메뉴 건너뛰기




Volumn 75, Issue 1, 2007, Pages 164-174

Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2

Author keywords

[No Author keywords available]

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 6; INTERLEUKIN 8; MESSENGER RNA; PEPTIDE; PROTEINASE; PROTEINASE ACTIVATED RECEPTOR 2; RECEPTOR BLOCKING AGENT; SERRALYSIN; TRYPSIN; TRYPTASE; UNCLASSIFIED DRUG;

EID: 33845995107     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.01239-06     Document Type: Article
Times cited : (88)

References (63)
  • 1
    • 33646368158 scopus 로고    scopus 로고
    • The house dust mite allergen Der p 1, unlike Der p 3, stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism
    • Adam, E., K. K. Hansen, O. F. Astudillo, L. Coulon, F. Bex, X. Duhant, E. Jaumotte, M. D. Hollenberg, and A. Jacquet. 2006. The house dust mite allergen Der p 1, unlike Der p 3, stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism. J. Biol. Chem. 281:6910-6923.
    • (2006) J. Biol. Chem , vol.281 , pp. 6910-6923
    • Adam, E.1    Hansen, K.K.2    Astudillo, O.F.3    Coulon, L.4    Bex, F.5    Duhant, X.6    Jaumotte, E.7    Hollenberg, M.D.8    Jacquet, A.9
  • 2
    • 0036151657 scopus 로고    scopus 로고
    • Modified proteinase-activated receptor-1 and -2 derived peptides inhibit proteinase-activated receptor-2 activation by trypsin
    • Al-Ani, B., M. Saifeddine, S. J. Wijesuriya, and M. D. Hollenberg. 2002. Modified proteinase-activated receptor-1 and -2 derived peptides inhibit proteinase-activated receptor-2 activation by trypsin. J. Pharmacol. Exp. Ther. 300:702-708.
    • (2002) J. Pharmacol. Exp. Ther , vol.300 , pp. 702-708
    • Al-Ani, B.1    Saifeddine, M.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 3
    • 0034946406 scopus 로고    scopus 로고
    • Colonization and infection by Serratia species in a paediatric surgical intensive care unit
    • Albers, M. J., J. W. Mouton, and D. Tibboel. 2001. Colonization and infection by Serratia species in a paediatric surgical intensive care unit. J. Hosp. Infect. 48:7-12.
    • (2001) J. Hosp. Infect , vol.48 , pp. 7-12
    • Albers, M.J.1    Mouton, J.W.2    Tibboel, D.3
  • 4
    • 0037108373 scopus 로고    scopus 로고
    • House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: The cysteine protease allergen, Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1
    • Asokananthan, N., P. T. Graham, D. J. Stewart, A. J. Bakker, K. A. Eidne, P. J. Thompson, and G. A. Stewart. 2002. House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: the cysteine protease allergen, Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1. J. Immunol. 169:4572-4578.
    • (2002) J. Immunol , vol.169 , pp. 4572-4578
    • Asokananthan, N.1    Graham, P.T.2    Stewart, D.J.3    Bakker, A.J.4    Eidne, K.A.5    Thompson, P.J.6    Stewart, G.A.7
  • 5
    • 0031757918 scopus 로고    scopus 로고
    • Antibiotic resistance and putative virulence factors of Serratia marcescens with respect to O and K serotypes
    • Aucken, H. M., and T. L. Pitt. 1998. Antibiotic resistance and putative virulence factors of Serratia marcescens with respect to O and K serotypes. J. Med. Microbiol. 47:1105-1113.
    • (1998) J. Med. Microbiol , vol.47 , pp. 1105-1113
    • Aucken, H.M.1    Pitt, T.L.2
  • 6
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A., and D. Baltimore. 1996. NF-κB: ten years after. Cell 87: 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas, R., J. Manos, and R. Suvanasuthi. 2004. Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides. Infect. Immun. 72:5159-5167.
    • (2004) Infect. Immun , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 9
    • 0033395306 scopus 로고    scopus 로고
    • Proteases from Aspergillus fumigatus induce interleukin (IL)-6 and IL-8 production in airway epithelial cell lines by transcriptional mechanisms
    • Borger, P., G. H. Koeter, J. A. Timmerman, E. Vellenga, J. F. Tomee, and H. F. Kauffman. 1999. Proteases from Aspergillus fumigatus induce interleukin (IL)-6 and IL-8 production in airway epithelial cell lines by transcriptional mechanisms. J. Infect. Dis. 180:1267-1274.
