메뉴 건너뛰기




Volumn 170, Issue 5, 2003, Pages 2340-2348

Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; ENDOTOXIN; GAMMA INTERFERON; HEAT SHOCK PROTEIN 60; I KAPPA B; INTERLEUKIN 10; INTERLEUKIN 12; INTERLEUKIN 1BETA; INTERLEUKIN 4; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; POLYMYXIN B; STRESS ACTIVATED PROTEIN KINASE; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA;

EID: 0345074067     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.170.5.2340     Document Type: Article
Times cited : (203)

References (48)
  • 1
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker, J., and E. A. Craig. 1994. Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219:11.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11
    • Becker, J.1    Craig, E.A.2
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571.
    • (1996) Nature , vol.381 , pp. 571
    • Hartl, F.U.1
  • 3
    • 0032101221 scopus 로고    scopus 로고
    • Heat shock proteins come of age: Primitive functions acquire new roles in an adaptive world
    • Srivastava, P. K., A. Menoret, S. Basu, R. J. Binder, and K. L. McQuade. 1998. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 8:657.
    • (1998) Immunity , vol.8 , pp. 657
    • Srivastava, P.K.1    Menoret, A.2    Basu, S.3    Binder, R.J.4    McQuade, K.L.5
  • 4
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated uptake of antigen/ heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways
    • Castellino, F., P. E. Boucher, K. Eichelberg, M. Mayhew, J. E. Rothman, A. N. Houghton, and R. N. Germain. 2000. Receptor-mediated uptake of antigen/ heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J. Exp. Med. 191:1957.
    • (2000) J. Exp. Med. , vol.191 , pp. 1957
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3    Mayhew, M.4    Rothman, J.E.5    Houghton, A.N.6    Germain, R.N.7
  • 5
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder, R. J., D. K. Han, and P. K. Srivastava. 2000. CD91: a receptor for heat shock protein gp96. Nat. Immunol. 1:151.
    • (2000) Nat. Immunol. , vol.1 , pp. 151
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 6
    • 0031035110 scopus 로고    scopus 로고
    • Delayed-type hypersensitivity elicited by synthetic peptides complexed with Mycobacterium tuberculosis hsp 70
    • Roman, E., and C. Moreno. 1997. Delayed-type hypersensitivity elicited by synthetic peptides complexed with Mycobacterium tuberculosis hsp 70. Immunology 90:52.
    • (1997) Immunology , vol.90 , pp. 52
    • Roman, E.1    Moreno, C.2
  • 7
    • 0030028801 scopus 로고    scopus 로고
    • Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24
    • Suzue, K., and R. A. Young. 1996. Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24. J. Immunol. 156:873.
    • (1996) J. Immunol. , vol.156 , pp. 873
    • Suzue, K.1    Young, R.A.2
  • 8
    • 0030016520 scopus 로고    scopus 로고
    • Synthetic peptides non-covalently bound to bacterial hsp 70 elicit peptide-specific T-cell responses in vivo
    • Roman, E., and C. Moreno. 1996. Synthetic peptides non-covalently bound to bacterial hsp 70 elicit peptide-specific T-cell responses in vivo. Immunology 88:487.
    • (1996) Immunology , vol.88 , pp. 487
    • Roman, E.1    Moreno, C.2
  • 9
    • 0025258481 scopus 로고
    • The mitochondriaI chaperonin hsp60 is required for its own assembly
    • Cheng, M. Y., F. U. Hartl, and A. L. Horwich. 1990. The mitochondriaI chaperonin hsp60 is required for its own assembly. Nature 348:455.
    • (1990) Nature , vol.348 , pp. 455
    • Cheng, M.Y.1    Hartl, F.U.2    Horwich, A.L.3
  • 10
    • 0025854087 scopus 로고
    • Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60
    • Wand-Württenberger, A., B. Schoel, J. Ivanyi, and S. H. Kaufmann. 1991. Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60. Eur. J. Immunol. 21:1089.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1089
    • Wand-Württenberger, A.1    Schoel, B.2    Ivanyi, J.3    Kaufmann, S.H.4
  • 11
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • Soltys, B. J., and R. S. Gupta. 1997. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol. Int. 21:315.
    • (1997) Cell Biol. Int. , vol.21 , pp. 315
    • Soltys, B.J.1    Gupta, R.S.2
  • 12
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys, B. J., and R. S. Gupta. 1996. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222:16.
    • (1996) Exp. Cell Res. , vol.222 , pp. 16
    • Soltys, B.J.1    Gupta, R.S.2
  • 13
    • 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
  • 14
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol, A., T. Bourcier, A. H. Lichtman, and P. Libby. 1999. Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. J. Clin. Invest. 103:571.
    • (1999) J. Clin. Invest. , vol.103 , pp. 571
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 15
    • 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., A. H. Lichtman, R. W. Finberg, P. Libby, and E. A. Kurt-Jones. 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.
    • (2000) J. Immunol. , vol.164 , pp. 13
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 16
    • 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. Imnumol. 164:558.
