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Volumn 143, Issue 1, 2006, Pages 85-92

Dose-dependent induction of IL-6 by plant-derived proteases in vitro

Author keywords

Cytokines; IL 6; Immunomodulation; MMLC; Proteases

Indexed keywords

BROMELAIN; CD14 ANTIGEN; GAMMA INTERFERON; INTERLEUKIN 10; INTERLEUKIN 6; PAPAIN; POLYMYXIN B; PROTEINASE; ANTIINFECTIVE AGENT; IMMUNOSUPPRESSIVE AGENT; LIPOPOLYSACCHARIDE; PEPTIDE HYDROLASE;

EID: 33644819544     PISSN: 00099104     EISSN: 13652249     Source Type: Journal    
DOI: 10.1111/j.1365-2249.2005.02970.x     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0034843751 scopus 로고    scopus 로고
    • Bromelain: Biochemistry, pharmacology and medical use
    • Maurer HR Bromelain: biochemistry, pharmacology and medical use Cell Mol Life Sci 2001 58 1234 45
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1234-45
    • Maurer, H.R.1
  • 2
    • 0036175469 scopus 로고    scopus 로고
    • Therapy with proteolytic enzymes in rheumatic disorders
    • Leipner J Iten F Saller R Therapy with proteolytic enzymes in rheumatic disorders Biodrugs 2001 15 779 89
    • (2001) Biodrugs , vol.15 , pp. 779-89
    • Leipner, J.1    Iten, F.2    Saller, R.3
  • 4
    • 0025065408 scopus 로고
    • Induction of tumor necrosis factor in human peripheral-blood mononuclear cells by proteolytic enzymes
    • Desser L Rehberger A Induction of tumor necrosis factor in human peripheral-blood mononuclear cells by proteolytic enzymes Oncology 1990 47 475 7
    • (1990) Oncology , vol.47 , pp. 475-7
    • Desser, L.1    Rehberger, A.2
  • 5
    • 0028171487 scopus 로고
    • Proteolytic enzymes and amylase induce cytokine production in human peripheral blood mononuclear cells in vitro
    • Desser L Rehberger A Paukovits W Proteolytic enzymes and amylase induce cytokine production in human peripheral blood mononuclear cells in vitro Cancer Biother 1994 9 253 63
    • (1994) Cancer Biother , vol.9 , pp. 253-63
    • Desser, L.1    Rehberger, A.2    Paukovits, W.3
  • 6
    • 0035946838 scopus 로고    scopus 로고
    • Bromelain activates murine macrophages and natural killer cells in vitro
    • Engwerda CR Andrew D Murphy M Mynott TL Bromelain activates murine macrophages and natural killer cells in vitro Cell Immunol 2001 210 5 10
    • (2001) Cell Immunol , vol.210 , pp. 5-10
    • Engwerda, C.R.1    Andrew, D.2    Murphy, M.3    Mynott, T.L.4
  • 7
    • 0027496317 scopus 로고
    • Cytokine synthesis in human peripheral blood mononuclear cells after oral administration of polyenzyme preparations
    • Desser L Rehberger A Kokron E Paukovits W Cytokine synthesis in human peripheral blood mononuclear cells after oral administration of polyenzyme preparations Oncology 1993 50 403 7
    • (1993) Oncology , vol.50 , pp. 403-7
    • Desser, L.1    Rehberger, A.2    Kokron, E.3    Paukovits, W.4
  • 9
    • 0033197918 scopus 로고    scopus 로고
    • Bromelain, from pineapple stems, proteolytically blocks activation of extracellular regulated kinase-2 in T cells
    • Mynott TL Ladhams A Scarmato P Engwerda CR Bromelain, from pineapple stems, proteolytically blocks activation of extracellular regulated kinase-2 in T cells J Immunol 1999 163 2568 75
    • (1999) J Immunol , vol.163 , pp. 2568-75
    • Mynott, T.L.1    Ladhams, A.2    Scarmato, P.3    Engwerda, C.R.4
  • 10
    • 0027077553 scopus 로고
    • Bromelain treatment of human T cells removes CD44, CD45RA, E2/MIC2, CD6, CD7, CD8, and Leu 8/LAM1 surface molecules and markedly enhances CD2-mediated T cell activation