    • (1999) J. Infect. Dis , vol.180 , pp. 1267-1274
    • Borger, P.1    Koeter, G.H.2    Timmerman, J.A.3    Vellenga, E.4    Tomee, J.F.5    Kauffman, H.F.6
  • 10
    • 0030036130 scopus 로고    scopus 로고
    • Serratia marcescens nosocomial outbreak due to contamination of hexetidine solution
    • Bosi, C., A. Davin-Regli, R. Charrel, B. Rocca, D. Monnet, and C. Bollet. 1996. Serratia marcescens nosocomial outbreak due to contamination of hexetidine solution. J. Hosp. Infect. 33:217-224.
    • (1996) J. Hosp. Infect , vol.33 , pp. 217-224
    • Bosi, C.1    Davin-Regli, A.2    Charrel, R.3    Rocca, B.4    Monnet, D.5    Bollet, C.6
  • 12
    • 6344248652 scopus 로고    scopus 로고
    • Protease-activated receptor signaling increases epithelial antimicrobial peptide expression
    • Chung, W. O., S. R. Hansen, D. Rao, and B. A. Dale. 2004. Protease-activated receptor signaling increases epithelial antimicrobial peptide expression. J. Immunol. 173:5165-5170.
    • (2004) J. Immunol , vol.173 , pp. 5165-5170
    • Chung, W.O.1    Hansen, S.R.2    Rao, D.3    Dale, B.A.4
  • 13
    • 0034748449 scopus 로고    scopus 로고
    • Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase
    • Compton, S. J., B. Renaux, S. J. Wijesuriya, and M. D. Hollenberg. 2001. Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase. Br. J. Pharmacol. 134:705-718.
    • (2001) Br. J. Pharmacol , vol.134 , pp. 705-718
    • Compton, S.J.1    Renaux, B.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 14
    • 0036905071 scopus 로고    scopus 로고
    • Glycosylation of human proteinase-activated receptor-2 (hPAR2): Role in cell surface expression and signalling
    • Compton, S. J., S. Sandhu, S. J. Wijesuriya, and M. D. Hollenberg. 2002. Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling. Biochem. J. 368:495-505.
    • (2002) Biochem. J , vol.368 , pp. 495-505
    • Compton, S.J.1    Sandhu, S.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 15
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery, 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-C1452.
    • (1998) Am. J. Physiol , vol.274
    • Dery, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 18
    • 0030735655 scopus 로고    scopus 로고
    • An epidemiological study of Serratia marcescens isolates from nosocomial infections by enzyme electrophoresis
    • Goullet, P., and B. Picard. 1997. An epidemiological study of Serratia marcescens isolates from nosocomial infections by enzyme electrophoresis. J. Med. Microbiol. 46:1019-1028.
    • (1997) J. Med. Microbiol , vol.46 , pp. 1019-1028
    • Goullet, P.1    Picard, B.2
  • 19
    • 0036445391 scopus 로고    scopus 로고
    • Antimicrobial activity and stability to proteolysis of small linear cationic peptides with D-amino acid substitutions
    • Hamamoto, K., Y. Kida, Y. Zhang, T. Shimizu, and K. Kuwano. 2002. Antimicrobial activity and stability to proteolysis of small linear cationic peptides with D-amino acid substitutions. Microbiol. Immunol. 46:741-749.
    • (2002) Microbiol. Immunol , vol.46 , pp. 741-749
    • Hamamoto, K.1    Kida, Y.2    Zhang, Y.3    Shimizu, T.4    Kuwano, K.5
  • 22
    • 0023774771 scopus 로고
    • Genetic analysis of extracellular proteins of Serratia marcescens
    • Hines, D. A., P. N. Saurugger, G. M. Ihler, and M. J. Benedik. 1988. Genetic analysis of extracellular proteins of Serratia marcescens. J. Bacteriol. 170: 4141-4146.
