메뉴 건너뛰기




Volumn 169, Issue 8, 2002, Pages 4594-4603

Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYCLOHEXIMIDE; CYTOCHALASIN B; CYTOKINE; G PROTEIN COUPLED RECEPTOR; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 8; MESSENGER RNA; MONOCLONAL ANTIBODY; MONOCYTE CHEMOTACTIC PROTEIN 1; MYELOBLASTIN; PROTEINASE ACTIVATED RECEPTOR 2; SERINE PROTEINASE INHIBITOR; TRYPSIN;

EID: 0037108503     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.169.8.4594     Document Type: Article
Times cited : (84)

References (52)
  • 1
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Déry, O., C. U. Corvera, M. Steinhoff, and N. W. Bunnett. 1998. Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. Am. J. Physiol. 274:C1429.
    • (1998) Am. J. Physiol. , vol.274
    • Déry, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 2
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin, S. R. 2000. Thrombin signalling and protease-activated receptors. Nature 407, 258.
    • (2000) Nature , vol.407 , pp. 258
    • Coughlin, S.R.1
  • 3
    • 0035952643 scopus 로고    scopus 로고
    • Protease activated receptors: Theme and variations
    • O'Brien, P. J., M. Molino, M. Kahn, and L. F. Brass, 2001. Protease activated receptors: theme and variations. Oncogene 20:1570.
    • (2001) Oncogene , vol.20 , pp. 1570
    • O'Brien, P.J.1    Molino, M.2    Kahn, M.3    Brass, L.F.4
  • 7
    • 0032510949 scopus 로고    scopus 로고
    • The human proteinase-activated receptor-3 (PAR-3) gene: Identification within a PAR gene cluster and characterization in vascular endothelial cells and platelets
    • , Schmidt, V. A., W. C. Nierman, D. R. Maglott, L. D. Cupit, K. A. Moskowitz, J. A. Wainer, and W. F. Bahou. 1998. The human proteinase-activated receptor-3 (PAR-3) gene: identification within a PAR gene cluster and characterization in vascular endothelial cells and platelets. J. Biol. Chem. 273:15061.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15061
    • Schmidt, V.A.1    Nierman, W.C.2    Maglott, D.R.3    Cupit, L.D.4    Moskowitz, K.A.5    Wainer, J.A.6    Bahou, W.F.7
  • 8
    • 0034608013 scopus 로고    scopus 로고
    • Thrombin responses in human endothelial cells: Contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1
    • O'Brien, P. J., N. Prevost, M. Molino, M. K. Hollinger, M. J. Woolkalis, D. S. Woulfe, and L. F. Brass. 2000. Thrombin responses in human endothelial cells: contributions from receptors other than PAR1 include the transactivation of PAR2 by thrombin-cleaved PAR1. J. Biol. Chem. 275:13502.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13502
    • O'Brien, P.J.1    Prevost, N.2    Molino, M.3    Hollinger, M.K.4    Woolkalis, M.J.5    Woulfe, D.S.6    Brass, L.F.7
  • 9
    • 0034923238 scopus 로고    scopus 로고
    • Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion
    • Lourbakos, A., J. Potempa, J. Travis, M. R, D'Andrea, P. Andrade-Gordon, R. Santulli, E. J. Mackie, and R. N. Pike. 2001, Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion. Infect. Immun. 69:5121.
    • (2001) Infect. Immun. , vol.69 , pp. 5121
    • Lourbakos, A.1    Potempa, J.2    Travis, J.3    D'Andrea, M.R.4    Andrade-Gordon, P.5    Santulli, R.6    Mackie, E.J.7    Pike, R.N.8
  • 10
    • 0030968521 scopus 로고    scopus 로고
    • Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: Evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor
    • Renesto, P., M. Si-Tahar, M. Moniatte, V. Balloy, A. Van Dorsselaer, D. Pidard, and M. Chignard. 1997. Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor. Blood 89:1944.
