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Volumn 170, Issue 11, 2003, Pages 5690-5696

Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CATHEPSIN G; CYTOKINE; GUANINE NUCLEOTIDE BINDING PROTEIN; INTERLEUKIN 8; LEUKOCYTE ELASTASE; LIGAND; MESSENGER RNA; MONOCYTE CHEMOTACTIC PROTEIN 1; MYELOBLASTIN; PEPTIDE; PHOSPHOLIPASE C; PROTEINASE ACTIVATED RECEPTOR 2; RECOMBINANT PROTEIN; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SERINE PROTEINASE; TRYPSIN;

EID: 0037797300     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.170.11.5690     Document Type: Article
Times cited : (147)

References (59)
  • 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
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0037108503 scopus 로고    scopus 로고
    • Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2
    • Uehara. A., S. Sugawara, K. Muramoto, and H. Takada. 2002. Activation of human oral epithelial cells by neutrophil proteinase 3 through protease-activated receptor-2. J. Immunol. 169:4594.
    • (2002) J. Immunol. , vol.169 , pp. 4594
    • Uehara, A.1    Sugawara, S.2    Muramoto, K.3    Takada, H.4
  • 9
    • 0012030796 scopus 로고
    • Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor a potent inhibitor of leukocyte elastase
    • Thompson, R. C., and K. Ohlsson. 1986. Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor a potent inhibitor of leukocyte elastase. Proc. Natl. Acad. Sci. USA 83:6692.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6692
    • Thompson, R.C.1    Ohlsson, K.2
  • 11
    • 0034630318 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor is a novel inhibitor of fibroblast-mediated collagen gel contraction
    • Sumi, Y., H. Muramatsu. K. Hata, M. Ueda, and T. Muramatsu. 2000. Secretory leukocyte protease inhibitor is a novel inhibitor of fibroblast-mediated collagen gel contraction. Exp. Cell Res. 256:203.
    • (2000) Exp. Cell Res. , vol.256 , pp. 203
    • Sumi, Y.1    Muramatsu, H.2    Hata, K.3    Ueda, M.4    Muramatsu, T.5
  • 12
    • 0026751871 scopus 로고
    • The serine-protease inhibitor of cartilage matrix is not a chondrocytic gene product
    • Böhm. B., T. Aigner, R. Kinne, and H. Burkhardt. 1992. The serine-protease inhibitor of cartilage matrix is not a chondrocytic gene product. Eur. J. Biochem. 207:773.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 773
    • Böhm, B.1    Aigner, T.2    Kinne, R.3    Burkhardt, H.4
  • 13
    • 0030941175 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor: A macrophage product induced by and antagonistic to bacterial lipopolysaccharide
    • Jin, F., C. Nathan, D. Radzioch, and A. Ding. 1997. Secretory leukocyte protease inhibitor: a macrophage product induced by and antagonistic to bacterial lipopolysaccharide. Cell 88:417.
    • (1997) Cell , vol.88 , pp. 417
    • Jin, F.1    Nathan, C.2    Radzioch, D.3    Ding, A.4
  • 14
    • 0030977618 scopus 로고    scopus 로고
    • Secretory leukocyte proteinase inhibitor is a major leukocyte elastase inhibitor in human neutrophils
    • Sallenove, J.-M., M. Si-Ta har, G. Cox, M. Chignard, and J. Gauldie. 1997. Secretory leukocyte proteinase inhibitor is a major leukocyte elastase inhibitor in human neutrophils. J. Leukocyte Biol. 61:695.
    • (1997) J. Leukocyte Biol. , vol.61 , pp. 695
    • Sallenove, J.-M.1    Si-Ta har, M.2    Cox, G.3    Chignard, M.4    Gauldie, J.5
  • 15
    • 0032745122 scopus 로고    scopus 로고
    • Expression of secretory leukocyte protease inhibitor in women with endometriosis
    • Suzumori, N., M. Sato, T. Yoneda, Y. Ozaki, H. Takagi, and K. Suzumori. 1999. Expression of secretory leukocyte protease inhibitor in women with endometriosis. Fertil. Steril. 72:857.
    • (1999) Fertil. Steril. , vol.72 , pp. 857
    • Suzumori, N.1    Sato, M.2    Yoneda, T.3    Ozaki, Y.4    Takagi, H.5    Suzumori, K.6
  • 16
    • 0035024013 scopus 로고    scopus 로고
    • Human alveolar macrophages express elafin and secretory leukocyte protease inhibitor
    • Mihara. A., and G. M. Tremblay. 2001. Human alveolar macrophages express elafin and secretory leukocyte protease inhibitor. Z. Naturforsch., C 56:291.