    • (2000) J. Immunol. , vol.164 , pp. 558
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 17
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas, R. M., P. Ahmad-Nejad, C. da Costa, T. Miethke, C. K. Kirschning, H. Häcker, and H. Wagner. Endocytosed HSP60s use Toll-like receptor 2 (TLR2) and TLR4 to activate the Toll/interleukin-1 receptor signaling pathway in innate immune cells. J. Biol. Chem. 276:31332.
    • J. Biol. Chem. , vol.276 , pp. 31332
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da Costa, C.3    Miethke, T.4    Kirschning, C.K.5    Häcker, H.6    Wagner, H.7
  • 18
    • 0037080218 scopus 로고    scopus 로고
    • The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins
    • Habich, C., K. Baumgart, H. Kolb, and V. Burkart. 2002. The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins. J. Immunol. 168:569.
    • (2002) J. Immunol. , vol.168 , pp. 569
    • Habich, C.1    Baumgart, K.2    Kolb, H.3    Burkart, V.4
  • 19
    • 0025249304 scopus 로고
    • Heat shock proteins and the immune response
    • Kaufmann, S. H. 1990. Heat shock proteins and the immune response. Immunol. Today 11:129.
    • (1990) Immunol. Today , vol.11 , pp. 129
    • Kaufmann, S.H.1
  • 20
    • 0025993122 scopus 로고
    • The 65-kDa heat-shock protein in the pathogenesis, prevention and therapy of autoimmune arthritis and diabetes mellitus in rats and mice
    • Feige, U., and I. R. Cohen. 1991. The 65-kDa heat-shock protein in the pathogenesis, prevention and therapy of autoimmune arthritis and diabetes mellitus in rats and mice. Springer Semin. Immunopathol. 13:99.
    • (1991) Springer Semin. Immunopathol. , vol.13 , pp. 99
    • Feige, U.1    Cohen, I.R.2
  • 24
    • 0033486007 scopus 로고    scopus 로고
    • T-cell priming by type-1 and type-2 polarized dendritic cells: The concept of a third signal
    • Kalinski, P., C. M. Hilkens, E. A. Wierenga, and M. L. Kapsenberg. 1999. T-cell priming by type-1 and type-2 polarized dendritic cells: the concept of a third signal. Immunol. Today 20:561.
    • (1999) Immunol. Today , vol.20 , pp. 561
    • Kalinski, P.1    Hilkens, C.M.2    Wierenga, E.A.3    Kapsenberg, M.L.4
  • 25
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J., and R. M. Steinman. 1998. Dendritic cells and the control of immunity. Nature 392-245.
    • (1998) Nature , vol.392 , pp. 245
    • Banchereau, J.1    Steinman, R.M.2
  • 26
    • 0029812593 scopus 로고    scopus 로고
    • Ligation of CD40 on dendritic cells triggers production of high levels of interleukin-12 and enhances T cell stimulatory capacity: T-T help via APC activation
    • Cella, M., D. Scheidegger, K. Palmer-Lehmann, P. Lane, A. Lanzavecchia, and G. Alber. 1996. Ligation of CD40 on dendritic cells triggers production of high levels of interleukin-12 and enhances T cell stimulatory capacity: T-T help via APC activation. J. Exp. Med. 184:747.
    • (1996) J. Exp. Med. , vol.184 , pp. 747
    • Cella, M.1    Scheidegger, D.2    Palmer-Lehmann, K.3    Lane, P.4    Lanzavecchia, A.5    Alber, G.6
  • 27
    • 0026345419 scopus 로고
    • Class II major histocompatibility complex molecules of murine dendritic cells: Synthesis, sialylation of invariant chain, and antigen processing capacity are down-regulated upon culture
    • Kämpgen, E., N. Koch, F. Koch, P. Stoger, C. Heufler, G. Schuler, and N. Romani. 1991. Class II major histocompatibility complex molecules of murine dendritic cells: synthesis, sialylation of invariant chain, and antigen processing capacity are down-regulated upon culture. Proc. Natl. Acad. Sci. USA 88:3014.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3014
    • Kämpgen, E.1    Koch, N.2    Koch, F.3    Stoger, P.4    Heufler, C.5    Schuler, G.6    Romani, N.7
  • 28
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto, F., M. Cella, C. Danieli, and A. Lanzavecchia. 1995. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. J. Exp. Med. 182:389.
