메뉴 건너뛰기




Volumn 7, Issue 2, 2002, Pages 130-136

Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: Activity is dependent on interaction with cell surface CD14

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; CD14 ANTIGEN; CHAPERONIN; CYTOKINE; GAMMA INTERFERON; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 10; INTERLEUKIN 12; INTERLEUKIN 1BETA; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 8; NEUTRALIZING ANTIBODY; TUMOR NECROSIS FACTOR ALPHA;

EID: 0036556704     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2002)007<0130:RLCBNC>2.0.CO;2     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 0034177888 scopus 로고    scopus 로고
    • Cutting edge: Cell surface expression and lipopolysaccharide signaling via the toll-like receptor 4-MD-2 complex on mouse peritoneal macrophages
    • Akashi S, Shimazu R, Ogata H, Nagai Y, Takeda K, Kimoto M, Miyake K. 2000. Cutting edge: cell surface expression and lipopolysaccharide signaling via the toll-like receptor 4-MD-2 complex on mouse peritoneal macrophages. J Immunol 164: 3471-3475.
    • (2000) J Immunol , vol.164 , pp. 3471-3475
    • Akashi, S.1    Shimazu, R.2    Ogata, H.3    Nagai, Y.4    Takeda, K.5    Kimoto, M.6    Miyake, K.7
  • 2
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • Chen W, Syldath U, Bellmann K, Burkart V, Kolb H. 1999. Human 60-kDa heat-shock protein: a danger signal to the innate immune system. J Immunol 162: 3212-3219.
    • (1999) J Immunol , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 3
    • 0033574415 scopus 로고    scopus 로고
    • Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction
    • Chow JC, Young DW, Golenbock DT, Christ WJ, Gusovsky E 1999. Toll-like receptor-4 mediates lipopolysaccharide-induced signal transduction. J Biol Chem 274: 10689-10692.
    • (1999) J Biol Chem , vol.274 , pp. 10689-10692
    • Chow, J.C.1    Young, D.W.2    Golenbock, D.T.3    Christ, W.J.4    Gusovsky, E.5
  • 5
    • 0033575308 scopus 로고    scopus 로고
    • Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form
    • Erbse A, Yifrach O, Jones S, Lund PA. 1999. Chaperone activity of a chimeric GroEL protein that can exist in a single or double ring form. J Biol Chem 274: 20351-20357
    • (1999) J Biol Chem , vol.274 , pp. 20351-20357
    • Erbse, A.1    Yifrach, O.2    Jones, S.3    Lund, P.A.4
  • 6
    • 0027472869 scopus 로고
    • Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells
    • Friedland JS, Shattock R, Remick DG, Griffin GE. 1993. Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells. Clin Exp Immunol 91: 58-62.
    • (1993) Clin Exp Immunol , vol.91 , pp. 58-62
    • Friedland, J.S.1    Shattock, R.2    Remick, D.G.3    Griffin, G.E.4
  • 7
    • 0031888740 scopus 로고    scopus 로고
    • GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells
    • Frisk A, Ison CA, Lagergard T. 1998. GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells. Infect Immun 66: 1252-1257.
    • (1998) Infect Immun , vol.66 , pp. 1252-1257
    • Frisk, A.1    Ison, C.A.2    Lagergard, T.3
  • 8
    • 0031030347 scopus 로고    scopus 로고
    • Cytokine and adhesion molecule expression in human monocytes and endothelial cells stimulated with bacterial heat shock proteins
    • Galdiero M, Cippolaro de L-Ero G, Marcatili A. 1997. Cytokine and adhesion molecule expression in human monocytes and endothelial cells stimulated with bacterial heat shock proteins. Infect Immun 65: 699-707.
