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Volumn 267, Issue 1, 2011, Pages 56-66

Cytokines regulate cysteine cathepsins during TLR responses

Author keywords

Cathepsins; Endosomal proteases; Inflammatory response; Macrophage activation; Pattern recognition receptors; Signal transduction; Toll like receptors

Indexed keywords

BETA INTERFERON; CATHEPSIN; CATHEPSIN B; CATHEPSIN L; CATHEPSIN S; CYTOKINE; INTERLEUKIN 1BETA; MESSENGER RNA; MYELOID DIFFERENTIATION FACTOR 88; NEUTRALIZING ANTIBODY; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TUMOR NECROSIS FACTOR ALPHA;

EID: 78651095760     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2010.11.004     Document Type: Article
Times cited : (49)

References (48)
  • 1
    • 33847183077 scopus 로고    scopus 로고
    • Cooperation of toll-like receptor signals in innate immune defense
    • Trinchieri G., Sher A. Cooperation of toll-like receptor signals in innate immune defense. Nat. Rev. Immunol. 2007, 7:179-190.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 179-190
    • Trinchieri, G.1    Sher, A.2
  • 2
    • 0034780463 scopus 로고    scopus 로고
    • Differential roles of toll-like receptors in the elicitation of proinflammatory responses by macrophages
    • Jones B.W., Heldwein K.A., Means T.K., Saukkonen J.J., J Fenton M. Differential roles of toll-like receptors in the elicitation of proinflammatory responses by macrophages. Ann. Rheum. Dis. 2001, 60(Suppl. 3):iii6-iii12.
    • (2001) Ann. Rheum. Dis. , vol.60 , Issue.SUPPL. 3
    • Jones, B.W.1    Heldwein, K.A.2    Means, T.K.3    Saukkonen, J.J.4    J Fenton, M.5
  • 7
    • 32944474237 scopus 로고    scopus 로고
    • Innate immunity gone awry: linking microbial infections to chronic inflammation and cancer
    • Karin M., Lawrence T., Nizet V. Innate immunity gone awry: linking microbial infections to chronic inflammation and cancer. Cell 2006, 124:823-835.
    • (2006) Cell , vol.124 , pp. 823-835
    • Karin, M.1    Lawrence, T.2    Nizet, V.3
  • 8
    • 43349095584 scopus 로고    scopus 로고
    • The role of epithelial Toll-like receptor signaling in the pathogenesis of intestinal inflammation
    • Gribar S.C., Anand R.J., Sodhi C.P., Hackam D.J. The role of epithelial Toll-like receptor signaling in the pathogenesis of intestinal inflammation. J. Leukoc. Biol. 2008, 83:493-498.
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 493-498
    • Gribar, S.C.1    Anand, R.J.2    Sodhi, C.P.3    Hackam, D.J.4
  • 9
    • 37749053740 scopus 로고    scopus 로고
    • Toll-like receptors in atherosclerosis
    • Tobias P.S., Curtiss L.K. Toll-like receptors in atherosclerosis. Biochem. Soc. Trans. 2007, 35:1453-1455.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1453-1455
    • Tobias, P.S.1    Curtiss, L.K.2
  • 10
    • 34547450707 scopus 로고    scopus 로고
    • Increased macrophage activation mediated through toll-like receptors in rheumatoid arthritis
    • Huang Q., Ma Y., Adebayo A., Pope R.M. Increased macrophage activation mediated through toll-like receptors in rheumatoid arthritis. Arthritis Rheum. 2007, 5:2192-2201.
    • (2007) Arthritis Rheum. , vol.5 , pp. 2192-2201
    • Huang, Q.1    Ma, Y.2    Adebayo, A.3    Pope, R.M.4
  • 11
    • 37849035627 scopus 로고    scopus 로고
    • TLR signaling by tumor and immune cells: a double-edged sword
    • Huang B., Zhao J., Unkeless J.C., Feng Z.H., Xiong H. TLR signaling by tumor and immune cells: a double-edged sword. Oncogene 2008, 27:218-224.
    • (2008) Oncogene , vol.27 , pp. 218-224
    • Huang, B.1    Zhao, J.2    Unkeless, J.C.3    Feng, Z.H.4    Xiong, H.5
  • 12
    • 1542604677 scopus 로고    scopus 로고
    • Cysteine proteases as disease markers
    • Berdowska I. Cysteine proteases as disease markers. Clin. Chim. Acta 2004, 342:41-69.
    • (2004) Clin. Chim. Acta , vol.342 , pp. 41-69
    • Berdowska, I.1
  • 13
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K., Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 2003, 3:472-482.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 16
