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Volumn 1823, Issue 11, 2012, Pages 2087-2093

Proteasome protease mediated regulation of cytokine induction and inflammation

Author keywords

Cytokines; LMP knockout mice; Proteasome; Proteasome inhibitors; Quercetin; Resveratrol

Indexed keywords

ADENOSINE A2A RECEPTOR; ADRENOMEDULLIN; CHYMOTRYPSIN; CILASTATIN PLUS IMIPENEM; COMPLEMENT COMPONENT C3; CXCL9 CHEMOKINE; CYCLIN D2; ENDOTHELIN 1; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 12; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 23P19; INTERLEUKIN 6; LACTACYSTIN; LIPOPOLYSACCHARIDE; MEVINOLIN; PROSTAGLANDIN SYNTHASE; PROTEASOME INHIBITOR; PROTEIN BCL 3; PROTEINASE INHIBITOR; QUERCETIN; RESVERATROL; STAT5A PROTEIN; TRANSCRIPTION FACTOR MAFF; TRYPSIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 1; UBIQUITIN; VASCULAR CELL ADHESION MOLECULE 1;

EID: 84866986070     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.06.016     Document Type: Review
Times cited : (52)

References (34)
  • 2
    • 0042847104 scopus 로고    scopus 로고
    • The proteasome as a LPS-binding protein in macrophages. Toxic lipopolysaccharide activates the proteasome complex
    • Qureshi N., Perera P.-Y., Splitter G., Morrison D.C., Vogel S.N. The proteasome as a LPS-binding protein in macrophages. Toxic lipopolysaccharide activates the proteasome complex. J. Immunol. 2003, 171:1515-1525.
    • (2003) J. Immunol. , vol.171 , pp. 1515-1525
    • Qureshi, N.1    Perera, P.-Y.2    Splitter, G.3    Morrison, D.C.4    Vogel, S.N.5
  • 4
    • 33745629870 scopus 로고    scopus 로고
    • Proteasome inhibitor, lactacystin blocks CpG DNA- and peptidoglycan induced inflammatory genes, cytokines and mitogen-activated protein kinases in macrophages
    • Shen J., Gao J.J., Zhang G., Tan X., Morrison D.C., Papasian C.J., Vogel S.N., Qureshi N. Proteasome inhibitor, lactacystin blocks CpG DNA- and peptidoglycan induced inflammatory genes, cytokines and mitogen-activated protein kinases in macrophages. Shock 2006, 25:594-599.
    • (2006) Shock , vol.25 , pp. 594-599
    • Shen, J.1    Gao, J.J.2    Zhang, G.3    Tan, X.4    Morrison, D.C.5    Papasian, C.J.6    Vogel, S.N.7    Qureshi, N.8
  • 9
    • 79952165858 scopus 로고    scopus 로고
    • A TLR-responsive kinase, protein kinase R (Pkr), is inactivated in endotoxin tolerance through differential K63/K48 ubiquitination
    • Perkins D., Qureshi N., Vogel S.N. A TLR-responsive kinase, protein kinase R (Pkr), is inactivated in endotoxin tolerance through differential K63/K48 ubiquitination. Mbio 2010, 1:e00239-e002310.
    • (2010) Mbio , vol.1
    • Perkins, D.1    Qureshi, N.2    Vogel, S.N.3
  • 10
    • 77953341124 scopus 로고    scopus 로고
    • Differential effects of lactacystin on cytokine production in activated Jurkat cells and murine splenocytes
    • Rockwell C.E., Qureshi N. Differential effects of lactacystin on cytokine production in activated Jurkat cells and murine splenocytes. Cytokine 2010, 51:12-17.
    • (2010) Cytokine , vol.51 , pp. 12-17
    • Rockwell, C.E.1    Qureshi, N.2
  • 12
    • 0030037846 scopus 로고    scopus 로고
    • Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-γ-induced subunits LMP2 and LMP7
    • Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L. Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-γ-induced subunits LMP2 and LMP7. J. Biol. Chem. 1996, 271:17275-17280.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17275-17280
    • Gaczynska, M.1    Goldberg, A.L.2    Tanaka, K.3    Hendil, K.B.4    Rock, K.L.5