    • (1997) Blood , vol.89 , pp. 1944
    • Renesto, P.1    Si-Tahar, M.2    Moniatte, M.3    Balloy, V.4    Van Dorsselaer, A.5    Pidard, D.6    Chignard, M.7
  • 11
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • Owen, C. A., and E. J. Campbell. 1999. The cell biology of leukocyte-mediated proteolysis. J. Leukocyte Biol. 65:137.
    • (1999) J. Leukocyte Biol. , vol.65 , pp. 137
    • Owen, C.A.1    Campbell, E.J.2
  • 12
    • 0024817730 scopus 로고
    • Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells
    • Bories, D., M.-C. Raynal, D. H. Solomon, Z. Darzynkiewicz, and Y. E. Cayre. 1989. Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells. Cell 59:959.
    • (1989) Cell , vol.59 , pp. 959
    • Bories, D.1    Raynal, M.-C.2    Solomon, D.H.3    Darzynkiewicz, Z.4    Cayre, Y.E.5
  • 13
    • 0025776716 scopus 로고
    • Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase: Structural and functional properties
    • Rao, N. V., N. G. Wehner, B. C. Marshall, W. R. Gray, B. H. Gray, and J. R. Hoidal. 1991. Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase: structural and functional properties. J. Biol. Chem. 266:9540.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9540
    • Rao, N.V.1    Wehner, N.G.2    Marshall, B.C.3    Gray, W.R.4    Gray, B.H.5    Hoidal, J.R.6
  • 14
    • 0034665315 scopus 로고    scopus 로고
    • Bioactive proteinase 3 on the cell surface of human neutrophils: Quantification, catalytic activity, and susceptibility to inhibition
    • Campbell, E. J., M. A. Campbell, and C. A. Owen. 2000. Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J. Immunol. 165:3366.
    • (2000) J. Immunol. , vol.165 , pp. 3366
    • Campbell, E.J.1    Campbell, M.A.2    Owen, C.A.3
  • 15
    • 0026070031 scopus 로고
    • Proteinase 3, the target antigen of anticytoplasmic antibodies circulating in Wegener's granulomatosis: Immunolocalization in normal and pathologic tissues
    • Braun, M. G., E. Csernok, W. L. Gross, and H. K. Muller-Hermelink. 1991. Proteinase 3, the target antigen of anticytoplasmic antibodies circulating in Wegener's granulomatosis: immunolocalization in normal and pathologic tissues. Am. J. Pathol. 139:831.
    • (1991) Am. J. Pathol. , vol.139 , pp. 831
    • Braun, M.G.1    Csernok, E.2    Gross, W.L.3    Muller-Hermelink, H.K.4
  • 16
    • 0025129105 scopus 로고
    • Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme
    • Lüdemann, J., B. Utecht, and W. L. Gross. 1990. Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme. J. Exp. Med. 171:357.
    • (1990) J. Exp. Med. , vol.171 , pp. 357
    • Lüdemann, J.1    Utecht, B.2    Gross, W.L.3
  • 17
    • 17144468862 scopus 로고    scopus 로고
    • A secreted proform of neutrophil proteinase 3 regulates the proliferation of granulopoietic progenitor cells
    • Sköld, S., B. Rosberg, U. Gullberg, and T. Olofsson. 1999. A secreted proform of neutrophil proteinase 3 regulates the proliferation of granulopoietic progenitor cells. Blood 93:849.