    • (1995) J. Exp. Med. , vol.182 , pp. 389
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 29
    • 0028970060 scopus 로고
    • Interleukin-12: A proinflammatory cytokine with immunoregulatory functions that bridge innate resistance and antigen-specific adaptive immunity
    • Trinchieri, G. 1995. Interleukin-12: a proinflammatory cytokine with immunoregulatory functions that bridge innate resistance and antigen-specific adaptive immunity. Annu. Rev. Immunol. 13:251.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 251
    • Trinchieri, G.1
  • 31
    • 0031705349 scopus 로고    scopus 로고
    • Production of functional IL-18 by different subtypes of murine and human dendritic cells (DC): DC-derived IL-18 enhances IL-12-dependent Th1 development
    • Stoll, S., H. Jonuleit, E. Schmitt, G. Müller, H. Yamauchi, M. Kurimoto, J. Knop, and A. H. Enk. 1998. Production of functional IL-18 by different subtypes of murine and human dendritic cells (DC): DC-derived IL-18 enhances IL-12-dependent Th1 development. Eur. J. Immunol. 28:3231.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3231
    • Stoll, S.1    Jonuleit, H.2    Schmitt, E.3    Müller, G.4    Yamauchi, H.5    Kurimoto, M.6    Knop, J.7    Enk, A.H.8
  • 32
    • 0033012030 scopus 로고    scopus 로고
    • An advanced culture method for generating large quantities of highly pure dendritic cells from mouse bone marrow
    • Lutz, M. B., N. Kukutsch, A. L. Ogilvie, S. Rossner, F. Koch, N. Romani, and G. Schuler. 1999. An advanced culture method for generating large quantities of highly pure dendritic cells from mouse bone marrow. J. Immunol. Methods 223:77.
    • (1999) J. Immunol. Methods , vol.223 , pp. 77
    • Lutz, M.B.1    Kukutsch, N.2    Ogilvie, A.L.3    Rossner, S.4    Koch, F.5    Romani, N.6    Schuler, G.7
  • 35
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea, A., S. K. Kraeft, E. A. Kurt-Jones, M. A. Stevenson, L. B. Chen, R. W. Finberg, G. C. Koo, and S. K. Calderwood. 2000. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6:435.
    • (2000) Nat. Med. , vol.6 , pp. 435
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 36
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway
    • Basu, S., R. J. Binder, R. Suto, K. M. Anderson, and P. K. Srivastava. 2000. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway. Int. Immunol. 12:1539.
    • (2000) Int. Immunol. , vol.12 , pp. 1539
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 38
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu. S., R. J. Binder, T. Ramalingam, and P. K. Srivastava. 2001. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 14:303.
    • (2001) Immunity , vol.14 , pp. 303
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 39
    • 0032910168 scopus 로고    scopus 로고
    • Organization and regulation of mitogen-activated protein kinase signaling pathways
    • Garrington, T. P., and G. L. Johnson. 1999. Organization and regulation of mitogen-activated protein kinase signaling pathways. Curr. Opin. Cell Biol. 11:211.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 211
    • Garrington, T.P.1    Johnson, G.L.2
  • 41
    • 0029855237 scopus 로고    scopus 로고
    • Control of the ERK MAP kinase cascade by Ras and Raf
    • Marais, R., and C. J. Marshall. 1996. Control of the ERK MAP kinase cascade by Ras and Raf. Cancer Surv. 27:101.
    • (1996) Cancer Surv. , vol.27 , pp. 101
    • Marais, R.1    Marshall, C.J.2
  • 43
    • 0035869634 scopus 로고    scopus 로고
    • A critical role for p38 mitogen-activated protein kinase in the maturation of human blood-derived dendritic cells induced by lipopolysaccharide, TNF-α, and contact sensitizers
    • Arrighi, J. F., M. Rebsamen, F. Rousset, V. Kindler, and C. Hauser. 2001. A critical role for p38 mitogen-activated protein kinase in the maturation of human blood-derived dendritic cells induced by lipopolysaccharide, TNF-α, and contact sensitizers. J. Immunol. 166:3837.
    • (2001) J. Immunol. , vol.166 , pp. 3837
    • Arrighi, J.F.1    Rebsamen, M.2    Rousset, F.3    Kindler, V.4    Hauser, C.5
  • 44
    • 0032488837 scopus 로고    scopus 로고
    • p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe. W., S. Plaisance, E. Boone, K. De Bosscher, M. L. Schmitz, W. Fiers, and G. Haegeman. 1998. p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor. J. Biol. Chem. 273:3285.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3285
    • Vanden Berghe, W.1    Plaisance, S.2    Boone, E.3    De Bosscher, K.4    Schmitz, M.L.5    Fiers, W.6    Haegeman, G.7
  • 45
    • 0032698069 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression: The role of TATA-binding protein (TBP)
    • Carter, A. B., K. L. Knudtson, M. M. Monick, and G. W. Hunninghake. 1999. The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression: the role of TATA-binding protein (TBP). J. Biol. Chem. 274:30858.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30858
    • Carter, A.B.1    Knudtson, K.L.2    Monick, M.M.3    Hunninghake, G.W.4
  • 48
    • 0025058568 scopus 로고
    • Induction and therapy of autoimmune diabetes in the non-obese diabetic (NOD/ Lt) mouse by a 65-kDa heat shock protein
    • Elias, D., D. Markovits, T. Reshef, R. van der Zee, and I. R. Cohen. 1990. Induction and therapy of autoimmune diabetes in the non-obese diabetic (NOD/ Lt) mouse by a 65-kDa heat shock protein. Proc. Natl. Acad. Sci. USA 87:1576.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1576
    • Elias, D.1    Markovits, D.2    Reshef, T.3    Van Der Zee, R.4    Cohen, I.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.