  • 15
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC class I-mediated antigen presentation
    • Kloetzel P.M., Ossendorp F. Proteasome and peptidase function in MHC class I-mediated antigen presentation. Curr. Opin. Immunol. 2004, 16:76-81.
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 18
    • 2142762520 scopus 로고    scopus 로고
    • TLRs: differential adapter utilization by toll-like receptors mediates TLR-specific patterns of gene expression
    • Vogel S.N., Fitzgerald K.A., Fenton M.J. TLRs: differential adapter utilization by toll-like receptors mediates TLR-specific patterns of gene expression. Mol. Interv. 2003, 3:466-477.
    • (2003) Mol. Interv. , vol.3 , pp. 466-477
    • Vogel, S.N.1    Fitzgerald, K.A.2    Fenton, M.J.3
  • 19
    • 67649422321 scopus 로고    scopus 로고
    • Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer
    • O'Neill L.A., Bryant J.C.E., Doyle S.I. Therapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer. Pharmacol. Rev. 2009, 61:177-197.
    • (2009) Pharmacol. Rev. , vol.61 , pp. 177-197
    • O'Neill, L.A.1    Bryant, J.C.E.2    Doyle, S.I.3
  • 21
    • 0027980321 scopus 로고
    • The ubiquitin proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 1994, 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 22
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103:351-361.
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 23
    • 34548225910 scopus 로고    scopus 로고
    • Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains
    • Abott D.W., Yang Y., Hutti J.E., Madhavarapu S., Kelliher M.A., Cantley L.C. Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains. Mol. Cell. Biol. 2007, 27:6012-6025.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6012-6025
    • Abott, D.W.1    Yang, Y.2    Hutti, J.E.3    Madhavarapu, S.4    Kelliher, M.A.5    Cantley, L.C.6
  • 24
    • 33746893480 scopus 로고    scopus 로고
    • Pellino proteins are more than scaffold proteins in TLR/IL-1R signalling: a role as novel RING E3-ubiquitin-ligases
    • Schauvilege R., Janssens S., Beyaert R. Pellino proteins are more than scaffold proteins in TLR/IL-1R signalling: a role as novel RING E3-ubiquitin-ligases. FEBS Lett. 2006, 580:4697-4702.
    • (2006) FEBS Lett. , vol.580 , pp. 4697-4702
    • Schauvilege, R.1    Janssens, S.2    Beyaert, R.3
  • 26
    • 49649125136 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Ro52 negatively regulates IFN-β production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3
    • Higgs R., Gabhann J.N., Larbi N.B., Breen E.P., Fitzgerald K.A., Jefferies C.A. The E3 ubiquitin ligase Ro52 negatively regulates IFN-β production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. J. Immunol. 2008, 181:1780-1786.
    • (2008) J. Immunol. , vol.181 , pp. 1780-1786
    • Higgs, R.1    Gabhann, J.N.2    Larbi, N.B.3    Breen, E.P.4    Fitzgerald, K.A.5    Jefferies, C.A.6
  • 27
    • 84857754073 scopus 로고    scopus 로고
    • A Critical Role for the Inducible Proteasomal Subunits LMP7 and MECL1 in Cytokine Production by Activated Murine Splenocytes
    • Rockwell C.E., Monaco J.J., Qureshi N. A Critical Role for the Inducible Proteasomal Subunits LMP7 and MECL1 in Cytokine Production by Activated Murine Splenocytes. Pharmacology 2012, 89:117-126.
    • (2012) Pharmacology , vol.89 , pp. 117-126
    • Rockwell, C.E.1    Monaco, J.J.2    Qureshi, N.3
  • 28
    • 0035399615 scopus 로고    scopus 로고
    • Diphosphoryl lipid A from Rhodobacter sphaeroides blocks the binding and internalization of lipopolysaccharide in RAW 264.7 cells