    • (1988) J. Bacteriol , vol.170 , pp. 4141-4146
    • Hines, D.A.1    Saurugger, P.N.2    Ihler, G.M.3    Benedik, M.J.4
  • 23
    • 0036262319 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXVIII. Proteinase-activated receptors
    • Hollenberg, M. D., and S. J. Compton. 2002. International Union of Pharmacology. XXVIII. Proteinase-activated receptors. Pharmacol. Rev. 54:203-217.
    • (2002) Pharmacol. Rev , vol.54 , pp. 203-217
    • Hollenberg, M.D.1    Compton, S.J.2
  • 24
    • 0031958730 scopus 로고    scopus 로고
    • The protease-activated receptors and their cellular expression and function in blood-related cells
    • Hou, L., G. L. Howells, S. Kapas, and M. G. Macey. 1998. The protease-activated receptors and their cellular expression and function in blood-related cells. Br. J. Haematol. 101:1-9.
    • (1998) Br. J. Haematol , vol.101 , pp. 1-9
    • Hou, L.1    Howells, G.L.2    Kapas, S.3    Macey, M.G.4
  • 26
    • 0022143023 scopus 로고
    • The serratial 56K protease as a major pathogenic factor in serratial keratitis. Clinical and experimental study
    • Kamata, R., K. Matsumoto, R. Okamura, T. Yamamoto, and H. Maeda. 1985. The serratial 56K protease as a major pathogenic factor in serratial keratitis. Clinical and experimental study. Ophthalmology 92:1452-1459.
    • (1985) Ophthalmology , vol.92 , pp. 1452-1459
    • Kamata, R.1    Matsumoto, K.2    Okamura, R.3    Yamamoto, T.4    Maeda, H.5
  • 27
    • 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. 276:31657-31666.
    • (2001) J. Biol. Chem , vol.276 , pp. 31657-31666
    • Kanke, T.1    Macfarlane, S.R.2    Seatter, M.J.3    Davenport, E.4    Paul, A.5    McKenzie, R.C.6    Plevin, R.7
  • 28
    • 0033933005 scopus 로고    scopus 로고
    • Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production
    • Kauffman, H. F., J. F. Tomee, M. A. van de Riet, A. J. Timmerman, and P. Borger. 2000. Protease-dependent activation of epithelial cells by fungal allergens leads to morphologic changes and cytokine production. J. Allergy Clin. Immunol. 105:1185-1193.
    • (2000) J. Allergy Clin. Immunol , vol.105 , pp. 1185-1193
    • Kauffman, H.F.1    Tomee, J.F.2    van de Riet, M.A.3    Timmerman, A.J.4    Borger, P.5
  • 30
    • 0035168317 scopus 로고    scopus 로고
    • Acholeplasma laidlawii up-regulates granulysin gene expression via transcription factor activator protein-1 in a human monocytic cell line, THP-1
    • Kida, Y., K. Kuwano, Y. Zhang, and S. Arai. 2001. Acholeplasma laidlawii up-regulates granulysin gene expression via transcription factor activator protein-1 in a human monocytic cell line, THP-1. Immunology 104:324-332.
    • (2001) Immunology , vol.104 , pp. 324-332
    • Kida, Y.1    Kuwano, K.2    Zhang, Y.3    Arai, S.4
  • 31
    • 11144337658 scopus 로고    scopus 로고
    • Conditional expression of liver-enriched transcriptional activator protein augments Acholeplasma laidlawii-induced granulysin gene expression in a human monocytic cell line, THP-1
    • Kida, Y., T. Shimizu, and K. Kuwano. 2005. Conditional expression of liver-enriched transcriptional activator protein augments Acholeplasma laidlawii-induced granulysin gene expression in a human monocytic cell line, THP-1. Immunology 114:121-132.
    • (2005) Immunology , vol.114 , pp. 121-132
    • Kida, Y.1    Shimizu, T.2    Kuwano, K.3
  • 32
    • 0036884082 scopus 로고    scopus 로고
    • Opposing roles of activator protein-1 and CCAAT/enhancer binding protein beta in the regulation of inducible granulysin gene expression in a human monocytic cell line, THP-1
    • Kida, Y., T. Shimizu, and K. Kuwano. 2002. Opposing roles of activator protein-1 and CCAAT/enhancer binding protein beta in the regulation of inducible granulysin gene expression in a human monocytic cell line, THP-1. Immunology 107:507-516.