    • 0030639088 scopus 로고    scopus 로고
    • T cell-derived IL-10 antagonizes macrophage function in mycobacterial infection
    • Murray P., Wang L., Onufryk C., Tepper R., Young R. T cell-derived IL-10 antagonizes macrophage function in mycobacterial infection. J. Immunol. 1997, 158:315-321.
    • (1997) J. Immunol. , vol.158 , pp. 315-321
    • Murray, P.1    Wang, L.2    Onufryk, C.3    Tepper, R.4    Young, R.5
  • 17
    • 33846918203 scopus 로고    scopus 로고
    • New assay using fluorogenic substrates and immunofluorescence staining to measure cysteine cathepsin activity in live cell subpopulations
    • Creasy B.M., Hartmann C.B., Higgins White F.K., McCoy K.L. New assay using fluorogenic substrates and immunofluorescence staining to measure cysteine cathepsin activity in live cell subpopulations. Cytometry Part A 2007, 71:114-123.
    • (2007) Cytometry Part A , vol.71 , pp. 114-123
    • Creasy, B.M.1    Hartmann, C.B.2    Higgins White, F.K.3    McCoy, K.L.4
  • 18
    • 33751327802 scopus 로고    scopus 로고
    • Quantitative analysis of protein co-localization on B cells opsonized with rituximab and complement using the ImageStream multispectral imaging flow cytometer
    • Beum P.V., Lindorfer M.A., Hall B.E., George T.C., Frost K., Morrissey P.J., Taylor R.P. Quantitative analysis of protein co-localization on B cells opsonized with rituximab and complement using the ImageStream multispectral imaging flow cytometer. J. Immunol. Methods 2006, 317:90-99.
    • (2006) J. Immunol. Methods , vol.317 , pp. 90-99
    • Beum, P.V.1    Lindorfer, M.A.2    Hall, B.E.3    George, T.C.4    Frost, K.5    Morrissey, P.J.6    Taylor, R.P.7
  • 20
    • 0033968625 scopus 로고    scopus 로고
    • Cellular responses to bacterial cell wall components are mediated through MyD88-dependent signaling cascades
    • Takeuchi O., Takeda K., Hoshino K., Adachi O., Ogawa T., Akira S. Cellular responses to bacterial cell wall components are mediated through MyD88-dependent signaling cascades. Int. Immunol. 2000, 12:113-117.
    • (2000) Int. Immunol. , vol.12 , pp. 113-117
    • Takeuchi, O.1    Takeda, K.2    Hoshino, K.3    Adachi, O.4    Ogawa, T.5    Akira, S.6
  • 23
    • 0034612067 scopus 로고    scopus 로고
    • Lipopolysaccharide induces expression of genes encoding pro-inflammatory cytokines and the elastin-degrading enzyme, cathepsin S, in human cervical smooth-muscle cells
    • Watari M., Watari H., Nachamkin I., Strauss J.F. Lipopolysaccharide induces expression of genes encoding pro-inflammatory cytokines and the elastin-degrading enzyme, cathepsin S, in human cervical smooth-muscle cells. J. Soc. Gynecol. Investig. 2000, 7:190-198.
    • (2000) J. Soc. Gynecol. Investig. , vol.7 , pp. 190-198
    • Watari, M.1    Watari, H.2    Nachamkin, I.3    Strauss, J.F.4
  • 24
    • 69449098465 scopus 로고    scopus 로고
    • Endosomal toll-like receptors in autoimmunity: mechanisms for clinical diversity
    • Trivedi S., Greidinger E.L. Endosomal toll-like receptors in autoimmunity: mechanisms for clinical diversity. Therapy 2009, 6:433-442.
    • (2009) Therapy , vol.6 , pp. 433-442
    • Trivedi, S.1    Greidinger, E.L.2
  • 26
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for toll-like receptor 9 activation
    • Park B., Brinkmann M.M., Spooner E., Lee C.C., Kim Y.-M., Ploegh H.L. Proteolytic cleavage in an endolysosomal compartment is required for toll-like receptor 9 activation. Nat. Immunol. 2008, 9:1407-1414.
    • (2008) Nat. Immunol. , vol.9 , pp. 1407-1414
    • Park, B.1    Brinkmann, M.M.2    Spooner, E.3    Lee, C.C.4    Kim, Y.-M.5    Ploegh, H.L.6
  • 27
    • 0036607441 scopus 로고    scopus 로고
    • Toll-like receptor signal transduction and the tailoring of innate immunity: a role for Mal?
    • O'Neill L.A. Toll-like receptor signal transduction and the tailoring of innate immunity: a role for Mal?. Trends Immunol. 2002, 23:296-300.