    • (1999) Blood , vol.93 , pp. 849
    • Sköld, S.1    Rosberg, B.2    Gullberg, U.3    Olofsson, T.4
  • 18
    • 0032989434 scopus 로고    scopus 로고
    • Converting enzyme-independent release of tumor necrosis factor α and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3
    • Coeshott, C., C. Ohnemus, A. Pilyavskaya, S. Ross, M. Wieczorek, H. Kroona, A. H. Leimer, and J. Cheronis. 1999. Converting enzyme-independent release of tumor necrosis factor α and IL-1β from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. Proc. Natl. Acad. Sci. USA 96:6261.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6261
    • Coeshott, C.1    Ohnemus, C.2    Pilyavskaya, A.3    Ross, S.4    Wieczorek, M.5    Kroona, H.6    Leimer, A.H.7    Cheronis, J.8
  • 20
    • 0035040674 scopus 로고    scopus 로고
    • Proteinase 3 enhances endothelial monocyte chemoattractant protein-1 production and induces increased adhesion of neutrophils to endothelial cells by up-regulating intercellular cell adhesion molecule-1
    • Taekema-Roelvink, M. E. J., C. van Kooten, S. van der Kooij, E. Heemskerk, and M. R. Daha. 2001. Proteinase 3 enhances endothelial monocyte chemoattractant protein-1 production and induces increased adhesion of neutrophils to endothelial cells by up-regulating intercellular cell adhesion molecule-1. J. Am. Soc. Nephrol. 12:932.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 932
    • Taekema-Roelvink, M.E.J.1    Van Kooten, C.2    Van der Kooij, S.3    Heemskerk, E.4    Daha, M.R.5
  • 21
    • 0025239075 scopus 로고
    • Azurocidin and a homologous serine protease from neutrophils: Differential antimicrobial and proteolytic properties
    • Campanelli, D., P. A. Detmars, C. F. Nathan, and J. E. Gabay. 1990. Azurocidin and a homologous serine protease from neutrophils: differential antimicrobial and proteolytic properties. J. Clin. Invest. 85:904.
    • (1990) J. Clin. Invest. , vol.85 , pp. 904
    • Campanelli, D.1    Detmars, P.A.2    Nathan, C.F.3    Gabay, J.E.4
  • 22
    • 0028145442 scopus 로고
    • Cytokine profile and ultrastructure of intraepithelial γδ T cells in chronically inflamed human gingiva suggest a cytotoxic effector function
    • Lundqvist, C., V. Baranov, S. Teglund, S. Hammarström, and M.-L. Hammarström. 1994. Cytokine profile and ultrastructure of intraepithelial γδ T cells in chronically inflamed human gingiva suggest a cytotoxic effector function. J. Immunol. 153:2302.
    • (1994) J. Immunol. , vol.153 , pp. 2302
    • Lundqvist, C.1    Baranov, V.2    Teglund, S.3    Hammarström, S.4    Hammarström, M.-L.5
  • 23
    • 7344251169 scopus 로고    scopus 로고
    • Differential expression of interleukin-8 and intercellular adhesion molecule-1 by human gingival epithelial cells in response to Actino bacillus actinomycetemcomitans or Porphyromonas gingivalis infection
    • Huang, G. T.-J., S. K. Haake, J.-W. Kim, and N.-H. Park. 1998. Differential expression of interleukin-8 and intercellular adhesion molecule-1 by human gingival epithelial cells in response to Actino bacillus actinomycetemcomitans or Porphyromonas gingivalis infection. Oral Microbiol. ImmunoI. 13:301.
    • (1998) Oral Microbiol. ImmunoI. , vol.13 , pp. 301
    • Huang, G.T.-J.1    Haake, S.K.2    Kim, J.-W.3    Park, N.-H.4
  • 24
    • 0032952806 scopus 로고    scopus 로고
    • Interleukin-6 (1L-6) and IL-8 are induced in human oral epithelial cells in response to exposure to periodontopathic Eikenella corrodens
    • Yumoto, H., H. Nakae, K. Fujinaka, S. Ebisu, and T. Matsuo. 1999. lnterleukin-6 (1L-6) and IL-8 are induced in human oral epithelial cells in response to exposure to periodontopathic Eikenella corrodens. Infect. Immun. 67:384.