    • (2002) Immunology , vol.107 , pp. 507-516
    • Kida, Y.1    Shimizu, T.2    Kuwano, K.3
  • 33
    • 33645046361 scopus 로고    scopus 로고
    • Sodium butyrate up-regulates cathelicidin gene expression via activator protein-1 and histone acetylation at the promoter region in a human lung epithelial cell line, EBC-1
    • Kida, Y., T. Shimizu, and K. Kuwano. 2006. Sodium butyrate up-regulates cathelicidin gene expression via activator protein-1 and histone acetylation at the promoter region in a human lung epithelial cell line, EBC-1. Mol. Immunol. 43:1972-1981.
    • (2006) Mol. Immunol , vol.43 , pp. 1972-1981
    • Kida, Y.1    Shimizu, T.2    Kuwano, K.3
  • 34
    • 0032193198 scopus 로고    scopus 로고
    • Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium
    • King, C., S. Brennan, P. J. Thompson, and G. A. Stewart. 1998. Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium. J. Immunol. 161:3645-3651.
    • (1998) J. Immunol , vol.161 , pp. 3645-3651
    • King, C.1    Brennan, S.2    Thompson, P.J.3    Stewart, G.A.4
  • 37
    • 0029907110 scopus 로고    scopus 로고
    • Role of microbial proteases in pathogenesis
    • Maeda, H. 1996. Role of microbial proteases in pathogenesis. Microbiol. Immunol. 40:685-699.
    • (1996) Microbiol. Immunol , vol.40 , pp. 685-699
    • Maeda, H.1
  • 38
    • 0024832373 scopus 로고
    • Pathogenic potentials of bacterial proteases
    • Maeda, H., and A. Molla. 1989. Pathogenic potentials of bacterial proteases. Clin. Chim. Acta 185:357-367.
    • (1989) Clin. Chim. Acta , vol.185 , pp. 357-367
    • Maeda, H.1    Molla, A.2
  • 39
    • 0029072045 scopus 로고
    • Serralysin and related bacterial proteinases
    • Maeda, H., and K. Morihara. 1995. Serralysin and related bacterial proteinases. Methods Enzymol. 248:395-413.
    • (1995) Methods Enzymol , vol.248 , pp. 395-413
    • Maeda, H.1    Morihara, K.2
  • 40
    • 0021335808 scopus 로고
    • Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958
    • Matsumoto, K., H. Maeda, K. Takata, R. Kamata, and R. Okamura. 1984. Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958. J. Bacteriol. 157:225-232.
    • (1984) J. Bacteriol , vol.157 , pp. 225-232
    • Matsumoto, K.1    Maeda, H.2    Takata, K.3    Kamata, R.4    Okamura, R.5
  • 41
    • 0021168136 scopus 로고
    • Pathogenesis of serratial infection: Activation of the Hageman factor-prekallikrein cascade by serratial protease
    • Matsumoto, K., T. Yamamoto, R. Kamata, and H. Maeda. 1984. Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease. J. Biochem. 96:739-749.
    • (1984) J. Biochem , vol.96 , pp. 739-749
    • Matsumoto, K.1    Yamamoto, T.2    Kamata, R.3    Maeda, H.4
  • 42
    • 0022514886 scopus 로고
    • Degradation of protease inhibitors, immunoglobulins, and other serum proteins by Serratia protease and its toxicity to fibroblast in culture
    • Molla, A., K. Matsumoto, I. Oyamada, T. Katsuki, and H. Maeda. 1986. Degradation of protease inhibitors, immunoglobulins, and other serum proteins by Serratia protease and its toxicity to fibroblast in culture. Infect. Immun. 53:522-529.
    • (1986) Infect. Immun , vol.53 , pp. 522-529
    • Molla, A.1    Matsumoto, K.2    Oyamada, I.3    Katsuki, T.4    Maeda, H.5
  • 43
    • 33644980644 scopus 로고    scopus 로고
    • The effect of continuous veno-venous hemofiltration or direct hemoperfusion with polymyxin B-immobilized fiber on neutrophil respiratory oxidative burst in patients with sepsis and septic shock
    • Naka, T., M. Shinozaki, T. Akizawa, Y. Shima, H. Takaesu, and H. Nasu. 2006. The effect of continuous veno-venous hemofiltration or direct hemoperfusion with polymyxin B-immobilized fiber on neutrophil respiratory oxidative burst in patients with sepsis and septic shock. Ther. Apher. Dial. 10:7-11.