    • (1997) Infect Immun , vol.65 , pp. 699-707
    • Galdiero, M.1    Cippolaro de L-Ero, G.2    Marcatili, A.3
  • 9
    • 0027335914 scopus 로고
    • Mutation Ala2→Ser destabilizes intersubunit interactions in the molecular chaperone GroEL
    • Horovitz A, Bochkareva ES, Kovalenko O, Girshovich AS. 1993. Mutation Ala2→Ser destabilizes intersubunit interactions in the molecular chaperone GroEL. J Mol Biol 231: 58-64.
    • (1993) J Mol Biol , vol.231 , pp. 58-64
    • Horovitz, A.1    Bochkareva, E.S.2    Kovalenko, O.3    Girshovich, A.S.4
  • 10
    • 0030846353 scopus 로고    scopus 로고
    • Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum legiiminosarum groEL homologue at 37°C but not at 43°C
    • Ivic A, Olden D, Wallington EJ, Lund PA. 1997. Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum legiiminosarum groEL homologue at 37°C but not at 43°C. Gene 194: 1-8.
    • (1997) Gene , vol.194 , pp. 1-8
    • Ivic, A.1    Olden, D.2    Wallington, E.J.3    Lund, P.A.4
  • 11
    • 0029091268 scopus 로고
    • The potent bone resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL
    • Kirby AC, Meghji S, Nair SP, et al. 1995. The potent bone resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL. J Clin Investig 96: 1185-1194.
    • (1995) J Clin Investig , vol.96 , pp. 1185-1194
    • Kirby, A.C.1    Meghji, S.2    Nair, S.P.3
  • 12
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol A, Lichtman AH, Finberg RW, Libby P, Kurt-Jones EA. 2000. Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J Immunol 164: 13-17.
    • (2000) J Immunol , vol.164 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 13
    • 1842412518 scopus 로고    scopus 로고
    • TNF-alpha, IL-1 alpha, IL-6, and ICAM-1 expression in human keratinocytes stimulated in vitro with Escherichia coli heat-shock proteins
    • Marcatili A, Cipollaro de l'Ero G, Galdiero M, Folgore A, Petrillo G. 1997. TNF-alpha, IL-1 alpha, IL-6, and ICAM-1 expression in human keratinocytes stimulated in vitro with Escherichia coli heat-shock proteins. Microbiology 143: 45-53.
    • (1997) Microbiology , vol.143 , pp. 45-53
    • Marcatili, A.1    Cipollaro de l'Ero, G.2    Galdiero, M.3    Folgore, A.4    Petrillo, G.5
  • 14
    • 0030728057 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: A potential contributory factor in Pott's disease
    • Meghji S, White PA, Nair SP, et al. 1997. Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: a potential contributory factor in Pott's disease. J Exp Med 186: 1241-1246.
    • (1997) J Exp Med , vol.186 , pp. 1241-1246
    • Meghji, S.1    White, P.A.2    Nair, S.P.3
  • 15
    • 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, Burkart V, Flohe S, Kolb H. 2000. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J Immunol 164: 558-561.
    • (2000) J Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 16
    • 0032896726 scopus 로고    scopus 로고
    • Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals
    • Pockley AG, Bulmer J, Hanks BM, Wright BH. 1999. Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals. Cell Stress Chaperones 4: 29-35.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 29-35
    • Pockley, A.G.1    Bulmer, J.2    Hanks, B.M.3    Wright, B.H.4
  • 18
    • 85012505857 scopus 로고    scopus 로고
    • Chaperonins are cell-signaling proteins: The unfolding biology of molecular chaperones
    • 15 September
    • Ranford J, Coates ARM, Henderson B. 2000. Chaperonins are cell-signaling proteins: the unfolding biology of molecular chaperones. Exp Rev Mol Med 15 September. Available at http://www-ermm.cbcu.cam.ac.uk/00002015h.htm.