    • (2001) Z. Naturforsch., C , vol.56 , pp. 291
    • Mihara, A.1    Tremblay, G.M.2
  • 17
    • 0000333702 scopus 로고
    • Production of cytokines by human gingival fibroblasts
    • S. Hamada, S. C. Holt, and J. R. McGhee, eds. Quintessence Publishing, Tokyo, Japan
    • Takada, H., J. Mihara, I. Morisaki, and S. Hamada. 1991. Production of cytokines by human gingival fibroblasts, In Periodontal Disease: Pathogens and Host Immune Responses. S. Hamada, S. C. Holt, and J. R. McGhee, eds. Quintessence Publishing, Tokyo, Japan, p. 265.
    • (1991) Periodontal Disease: Pathogens and Host Immune Responses , pp. 265
    • Takada, H.1    Mihara, J.2    Morisaki, I.3    Hamada, S.4
  • 18
    • 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
  • 19
    • 0034669918 scopus 로고    scopus 로고
    • Cleavage of CD14 on human gingival fibroblasts cocultured with activated neutrophils is mediated by human leukocyte elastase resulting in down-regulation of lipopolysaccharide-induced IL-8 production
    • Nemoto, E., S. Sugawara. H. Tada, H. Takada, H. Shimauchi, and H. Horiuchi. 2000. Cleavage of CD14 on human gingival fibroblasts cocultured with activated neutrophils is mediated by human leukocyte elastase resulting in down-regulation of lipopolysaccharide-induced IL-8 production. J. Immunol. 165:5807.
    • (2000) J. Immunol. , vol.165 , pp. 5807
    • Nemoto, E.1    Sugawara, S.2    Tada, H.3    Takada, H.4    Shimauchi, H.5    Horiuchi, H.6
  • 20
    • 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
  • 21
    • 0037651517 scopus 로고
    • Establishment of human tumor cell line (Ueda-1) derived from squamous cell carcinoma of the floor of the mouth
    • Miyauchi, S., T. Moroyama, T. Sakamoto, T. Okamoto, and K. Takada. 1985. Establishment of human tumor cell line (Ueda-1) derived from squamous cell carcinoma of the floor of the mouth. Jpn. J. Oral Maxillofac. Surg. 31:1347.
    • (1985) Jpn. J. Oral Maxillofac. Surg. , vol.31 , pp. 1347
    • Miyauchi, S.1    Moroyama, T.2    Sakamoto, T.3    Okamoto, T.4    Takada, K.5
  • 22
    • 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
  • 24
    • 0035017259 scopus 로고    scopus 로고
    • Secretion and gene expression of secretory leukocyte protease inhibitor by human airway submucosal glands
    • Saitoh, H., T. Masuda, S. Shimura, T. Fushimi, and K. Shirato. 2001. Secretion and gene expression of secretory leukocyte protease inhibitor by human airway submucosal glands. Am. J. Physiol. 280:L79.
    • (2001) Am. J. Physiol. , vol.280
    • Saitoh, H.1    Masuda, T.2    Shimura, S.3    Fushimi, T.4    Shirato, K.5
  • 25
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T. K., 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.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 26
    • 0030589624 scopus 로고    scopus 로고
    • Trypsin induced von Willebrand factor release from human endothelial cells is mediated by PAR-2 activation
    • Storck, J., B. Küsters, 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 , Issue.463
    • Storck, J.1    Küsters, B.2    Vahland, M.3    Morys-Wortmann, C.4    Zimmermann, E.R.5
  • 27
    • 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
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0025347444 scopus 로고
    • Skin-derived antileukoproteinase (SKALP): Characterization of two new elastase inhibitors from psoriatic epidermis
    • Schalkwijk, J., A. Chang, P. Janssen, G. J. de Jongh, and P. D Mier. 1990. Skin-derived antileukoproteinase (SKALP): characterization of two new elastase inhibitors from psoriatic epidermis. Br. J. Dermatol. 122:641.
    • (1990) Br. J. Dermatol. , vol.122 , pp. 641
    • Schalkwijk, J.1    Chang, A.2    Janssen, P.3    De Jongh, G.J.4    Mier, P.D.5
  • 34
    • 0025168332 scopus 로고
    • Elafin: An elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence
    • Wiedow, O., J. Schröder, H. Gregory, J. A. Young, and E. Christopher. 1990. Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J. Biol. Chem. 265:14791.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14791
    • Wiedow, O.1    Schröder, J.2    Gregory, H.3    Young, J.A.4    Christopher, E.5
  • 37
    • 0028389208 scopus 로고
    • Differential expression of protease inhibitor and small proline-rich protein genes between normal human oral tissue and odontogenic keratinocytes
    • Robinson, P. A., J. J. Marley, A. S. High, and W. J. Humw. 1994. Differential expression of protease inhibitor and small proline-rich protein genes between normal human oral tissue and odontogenic keratinocytes. Arch. Oral Biol. 39:251.