    • (2006) Ther. Apher. Dial , vol.10 , pp. 7-11
    • Naka, T.1    Shinozaki, M.2    Akizawa, T.3    Shima, Y.4    Takaesu, H.5    Nasu, H.6
  • 45
    • 0029113121 scopus 로고
    • Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2
    • Nystedt, S., K. Emilsson, A. K. Larsson, B. Strombeck, and J. Sundelin. 1995. Molecular cloning and functional expression of the gene encoding the human proteinase-activated receptor 2. Eur. J. Biochem. 232:84-89.
    • (1995) Eur. J. Biochem , vol.232 , pp. 84-89
    • Nystedt, S.1    Emilsson, K.2    Larsson, A.K.3    Strombeck, B.4    Sundelin, J.5
  • 46
    • 15844401726 scopus 로고    scopus 로고
    • The proteinase-activated receptor 2 is induced by inflammatory mediators in human endothelial cells: Comparison with the 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 the thrombin receptor. J. Biol. Chem. 271:14910-14915.
    • (1996) J. Biol. Chem , vol.271 , pp. 14910-14915
    • Nystedt, S.1    Ramakrishnan, V.2    Sundelin, J.3
  • 47
    • 1642279517 scopus 로고    scopus 로고
    • Protease-activated receptors: Contribution to physiology and disease
    • Ossovskaya, V. S., and N. W. Bunnett. 2004. Protease-activated receptors: contribution to physiology and disease. Physiol. Rev. 84:579-621.
    • (2004) Physiol. Rev , vol.84 , pp. 579-621
    • Ossovskaya, V.S.1    Bunnett, N.W.2
  • 48
    • 15044340298 scopus 로고    scopus 로고
    • German cockroach proteases regulate interleukin-8 expression via nuclear factor for interleukin-6 in human bronchial epithelial cells
    • Page, K., V. S. Hughes, K. K. Odoms, K. E. Dunsmore, and M. B. Hershenson. 2005. German cockroach proteases regulate interleukin-8 expression via nuclear factor for interleukin-6 in human bronchial epithelial cells. Am. J. Respir. Cell Mol. Biol. 32:225-231.
    • (2005) Am. J. Respir. Cell Mol. Biol , vol.32 , pp. 225-231
    • Page, K.1    Hughes, V.S.2    Odoms, K.K.3    Dunsmore, K.E.4    Hershenson, M.B.5
  • 49
    • 0032491401 scopus 로고    scopus 로고
    • The role of C/EBP isoforms in the control of inflammatory and native immunity functions
    • Poli, V. 1998. The role of C/EBP isoforms in the control of inflammatory and native immunity functions. J. Biol. Chem. 273:29279- 29282.
    • (1998) J. Biol. Chem , vol.273 , pp. 29279-29282
    • Poli, V.1
  • 50
    • 0036683653 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding proteins: Structure, function and regulation
    • Ramji, D. P., and P. Foka. 2002. CCAAT/enhancer-binding proteins: structure, function and regulation. Biochem. J. 365:561-575.
    • (2002) Biochem. J , vol.365 , pp. 561-575
    • Ramji, D.P.1    Foka, P.2
  • 51
    • 7944224566 scopus 로고    scopus 로고
    • The role of protease activation of inflammation in allergic respiratory diseases
    • Reed, C. E., and H. Kita. 2004. The role of protease activation of inflammation in allergic respiratory diseases. J. Allergy Clin. Immunol. 114:997-1008.
    • (2004) J. Allergy Clin. Immunol , vol.114 , pp. 997-1008
    • Reed, C.E.1    Kita, H.2
  • 52
    • 0035874536 scopus 로고    scopus 로고
    • Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1
    • Riewald, M., V. V. Kravchenko, R. J. Petrovan, P. J. O'Brien, L. F. Brass, R. J. Ulevitch, and W. Ruf. 2001. Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1. Blood 97:3109-3116.