    • (1999) Infect. Immun. , vol.67 , pp. 384
    • Yumoto, H.1    Nakae, H.2    Fujinaka, K.3    Ebisu, S.4    Matsuo, T.5
  • 25
    • 0036142393 scopus 로고    scopus 로고
    • Activation of human gingival epithelial cells by cell-surface components of black-pigmented bacteria: Augmentation of production of interleukin-8, granulocyte colony-stimulating factor and granulocyte-macrophage colony-stimulating factor and expression of intercellular adhesion molecule 1
    • Sugiyama, A., A. Uehara, K. Iki, K. Matsushita, R. Nakamura, T. Ogawa, S. Sugawara, and H. Takada. 2002. Activation of human gingival epithelial cells by cell-surface components of black-pigmented bacteria: augmentation of production of interleukin-8, granulocyte colony-stimulating factor and granulocyte-macrophage colony-stimulating factor and expression of intercellular adhesion molecule 1. J. Med. Microbiol. 51:27.
    • (2002) J. Med. Microbiol. , vol.51 , pp. 27
    • Sugiyama, A.1    Uehara, A.2    Iki, K.3    Matsushita, K.4    Nakamura, R.5    Ogawa, T.6    Sugawara, S.7    Takada, H.8
  • 26
    • 0034839783 scopus 로고    scopus 로고
    • Contrasting responses of human gingival and colonic epithelial cells to lipopolysaccharide, lipoteichoic acids and peptidoglycans in the presence of soluble CD14
    • Uehara, A., S. Sugawara, R. Tamai, and H. Takada. 2001. Contrasting responses of human gingival and colonic epithelial cells to lipopolysaccharide, lipoteichoic acids and peptidoglycans in the presence of soluble CD14. Med. Microbiol. Immunol. 189:185.
    • (2001) Med. Microbiol. Immunol. , vol.189 , pp. 185
    • Uehara, A.1    Sugawara, S.2    Tamai, R.3    Takada, H.4
  • 28
    • 0024367423 scopus 로고
    • Variant sublines with different metastatic potentials selected in nude mice from human oral squamous cell carcinomas
    • Momose, F., T. Araida, A. Negishi, H. Ichijo, S. Shioda, and S. Sasaki. 1989. Variant sublines with different metastatic potentials selected in nude mice from human oral squamous cell carcinomas. J. Oral Pathol. Med. 18:391.
    • (1989) J. Oral Pathol. Med. , vol.18 , pp. 391
    • Momose, F.1    Araida, T.2    Negishi, A.3    Ichijo, H.4    Shioda, S.5    Sasaki, S.6
  • 29
    • 84873762554 scopus 로고
    • Propagation in a fluid medium of a human epidermoid carcinoma, strain KB
    • Eagle, H. 1955. Propagation in a fluid medium of a human epidermoid carcinoma, strain KB. Proc. Soc. Exp. Biol. Med. 89:362.
    • (1955) Proc. Soc. Exp. Biol. Med. , vol.89 , pp. 362
    • Eagle, H.1
  • 30
    • 0018902785 scopus 로고
    • Optimal conditions for simultaneous purification of mononuclear and polymorphonuclear leukocytes from human blood by the Hypaque-Ficoll method
    • Ferrante, A., and Y. H. Thong. 1980. Optimal conditions for simultaneous purification of mononuclear and polymorphonuclear leukocytes from human blood by the Hypaque-Ficoll method. J. Immunol. Methods 36:109.
    • (1980) J. Immunol. Methods , vol.36 , pp. 109
    • Ferrante, A.1    Thong, Y.H.2
  • 31
    • 0034235313 scopus 로고    scopus 로고
    • Proteolysis of human monocyte CD14 by cysteine proteinases (gingipains) from Porphyromonas gingivalis leading to lipopolysaccharide hyporesponsiveness
    • Sugawara, S., E. Nemoto, H. Tada, K. Miyake, T. Imamura, and H. Takada. 2000. Proteolysis of human monocyte CD14 by cysteine proteinases (gingipains) from Porphyromonas gingivalis leading to lipopolysaccharide hyporesponsiveness. J. Immunol. 165:411.