    • (1994) Arch. Oral Biol. , vol.39 , pp. 251
    • Robinson, P.A.1    Marley, J.J.2    High, A.S.3    Humw, W.J.4
  • 38
    • 0002346723 scopus 로고    scopus 로고
    • Leukocyte elastase
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA
    • Bieth, J. G. 1999. Leukocyte elastase. In Handbook of Proteolytic Enzymes. A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA, p. 54.
    • (1999) Handbook of Proteolytic Enzymes , pp. 54
    • Bieth, J.G.1
  • 39
    • 0002364218 scopus 로고    scopus 로고
    • Handbook of Proteolytic Enzymes
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA
    • Salvesen, G. S. 1999. Cathepsin G. In Handbook of Proteolytic Enzymes. A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA, p. 60.
    • (1999) , pp. 60
    • Salvesen, G.S.1    Cathepsin, G.2
  • 40
    • 0005950188 scopus 로고    scopus 로고
    • Myeloblastin
    • A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA
    • Hoidal, J. R. 1999. Myeloblastin. In Handbook of Proteolytic Enzymes. A. J. Barrett, N. D. Rawlings, and J. F. Woessner, eds. Academic Press, San Diego, CA, p. 62.
    • (1999) Handbook of Proteolytic Enzymes , pp. 62
    • Hoidal, J.R.1
  • 41
    • 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
  • 42
    • 0034745133 scopus 로고    scopus 로고
    • Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets
    • Cumashi, A., H. Ansuini, N. Celli, A. De Blasi, P. J. O'Brien, L. F. Brass, and M. Molino. 2001. Neutrophil proteases can inactivate human PAR3 and abolish the co-receptor function of PAR3 on murine platelets. Thromb. Haemostasis 85:533.
    • (2001) Thromb. Haemostasis , vol.85 , pp. 533
    • Cumashi, A.1    Ansuini, H.2    Celli, N.3    De Blasi, A.4    O'Brien, P.J.5    Brass, L.F.6    Molino, M.7
  • 44
    • 0032469877 scopus 로고    scopus 로고
    • Interactions between nonimmune 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 nonimmune 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
  • 45
    • 0031063446 scopus 로고    scopus 로고
    • Immunohistochemical study of cathepsin G and medullasin in inflamed gingival tissues from periodontal patients
    • Kunimatsu, K., Y. Ozaki, Y. Hara, Y. Aoki, K. Yamamoto, and I. Kato. 1997, Immunohistochemical study of cathepsin G and medullasin in inflamed gingival tissues from periodontal patients. J. Periodont. Res. 32:264.
    • (1997) J. Periodont. Res. , vol.32 , pp. 264
    • Kunimatsu, K.1    Ozaki, Y.2    Hara, Y.3    Aoki, Y.4    Yamamoto, K.5    Kato, I.6
  • 47
    • 0031305785 scopus 로고    scopus 로고
    • Subgingival temperature: Relation to gingival crevicular fluid enzymes, cytokines, and subgingival plaque micro-organisms
    • Wolff, L. F., N. J. Koller, Q. T. Smith, A. Mathur, and D. Aeppli. 1997. Subgingival temperature: relation to gingival crevicular fluid enzymes, cytokines, and subgingival plaque micro-organisms. J. Clin. Periodontol. 24:900.
    • (1997) J. Clin. Periodontol. , vol.24 , pp. 900
    • Wolff, L.F.1    Koller, N.J.2    Smith, Q.T.3    Mathur, A.4    Aeppli, D.5
  • 48
    • 0028787054 scopus 로고
    • Nonisotropic enzyme-inhibitor interactions: A novel nonoxidative mechanism for quantum proteolysis by human neutrophils
    • Liou, T. G., and E. J. Campbell. 1995. Nonisotropic enzyme-inhibitor interactions: a novel nonoxidative mechanism for quantum proteolysis by human neutrophils. Biochemistry 34:16171.
    • (1995) Biochemistry , vol.34 , pp. 16171
    • Liou, T.G.1    Campbell, E.J.2
  • 49
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen, C. A., M. A. Campbell. P. L. Sannes, S. S. Boukedes, and E. J. Campbell. 1995. Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131:775.
    • (1995) J. Cell Biol. , vol.131 , pp. 775
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 50
    • 0030948848 scopus 로고    scopus 로고
    • Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity
    • Owen, C. A., M. A. Campbell, S. S. Boukedes, and E. J. Campbell. 1997. Cytokines regulate membrane-bound leukocyte elastase on neutrophils: a novel mechanism for effector activity. Am. J. Physiol. 272:L385.
    • (1997) Am. J. Physiol. , vol.272
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 51
    • 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
  • 52
    • 0034704593 scopus 로고    scopus 로고
    • Control of TH2 polarization by the chemokine monocyte chemoattractant proein-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 proein-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
  • 53
    • 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
  • 55
    • 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
  • 56
    • 0035184146 scopus 로고    scopus 로고
    • Protease-activated receptors in human airways: Upregulation 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: upregulation 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


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