    • (2001) Blood , vol.97 , pp. 3109-3116
    • Riewald, M.1    Kravchenko, V.V.2    Petrovan, R.J.3    O'Brien, P.J.4    Brass, L.F.5    Ulevitch, R.J.6    Ruf, W.7
  • 54
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen, A., I. M. Frick, E. Andersson, H. Tapper, and L. Bjorck. 2002. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol. Microbiol. 46:157-168.
    • (2002) Mol. Microbiol , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 57
    • 0031577276 scopus 로고    scopus 로고
    • The allergen Der p1 induces NF-κB activation through interference with IκB α function in asthmatic bronchial epithelial cells
    • Stacey, M. A., G. Sun, G. Vassalli, M. Marini, A. Bellini, and S. Mattoli. 1997. The allergen Der p1 induces NF-κB activation through interference with IκB α function in asthmatic bronchial epithelial cells. Biochem. Biophys. Res. Commun. 236:522-526.
    • (1997) Biochem. Biophys. Res. Commun , vol.236 , pp. 522-526
    • Stacey, M.A.1    Sun, G.2    Vassalli, G.3    Marini, M.4    Bellini, A.5    Mattoli, S.6
  • 58
    • 0035879347 scopus 로고    scopus 로고
    • Interaction of mite allergens Der p3 and Der p9 with protease-activated receptor-2 expressed by lung epithelial cells
    • Sun, G., M. A. Stacey, M. Schmidt, L. Mori, and S. Mattoli. 2001. Interaction of mite allergens Der p3 and Der p9 with protease-activated receptor-2 expressed by lung epithelial cells. J. Immunol. 167:1014-1021.
    • (2001) J. Immunol , vol.167 , pp. 1014-1021
    • Sun, G.1    Stacey, M.A.2    Schmidt, M.3    Mori, L.4    Mattoli, S.5
  • 59
    • 0028986193 scopus 로고
    • NF-κβ: A lesson in family values
    • Thanos, D., and T. Maniatis. 1995. NF-κβ: a lesson in family values. Cell 80:529-532.
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 60
    • 0030941873 scopus 로고    scopus 로고
    • Proteases from Aspergillus fumigatus induce release of proinflammatory cytokines and cell detachment in airway epithelial cell lines
    • Tomee, J. F., A. T. Wierenga, P. S. Hiemstra, and H. K. Kauffman. 1997. Proteases from Aspergillus fumigatus induce release of proinflammatory cytokines and cell detachment in airway epithelial cell lines. J. Infect. Dis. 176:300-303.
    • (1997) J. Infect. Dis , vol.176 , pp. 300-303
    • Tomee, J.F.1    Wierenga, A.T.2    Hiemstra, P.S.3    Kauffman, H.K.4
  • 61
    • 0037797300 scopus 로고    scopus 로고
    • . Uehara, A., K. Muramoto, H. Takada, and S. Sugawara. 2003. Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2. J. Immunol. 170:5690-5696.
    • . Uehara, A., K. Muramoto, H. Takada, and S. Sugawara. 2003. Neutrophil serine proteinases activate human nonepithelial cells to produce inflammatory cytokines through protease-activated receptor 2. J. Immunol. 170:5690-5696.
  • 62
    • 0030797701 scopus 로고    scopus 로고
    • Serratia marcescens infections in neonatal departments: Description of an outbreak and review of the literature
    • van Ogtrop, M. L., D. van Zoeren-Grobben, E. M. Verbakel-Salomons, and C. P. van Boven. 1997. Serratia marcescens infections in neonatal departments: description of an outbreak and review of the literature. J. Hosp. Infect. 36:95-103.
    • (1997) J. Hosp. Infect , vol.36 , pp. 95-103
    • van Ogtrop, M.L.1    van Zoeren-Grobben, D.2    Verbakel-Salomons, E.M.3    van Boven, C.P.4
  • 63
    • 0018745943 scopus 로고
    • Serratia marcescens: Historical perspective and clinical review
    • Yu, V. L. 1979. Serratia marcescens: historical perspective and clinical review. N. Engl. J. Med. 300:887-893.
    • (1979) N. Engl. J. Med , vol.300 , pp. 887-893
    • Yu, V.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.