Edgeworth. 1989. Monoclonal antibody 5.5 reacts with p8, 14, a myeloid molecule associated with some vascular endothelium. Eur. J. Immunol. 19:1053.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 1053
    • Hogg, N.1    Allen, C.2    Edgeworth, J.3
  • 48
    • 0036479102 scopus 로고    scopus 로고
    • The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells
    • Robinson, M. J., P. Tessier, R. Poulsom, and N. Hogg. 2002. The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells. J. Biol. Chem. 277:3658.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3658
    • Robinson, M.J.1    Tessier, P.2    Poulsom, R.3    Hogg, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.