    • Hale LP Haynes BF Bromelain treatment of human T cells removes CD44, CD45RA, E2/MIC2, CD6, CD7, CD8, and Leu 8/LAM1 surface molecules and markedly enhances CD2-mediated T cell activation J Immunol 1992 149 3809 16
    • (1992) J Immunol , vol.149 , pp. 3809-16
    • Hale, L.P.1    Haynes, B.F.2
  • 11
    • 0027937009 scopus 로고
    • Bromelain protease F9 reduces the CD44 mediated adhesion of human peripheral blood lymphocytes to human umbilical vein endothelial cells
    • Munzig E Eckert K Harrach T Graf H Maurer HR Bromelain protease F9 reduces the CD44 mediated adhesion of human peripheral blood lymphocytes to human umbilical vein endothelial cells FEBS Lett 1994 351 215 8
    • (1994) FEBS Lett , vol.351 , pp. 215-8
    • Munzig, E.1    Eckert, K.2    Harrach, T.3    Graf, H.4    Maurer, H.R.5
  • 12
    • 0032926775 scopus 로고    scopus 로고
    • Prevention of murine EAE by oral hydrolytic enzyme treatment
    • Targoni OS Tary-Lehmann M Lehmann PV Prevention of murine EAE by oral hydrolytic enzyme treatment J Autoimmun 1999 12 191 8
    • (1999) J Autoimmun , vol.12 , pp. 191-8
    • Targoni, O.S.1    Tary-Lehmann, M.2    Lehmann, P.V.3
  • 13
    • 0035680491 scopus 로고    scopus 로고
    • Protease administration decreases enhanced transforming growth factor-beta 1 content in isolated glomeruli of diabetic rats
    • Paczek L Gaciong Z Bartlomiejczyk I Sebekova K Birkenmeier G Heidland A Protease administration decreases enhanced transforming growth factor-beta 1 content in isolated glomeruli of diabetic rats Drugs Exp Clin Res 2001 27 141 9
    • (2001) Drugs Exp Clin Res , vol.27 , pp. 141-9
    • Paczek, L.1    Gaciong, Z.2    Bartlomiejczyk, I.3    Sebekova, K.4    Birkenmeier, G.5    Heidland, A.6
  • 14
    • 0035946842 scopus 로고    scopus 로고
    • Bromelain modulates T cell and B cell immune responses in vitro and in vivo
    • Engwerda CR Andrew D Ladhams A Mynott TL Bromelain modulates T cell and B cell immune responses in vitro and in vivo Cell Immunol 2001 210 66 75
    • (2001) Cell Immunol , vol.210 , pp. 66-75
    • Engwerda, C.R.1    Andrew, D.2    Ladhams, A.3    Mynott, T.L.4
  • 15
    • 0036389659 scopus 로고    scopus 로고
    • Administration of proteolytic enzymes bromelain and trypsin diminish the number of CD4+ cells and the interferon-gamma response in Peyer's patches and spleen in endotoxemic balb/c mice
    • Manhart N Akomeah R Bergmeister H Spittler A Ploner M Roth E Administration of proteolytic enzymes bromelain and trypsin diminish the number of CD4+ cells and the interferon-gamma response in Peyer's patches and spleen in endotoxemic balb/c mice Cell Immunol 2002 215 113 9
    • (2002) Cell Immunol , vol.215 , pp. 113-9
    • Manhart, N.1    Akomeah, R.2    Bergmeister, H.3    Spittler, A.4    Ploner, M.5    Roth, E.6
  • 17
    • 1642547107 scopus 로고    scopus 로고
    • Combined activation of innate and T cell immunity for recognizing immunomodulatory properties of therapeutic agents
    • Rose B Herder C Loffler H Kolb H Martin S Combined activation of innate and T cell immunity for recognizing immunomodulatory properties of therapeutic agents J Leukoc Biol 2004 75 624 30
    • (2004) J Leukoc Biol , vol.75 , pp. 624-30
    • Rose, B.1    Herder, C.2    Loffler, H.3    Kolb, H.4    Martin, S.5
  • 18
    • 0036889996 scopus 로고    scopus 로고
    • The two faces of IL-6 on Th1/Th2 differentiation
    • Diehl S Rincon M The two faces of IL-6 on Th1/Th2 differentiation Mol Immunol 2002 39 531 6
    • (2002) Mol Immunol , vol.39 , pp. 531-6