    • Kutuzova G.D., Albrecht R.M., Erickson C.M., Qureshi N. Diphosphoryl lipid A from Rhodobacter sphaeroides blocks the binding and internalization of lipopolysaccharide in RAW 264.7 cells. J. Immunol. 2001, 167:482-489.
    • (2001) J. Immunol. , vol.167 , pp. 482-489
    • Kutuzova, G.D.1    Albrecht, R.M.2    Erickson, C.M.3    Qureshi, N.4
  • 29
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-β
    • Kagan J.C., Su T., Hornig T., Chow A., Akira S., Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-β. Nat. Immunol. 2008, 9:361-368.
    • (2008) Nat. Immunol. , vol.9 , pp. 361-368
    • Kagan, J.C.1    Su, T.2    Hornig, T.3    Chow, A.4    Akira, S.5    Medzhitov, R.6
  • 30
    • 0033529171 scopus 로고    scopus 로고
    • 1 arrest is through inhibition of the proteasome, independent of hydroxymethyl glutaryl-CoA reductase
    • 1 arrest is through inhibition of the proteasome, independent of hydroxymethyl glutaryl-CoA reductase. PNAS 1999, 96:7797-7802.
    • (1999) PNAS , vol.96 , pp. 7797-7802
    • Rao, S.1    Porter, D.C.2    Chen, X.3    Herliczek, T.4    Lowe, M.5    Keyomarsi, K.6
  • 31
    • 83655181363 scopus 로고    scopus 로고
    • Inhibition of nitric oxide in LPS-stimulated macrophages of young and senescent mice by δ-tocotrienol and quercetin
    • Qureshi A.A., Tan X., Reis J.C., Badr M.Z., Papasian C.J., Morrison D.C., Qureshi N. Inhibition of nitric oxide in LPS-stimulated macrophages of young and senescent mice by δ-tocotrienol and quercetin. Lipids Health Dis. 2011, 10:239.
    • (2011) Lipids Health Dis. , vol.10 , pp. 239
    • Qureshi, A.A.1    Tan, X.2    Reis, J.C.3    Badr, M.Z.4    Papasian, C.J.5    Morrison, D.C.6    Qureshi, N.7
  • 32
    • 79952053160 scopus 로고    scopus 로고
    • δ-Tocotrienol and quercetin reduce serum levels of nitric oxide and lipid parameters in female chickens
    • Qureshi A.A., Reis J., Qureshi N., Papasian C.J., Morrison D.C., Schaefer D.M. δ-Tocotrienol and quercetin reduce serum levels of nitric oxide and lipid parameters in female chickens. Lipids Health Dis. March 2011, 10:39.
    • (2011) Lipids Health Dis. , vol.10 , pp. 39
    • Qureshi, A.A.1    Reis, J.2    Qureshi, N.3    Papasian, C.J.4    Morrison, D.C.5    Schaefer, D.M.6
  • 33
    • 80053898277 scopus 로고    scopus 로고
    • Suppression of nitric oxide production and pro-inflammatory cytokines by novel proteasome inhibitors in various experimental models
    • Qureshi A.A., Tan X., Reis J., Badr M.Z., Papasian C.J., Morrison D.C., Qureshi N. Suppression of nitric oxide production and pro-inflammatory cytokines by novel proteasome inhibitors in various experimental models. Lipids Health Dis. 2011, 10:177.
    • (2011) Lipids Health Dis. , vol.10 , pp. 177
    • Qureshi, A.A.1    Tan, X.2    Reis, J.3    Badr, M.Z.4    Papasian, C.J.5    Morrison, D.C.6    Qureshi, N.7
  • 34
    • 84862180074 scopus 로고    scopus 로고
    • Inhibition of nitric oxide and inflammatory cytokines in LPS-stimulated murine macrophages by Resveratrol, a potent proteasome inhibitor
    • Qureshi A.A., Guan X.-Q., Reis J.C., Papasian C.J., Jabre S., Morrison D.C., Qureshi N. Inhibition of nitric oxide and inflammatory cytokines in LPS-stimulated murine macrophages by Resveratrol, a potent proteasome inhibitor. Lipids Health Dis. 2012, 11:76.
    • (2012) Lipids Health Dis. , vol.11 , pp. 76
    • Qureshi, A.A.1    Guan, X.-Q.2    Reis, J.C.3    Papasian, C.J.4    Jabre, S.5    Morrison, D.C.6    Qureshi, N.7


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