    • (2000) J. Immunol. , vol.165 , pp. 411
    • Sugawara, S.1    Nemoto, E.2    Tada, H.3    Miyake, K.4    Imamura, T.5    Takada, H.6
  • 32
    • 0031813835 scopus 로고    scopus 로고
    • Heterogeneous expression and release of CD14 by human gingival fibroblasts: Characterization and CD14-mediated interleukin-8 secretion in response to lipopolysaccharide
    • Sugawara, S., A. Sugiyama, E. Nemoto, H. Rikiishi, and H. Takada. 1998. Heterogeneous expression and release of CD14 by human gingival fibroblasts: characterization and CD14-mediated interleukin-8 secretion in response to lipopolysaccharide. Infect. Immun. 66:3043.
    • (1998) Infect. Immun. , vol.66 , pp. 3043
    • Sugawara, S.1    Sugiyama, A.2    Nemoto, E.3    Rikiishi, H.4    Takada, H.5
  • 33
    • 0024521294 scopus 로고
    • Monocyte-lymphocyte discrimination in a new microtitre-based adhesion assay
    • Bath, P. M. W., R. F. G. Booth, and D. G. Hassall. 1989. Monocyte-lymphocyte discrimination in a new microtitre-based adhesion assay. J. Immunol. Methods 118:59.
    • (1989) J. Immunol. Methods , vol.118 , pp. 59
    • Bath, P.M.W.1    Booth, R.F.G.2    Hassall, D.G.3
  • 34
    • 0028674497 scopus 로고
    • Myeloblastin: Leukocyte proteinase 3
    • Hoidal, J. R., N. V. Rao, and B. Gray. 1994. Myeloblastin: leukocyte proteinase 3. Methods Enzymol. 244:61.
    • (1994) Methods Enzymol. , vol.244 , pp. 61
    • Hoidal, J.R.1    Rao, N.V.2    Gray, B.3
  • 35
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T. H., D. T. Hung, V. I. Wheaton, and S. R. Coughlin. 1991. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64:1057.
    • (1991) Cell , vol.64 , pp. 1057
    • Vu, T.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 36
    • 0030589624 scopus 로고    scopus 로고
    • Trypsin induced von Willebrand factor release from human endothelial cells is mediated by PAR-2 activation
    • Storck, J., B. Kusters, M. Vahland, C. Morys-Wortmann, and E. R. Zimmermann. 1996. Trypsin induced von Willebrand factor release from human endothelial cells is mediated by PAR-2 activation. Thromb. Res. 84:463.
    • (1996) Thromb. Res. , vol.84 , pp. 463
    • Storck, J.1    Kusters, B.2    Vahland, M.3    Morys-Wortmann, C.4    Zimmermann, E.R.5
  • 38
    • 0032563094 scopus 로고    scopus 로고
    • Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily
    • Tateno, H., A. Saneyoshi, T. Ogawa, K. Muramoto, H. Kamiya, and M. Saneyoshi. 1998. Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily. J. Biol. Chem. 273:19190.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19190
    • Tateno, H.1    Saneyoshi, A.2    Ogawa, T.3    Muramoto, K.4    Kamiya, H.5    Saneyoshi, M.6
  • 39
    • 0010801882 scopus 로고
    • Useful tool for characterizing some of the polymerization properties of actin
    • Korn, E. D. 1981. Useful tool for characterizing some of the polymerization properties of actin. Physiol. Rev. 62:672.
    • (1981) Physiol. Rev. , vol.62 , pp. 672
    • Korn, E.D.1
  • 40
    • 15844401726 scopus 로고    scopus 로고
    • The proteinase-activated receptor 2 is induced by inflammatory mediators in human endothelial cells: Comparison with thrombin receptor
    • Nystedt, S., V. Ramakrishnan, and J. Sundelin. 1996. The proteinase-activated receptor 2 is induced by inflammatory mediators in human endothelial cells: comparison with thrombin receptor. J. Biol. Chem. 271:14910.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14910
    • Nystedt, S.1    Ramakrishnan, V.2    Sundelin, J.3
  • 41
    • 0035184146 scopus 로고    scopus 로고
    • Protease-activated receptors in human airways: Up-regulation of PAR-2 in respiratory epithelium from patients with asthma
    • Knight, D. A, S. Lim, A. K. Scaffidi, N. Roche, K. F. Chung, G. A. Stewart, and P. J. Thompson. 2001. Protease-activated receptors in human airways: up-regulation of PAR-2 in respiratory epithelium from patients with asthma. J. Allergy Clin. Immunol. 108:797.