    • Diehl, S.1    Rincon, M.2
  • 19
    • 0023318212 scopus 로고
    • Isolation and functional activity of human blood monocytes after adherence to plastic surfaces: Comparison of different detachment methods
    • Nielsen H Isolation and functional activity of human blood monocytes after adherence to plastic surfaces: comparison of different detachment methods Acta Pathol Microbiol Immunol Scand [C] 1987 95 81 4
    • (1987) Acta Pathol Microbiol Immunol Scand [c] , vol.95 , pp. 81-4
    • Nielsen, H.1
  • 20
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery O Corvera CU Steinhoff M Bunnett NW Proteinase-activated receptors: novel mechanisms of signaling by serine proteases Am J Physiol 1998 274 C1429 C1452
    • (1998) Am J Physiol , vol.274
    • Dery, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 21
    • 0036592015 scopus 로고    scopus 로고
    • Protease-activated receptors: A means of converting extracellular proteolysis into intracellular signals
    • Mackie EJ Pagel CN Smith R de Niese MR Song SJ Pike RN Protease-activated receptors: a means of converting extracellular proteolysis into intracellular signals IUBMB Life 2002 53 277 81
    • (2002) IUBMB Life , vol.53 , pp. 277-81
    • MacKie, E.J.1    Pagel, C.N.2    Smith, R.3    De Niese, M.R.4    Song, S.J.5    Pike, R.N.6
  • 23
    • 0031753528 scopus 로고    scopus 로고
    • Borrelia burgdorferi-infected, interleukin-6-deficient mice have decreased Th2 responses and increased lyme arthritis
    • Anguita J Rincon M Samanta S Barthold SW Flavell RA Fikrig E Borrelia burgdorferi-infected, interleukin-6-deficient mice have decreased Th2 responses and increased lyme arthritis J Infect Dis 1998 178 1512 5
    • (1998) J Infect Dis , vol.178 , pp. 1512-5
    • Anguita, J.1    Rincon, M.2    Samanta, S.3    Barthold, S.W.4    Flavell, R.A.5    Fikrig, E.6
  • 24
    • 0031690174 scopus 로고    scopus 로고
    • A role for interleukin-6 in host defense against murine Chlamydia trachomatis infection
    • Williams DM Grubbs BG Darville T Kelly K Rank RG A role for interleukin-6 in host defense against murine Chlamydia trachomatis infection Infect Immun 1998 66 4564 7
    • (1998) Infect Immun , vol.66 , pp. 4564-7
    • Williams, D.M.1    Grubbs, B.G.2    Darville, T.3    Kelly, K.4    Rank, R.G.5
  • 26
    • 0030914438 scopus 로고    scopus 로고
    • Impaired resistance to the development of toxoplasmic encephalitis in interleukin-6-deficient mice
    • Suzuki Y Rani S Liesenfeld O et al. Impaired resistance to the development of toxoplasmic encephalitis in interleukin-6-deficient mice Infect Immun 1997 65 2339 45
    • (1997) Infect Immun , vol.65 , pp. 2339-45
    • Suzuki, Y.1    Rani, S.2    Liesenfeld, O.3
  • 27
    • 0036151250 scopus 로고    scopus 로고
    • Interleukin-6 is required for parasite specific response and host resistance to Trypanosoma cruzi
    • Gao W Pereira MA Interleukin-6 is required for parasite specific response and host resistance to Trypanosoma cruzi Int J Parasitol 2002 32 167 70
    • (2002) Int J Parasitol , vol.32 , pp. 167-70
    • Gao, W.1    Pereira, M.A.2
  • 28
    • 0037369751 scopus 로고    scopus 로고
    • Interleukin-6-deficient mice are highly susceptible to Giardia lamblia infection but exhibit normal intestinal immunoglobulin a responses against the parasite
    • Bienz M Dai WJ Welle M Gottstein B Muller N Interleukin-6-deficient mice are highly susceptible to Giardia lamblia infection but exhibit normal intestinal immunoglobulin A responses against the parasite Infect Immun 2003 71 1569 73