    • (2000) Exp Rev Mol Med
    • Ranford, J.1    Coates, A.R.M.2    Henderson, B.3
  • 19
    • 0031830486 scopus 로고    scopus 로고
    • The Escherichia coli chaperonin 60 (groEL) is a potent stimulator of osteoclast formation
    • Reddi K, Meghji S, Nair SP, et al. 1998. The Escherichia coli chaperonin 60 (groEL) is a potent stimulator of osteoclast formation. J Bone Miner Res 13: 1260-1266.
    • (1998) J Bone Miner Res , vol.13 , pp. 1260-1266
    • Reddi, K.1    Meghji, S.2    Nair, S.P.3
  • 21
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • Soltys BJ, Gupta RS. 1997. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol Int 21: 315-320.
    • (1997) Cell Biol Int , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 22
    • 0029874051 scopus 로고    scopus 로고
    • The myeloid differentiation antigen CD14 is N-and O-glycosylated. Contribution of N-linked glycosylation to different soluble CD14 isoforms
    • Stelter F, Pfister M, Bernheiden M, Jack RS, Bufler P, Engelmann H, Schutt C. 1996. The myeloid differentiation antigen CD14 is N-and O-glycosylated. Contribution of N-linked glycosylation to different soluble CD14 isoforms. Eur J Biochem 236: 457-464.
    • (1996) Eur J Biochem , vol.236 , pp. 457-464
    • Stelter, F.1    Pfister, M.2    Bernheiden, M.3    Jack, R.S.4    Bufler, P.5    Engelmann, H.6    Schutt, C.7
  • 23
    • 0029890168 scopus 로고    scopus 로고
    • Endotoxin signal transduction in macrophages
    • Sweet MJ, Hume DA. 1996. Endotoxin signal transduction in macrophages. J Leukoc Biol 60: 8-26.
    • (1996) J Leukoc Biol , vol.60 , pp. 8-26
    • Sweet, M.J.1    Hume, D.A.2
  • 24
    • 7344240408 scopus 로고    scopus 로고
    • Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation
    • Tabona P, Reddi K, Khan S, et al. 1998. Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. J Immunol 161: 1414-1421.
    • (1998) J Immunol , vol.161 , pp. 1414-1421
    • Tabona, P.1    Reddi, K.2    Khan, S.3
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0028091148 scopus 로고
    • Rhizobium leguminosarum contains multiple chaperonin (Cpn60) genes
    • Wallington EJ, Lund PA. 1994. Rhizobium leguminosarum contains multiple chaperonin (Cpn60) genes. Microbiology 140: 113-122.
    • (1994) Microbiology , vol.140 , pp. 113-122
    • Wallington, E.J.1    Lund, P.A.2
  • 27
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright SD, Ramos RA, Tobias PS, Ulevitch RJ, Mathison JC. 1990. CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 249: 1431-1433.
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 28
    • 0034604242 scopus 로고    scopus 로고
    • Serum soluble heat shock protein 60 is elevated in subjects with atherosclerosis in a general population
    • Xu Q, Schett G, Perschinka H, et al. 2000. Serum soluble heat shock protein 60 is elevated in subjects with atherosclerosis in a general population. Circulation 102: 14-20.
    • (2000) Circulation , vol.102 , pp. 14-20
    • Xu, Q.1    Schett, G.2    Perschinka, H.3
  • 29
    • 0029742511 scopus 로고    scopus 로고
    • Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helicobacter pylori
    • Yamaguchi H, Osaki T, Taguchi H, Hanawa T, Yamamoto T, Kamiya S. 1996. Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helicobacter pylori. J Med Microbiol 45: 270-277.
    • (1996) J Med Microbiol , vol.45 , pp. 270-277
    • Yamaguchi, H.1    Osaki, T.2    Taguchi, H.3    Hanawa, T.4    Yamamoto, T.5    Kamiya, S.6
  • 30
    • 0032541661 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signaling
    • Yang RB, Mark MR, Gray A, et al. 1998. Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signaling. Nature 395: 284-288.
    • (1998) Nature , vol.395 , pp. 284-288
    • Yang, R.B.1    Mark, M.R.2    Gray, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.