    • (2002) Trends Immunol. , vol.23 , pp. 296-300
    • O'Neill, L.A.1
  • 28
    • 30044442866 scopus 로고    scopus 로고
    • How toll-like receptors signal: what we know and what we don't know
    • O'Neill L.A. How toll-like receptors signal: what we know and what we don't know. Curr. Opin. Immunol. 2006, 18:3-9.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 3-9
    • O'Neill, L.A.1
  • 29
    • 0030837038 scopus 로고    scopus 로고
    • Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells
    • Lemaire R., Huet G., Zerimech F., Grard G., Fontaine C., Duquesnoy B., Flipo R.M. Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br. J. Rheumatol. 1997, 36:735-743.
    • (1997) Br. J. Rheumatol. , vol.36 , pp. 735-743
    • Lemaire, R.1    Huet, G.2    Zerimech, F.3    Grard, G.4    Fontaine, C.5    Duquesnoy, B.6    Flipo, R.M.7
  • 30
    • 0028904111 scopus 로고
    • Gamma-interferon causes a selective induction of the lysosomal proteases, cathepsins B and L, in macrophages
    • Lah T.T., Hawley M., Rock R.L., Goldberg A.L. Gamma-interferon causes a selective induction of the lysosomal proteases, cathepsins B and L, in macrophages. FEBS Lett. 1995, 363:85-89.
    • (1995) FEBS Lett. , vol.363 , pp. 85-89
    • Lah, T.T.1    Hawley, M.2    Rock, R.L.3    Goldberg, A.L.4
  • 31
    • 27744449724 scopus 로고    scopus 로고
    • IL-6-STAT3 controls intracellular MHC class II alphabeta dimer level through cathepsin S activity in dendritic cells
    • Kitamura H., Kamon H., Sawa S., Park S.J., Katunuma N., Ishihara K., Murakami M., Hirano T. IL-6-STAT3 controls intracellular MHC class II alphabeta dimer level through cathepsin S activity in dendritic cells. Immunity 2005, 23:491-502.
    • (2005) Immunity , vol.23 , pp. 491-502
    • Kitamura, H.1    Kamon, H.2    Sawa, S.3    Park, S.J.4    Katunuma, N.5    Ishihara, K.6    Murakami, M.7    Hirano, T.8
  • 33
    • 0035896750 scopus 로고    scopus 로고
    • Cytokines regulate proteolysis in major histocompatibility complex class II-dependent antigen presentation by dendritic cells
    • Fiebiger E., Meraner P., Weber E., Fang I.F., Stingl G., Ploegh H., Maurer D. Cytokines regulate proteolysis in major histocompatibility complex class II-dependent antigen presentation by dendritic cells. J. Exp. Med. 2001, 193:881-892.
    • (2001) J. Exp. Med. , vol.193 , pp. 881-892
    • Fiebiger, E.1    Meraner, P.2    Weber, E.3    Fang, I.F.4    Stingl, G.5    Ploegh, H.6    Maurer, D.7
  • 34
    • 17744369711 scopus 로고    scopus 로고
    • Differential induction of the toll-like receptor 4-MyD88-dependent and -independent signaling pathways by endotoxins
    • Zughaier S., Zimmer S., Datta A., Carlson R., Stephens D. Differential induction of the toll-like receptor 4-MyD88-dependent and -independent signaling pathways by endotoxins. Infect. Immun. 2005, 73:2940-2950.
    • (2005) Infect. Immun. , vol.73 , pp. 2940-2950
    • Zughaier, S.1    Zimmer, S.2    Datta, A.3    Carlson, R.4    Stephens, D.5
  • 35
    • 0035933763 scopus 로고    scopus 로고
    • Cathepsin S regulates the expression of cathepsin L and the turnover of gamma-interferon-inducible lysosomal thiol reductase in B lymphocytes
    • Honey K., Duff M., Beers C., Brissette W.H., Elliott E.A., Peters C., Maric M., Cresswell P., Rudensky A. Cathepsin S regulates the expression of cathepsin L and the turnover of gamma-interferon-inducible lysosomal thiol reductase in B lymphocytes. J. Biol. Chem. 2001, 276:22573-22578.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22573-22578
    • Honey, K.1    Duff, M.2    Beers, C.3    Brissette, W.H.4    Elliott, E.A.5    Peters, C.6    Maric, M.7    Cresswell, P.8    Rudensky, A.9
  • 36
    • 0031829713 scopus 로고    scopus 로고
    • Differential expression of cathepsins B and L compared with matrix metalloproteinases and their respective inhibitors in rheumatoid arthritis and osteoarthritis: a parallel investigation by semiquantitative reverse transcriptase-polymerase chain reaction and immunohistochemistry