    • (2003) Infect Immun , vol.71 , pp. 1569-73
    • Bienz, M.1    Dai, W.J.2    Welle, M.3    Gottstein, B.4    Muller, N.5
  • 29
    • 0035450086 scopus 로고    scopus 로고
    • Impaired antifungal effector activity but not inflammatory cell recruitment in interleukin-6-deficient mice with invasive pulmonary aspergillosis
    • Cenci E Mencacci A Casagrande A Mosci P Bistoni F Romani L Impaired antifungal effector activity but not inflammatory cell recruitment in interleukin-6-deficient mice with invasive pulmonary aspergillosis J Infect Dis 2001 184 610 7
    • (2001) J Infect Dis , vol.184 , pp. 610-7
    • Cenci, E.1    Mencacci, A.2    Casagrande, A.3    Mosci, P.4    Bistoni, F.5    Romani, L.6
  • 32
    • 0038341934 scopus 로고    scopus 로고
    • Essential involvement of IL-6 in the skin wound-healing process as evidenced by delayed wound healing in IL-6-deficient mice
    • Lin ZQ Kondo T Ishida Y Takayasu T Mukaida N Essential involvement of IL-6 in the skin wound-healing process as evidenced by delayed wound healing in IL-6-deficient mice J Leukoc Biol 2003 73 713 21
    • (2003) J Leukoc Biol , vol.73 , pp. 713-21
    • Lin, Z.Q.1    Kondo, T.2    Ishida, Y.3    Takayasu, T.4    Mukaida, N.5
  • 35
    • 0031441582 scopus 로고    scopus 로고
    • Nociceptive responses in interleukin-6-deficient mice to peripheral inflammation and peripheral nerve section
    • Xu XJ Hao JX Andell-Jonsson S Poli V Bartfai T Wiesenfeld-Hallin Z Nociceptive responses in interleukin-6-deficient mice to peripheral inflammation and peripheral nerve section Cytokine 1997 9 1028 33
    • (1997) Cytokine , vol.9 , pp. 1028-33
    • Xu, X.J.1    Hao, J.X.2    Andell-Jonsson, S.3    Poli, V.4    Bartfai, T.5    Wiesenfeld-Hallin, Z.6
  • 36
    • 0032561162 scopus 로고    scopus 로고
    • Tumor growth and food intake in interleukin-6 gene knock-out mice
    • Molotkov A Satoh M Tohyama C Tumor growth and food intake in interleukin-6 gene knock-out mice Cancer Lett 1998 132 187 92
    • (1998) Cancer Lett , vol.132 , pp. 187-92
    • Molotkov, A.1    Satoh, M.2    Tohyama, C.3
  • 37
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E Rivera S Gabayan V Keller C Taudorf S Pedersen BK Ganz T IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin J Clin Invest 2004 113 1271 6
    • (2004) J Clin Invest , vol.113 , pp. 1271-6
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 39
    • 0030878648 scopus 로고    scopus 로고
    • Intestinal absorption of undegraded proteins in men: Presence of bromelain in plasma after oral intake
    • Castell JV Friedrich G Kuhn CS Poppe GE Intestinal absorption of undegraded proteins in men: presence of bromelain in plasma after oral intake Am J Physiol 1997 273 G139 G146
    • (1997) Am J Physiol , vol.273
    • Castell, J.V.1    Friedrich, G.2    Kuhn, C.S.3    Poppe, G.E.4
  • 41
    • 0031396359 scopus 로고    scopus 로고
    • Concentrations of soluble tumor necrosis factor receptors, beta2-microglobulin, IL-6 and TNF in serum of multiple myeloma patients after chemotherapy and after combined enzyme-therapy
    • Desser L Sakalova A Zavadova E Holomanova D Mohr T Concentrations of soluble tumor necrosis factor receptors, beta2-microglobulin, IL-6 and TNF in serum of multiple myeloma patients after chemotherapy and after combined enzyme-therapy Int J Immunotherapy 1997 13 121 30
    • (1997) Int J Immunotherapy , vol.13 , pp. 121-30
    • Desser, L.1    Sakalova, A.2    Zavadova, E.3    Holomanova, D.4    Mohr, T.5


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