    • (2001) J. Allergy Clin. Immunol. , vol.108 , pp. 797
    • Knight, D.A.1    Lim, S.2    Scaffidi, A.K.3    Roche, N.4    Chung, K.F.5    Stewart, G.A.6    Thompson, P.J.7
  • 42
    • 0035943658 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory κB kinases in NCTC 2544 keratinocytes
    • Kanke, T., S. R. Macfarlane, M. J. Seatter, E. Davenport, A. Paul, R. C. McKenzie, and R. Plevin. 2001. Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory κB kinases in NCTC 2544 keratinocytes. J. Biol. Chem. 276:31657.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31657
    • Kanke, T.1    Macfarlane, S.R.2    Seatter, M.J.3    Davenport, E.4    Paul, A.5    McKenzie, R.C.6    Plevin, R.7
  • 43
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokines; CXC and CC chemokines
    • Baggiolini, M., B. Dewald, and B. Moser. 1994. Interleukin-8 and related chemotactic cytokines; CXC and CC chemokines. Adv. Immunol. 55:97.
    • (1994) Adv. Immunol. , vol.55 , pp. 97
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 44
    • 0034704593 scopus 로고    scopus 로고
    • Control of TH2 polarization by the chemokine monocyte chemoattractant protein-1
    • Gu, L., S. Tseng, R. M. Homer, C. Tam, M. Loda, and B. J. Rollins. 2000. Control of TH2 polarization by the chemokine monocyte chemoattractant protein-1. Nature 404:407.
    • (2000) Nature , vol.404 , pp. 407
    • Gu, L.1    Tseng, S.2    Homer, R.M.3    Tam, C.4    Loda, M.5    Rollins, B.J.6
  • 45
    • 0035911254 scopus 로고    scopus 로고
    • Absence of monocyte chemoattractant protein 1 in mice leads to decreased local macrophage recruitment and antigen-specific T helper cell type 1 immune response in experimental autoimmune encephalomyelitis
    • Huang, D., J. Wang, P. Kivisakk, B. J. Rollins, and R. M. Ransohoff. 2001. Absence of monocyte chemoattractant protein 1 in mice leads to decreased local macrophage recruitment and antigen-specific T helper cell type 1 immune response in experimental autoimmune encephalomyelitis. J. Exp. Med. 193:713.
    • (2001) J. Exp. Med. , vol.193 , pp. 713
    • Huang, D.1    Wang, J.2    Kivisakk, P.3    Rollins, B.J.4    Ransohoff, R.M.5
  • 46
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • Van Kooyk, Y., and C. G. Figdor. 2000. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr. Opin. Cell Biol. 12:542.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 542
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 48
    • 0032469877 scopus 로고    scopus 로고
    • Interactions between non-immune host cells and the immune system during periodontal disease: Role of the gingival keratinocyte
    • Suchett-Kaye, G., J.-J. Morrier, and O. Barsotti. 1998. Interactions between non-immune host cells and the immune system during periodontal disease: role of the gingival keratinocyte. Crit. Rev. Oral Biol. Med. 9:292.
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 292
    • Suchett-Kaye, G.1    Morrier, J.-J.2    Barsotti, O.3
  • 50
    • 0035575784 scopus 로고    scopus 로고
    • Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2
    • Miike, S., A. S. McWilliam, and H. Kita. 2001. Trypsin induces activation and inflammatory mediator release from human eosinophils through protease-activated receptor-2. J. Immunol. 167:6615.
    • (2001) J. Immunol. , vol.167 , pp. 6615
    • Miike, S.1    McWilliam, A.S.2    Kita, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.