    • Keyszer G., Redlich A., Haupl T., Zacher J., Sparmann M., Engethum U., Gay S., Burmester G.R. Differential expression of cathepsins B and L compared with matrix metalloproteinases and their respective inhibitors in rheumatoid arthritis and osteoarthritis: a parallel investigation by semiquantitative reverse transcriptase-polymerase chain reaction and immunohistochemistry. Arthritis Rheum. 1998, 41:1378-1387.
    • (1998) Arthritis Rheum. , vol.41 , pp. 1378-1387
    • Keyszer, G.1    Redlich, A.2    Haupl, T.3    Zacher, J.4    Sparmann, M.5    Engethum, U.6    Gay, S.7    Burmester, G.R.8
  • 38
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala N. The role of cystatins in cells of the immune system. FEBS Lett. 2006, 580:6295-6301.
    • (2006) FEBS Lett. , vol.580 , pp. 6295-6301
    • Kopitar-Jerala, N.1
  • 39
    • 26044473585 scopus 로고    scopus 로고
    • In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S
    • Boes M., van der Wel N., Peperzak V., Kim Y.M., Peters P.J., Ploegh H. In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S. Eur. J. Immunol. 2005, 35:2552-2562.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2552-2562
    • Boes, M.1    van der Wel, N.2    Peperzak, V.3    Kim, Y.M.4    Peters, P.J.5    Ploegh, H.6
  • 40
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre P., Mellman I. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 1998, 93:1135-1145.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 41
    • 22144469068 scopus 로고    scopus 로고
    • Differentiation- and maturation-dependent content, localization, and secretion of cystatin C in human dendritic cells
    • Zavasnik-Bergant T., Repnik U., Schweiger A., Romih R., Jeras M., Turk V., Kos J. Differentiation- and maturation-dependent content, localization, and secretion of cystatin C in human dendritic cells. J. Leukoc. Biol. 2005, 78:122-134.
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 122-134
    • Zavasnik-Bergant, T.1    Repnik, U.2    Schweiger, A.3    Romih, R.4    Jeras, M.5    Turk, V.6    Kos, J.7
  • 42
    • 0242495719 scopus 로고    scopus 로고
    • The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation
    • El Sukkari D., Wilson N.S., Hakansson K., Steptoe R.J., Grubb A., Shortman K., Villadangos J.A. The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation. J. Immunol. 2003, 171:5003-5011.
    • (2003) J. Immunol. , vol.171 , pp. 5003-5011
    • El Sukkari, D.1    Wilson, N.S.2    Hakansson, K.3    Steptoe, R.J.4    Grubb, A.5    Shortman, K.6    Villadangos, J.A.7
  • 43
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta E.S., Ebersold M., Garrett W., Pypaert M., Mellman I. Activation of lysosomal function during dendritic cell maturation. Science 2003, 299:1400-1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 44
    • 34249779825 scopus 로고    scopus 로고
    • Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells
    • Vyas J.M., Kim Y.-M., Artavanis-Tsakona K., Love C.J., Van der Veen A.G., Ploegh H. Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. J. Immunol. 2007, 178:7199-7210.
    • (2007) J. Immunol. , vol.178 , pp. 7199-7210
    • Vyas, J.M.1    Kim, Y.-M.2    Artavanis-Tsakona, K.3    Love, C.J.4    Van der Veen, A.G.5    Ploegh, H.6
  • 47
    • 37549011741 scopus 로고    scopus 로고
    • IFN-β modulates the response to TLR stimulation in human DC: involvement of IFN regulatory factor-1(IRF-1) in IL-27 gene expression
    • Remoli M.E., Gafa V., Giacomini E., Severa M., Lande R., Coccia E.M. IFN-β modulates the response to TLR stimulation in human DC: involvement of IFN regulatory factor-1(IRF-1) in IL-27 gene expression. Eur. J. Immunol. 2007, 37:3499-3508.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 3499-3508
    • Remoli, M.E.1    Gafa, V.2    Giacomini, E.3    Severa, M.4    Lande, R.5    Coccia, E.M.6


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