메뉴 건너뛰기




Volumn 76, Issue 10, 2008, Pages 1214-1228

Actin cytoskeleton differentially modulates NF-κB-mediated IL-8 expression in myelomonocytic cells

Author keywords

Actin cytoskeleton; Cytochalasin D; Interleukin 8; LPS; NF B; TNF

Indexed keywords

ACTIN; CYTOCHALASIN D; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; SYNAPTOTAGMIN I; TUMOR NECROSIS FACTOR ALPHA;

EID: 54249085295     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.08.017     Document Type: Article
Times cited : (31)

References (80)
  • 1
    • 0035178210 scopus 로고    scopus 로고
    • Cell motility: can Rho GTPases and microtubules point the way?
    • Wittmann T., and Waterman-Storer C.M. Cell motility: can Rho GTPases and microtubules point the way?. J Cell Sci 114 Pt21 (2001) 3795-3803
    • (2001) J Cell Sci , vol.114 , Issue.PART 21 , pp. 3795-3803
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 3
    • 0034846886 scopus 로고    scopus 로고
    • Regulation of interleukin-8 gene expression after phagocytosis of zymosan by human monocytic cells
    • Friedland J.S., Constantin D., Shaw T.C., and Stylianou E. Regulation of interleukin-8 gene expression after phagocytosis of zymosan by human monocytic cells. J Leukoc Bio 70 3 (2001) 447-454
    • (2001) J Leukoc Bio , vol.70 , Issue.3 , pp. 447-454
    • Friedland, J.S.1    Constantin, D.2    Shaw, T.C.3    Stylianou, E.4
  • 4
    • 0034966992 scopus 로고    scopus 로고
    • Cytokinesis in prokaryotes and eukaryotes: common principles and different solutions
    • Nanninga N. Cytokinesis in prokaryotes and eukaryotes: common principles and different solutions. Microbiol Mol Biol Rev 65 2 (2001) 319-333
    • (2001) Microbiol Mol Biol Rev , vol.65 , Issue.2 , pp. 319-333
    • Nanninga, N.1
  • 5
    • 0032437666 scopus 로고    scopus 로고
    • Signaling to the actin cytoskeleton
    • Schmidt A., and Hall M.N. Signaling to the actin cytoskeleton. Annu Rev Cell Dev Biol 14 (1998) 305-338
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 305-338
    • Schmidt, A.1    Hall, M.N.2
  • 6
    • 33646137375 scopus 로고    scopus 로고
    • Cytoskeletal architecture differentially controls post-transcriptional processing of IL-6 and IL-8 mRNA in airway epithelial-like cells
    • Van den Berg A., Freitas J., Keles F., Snoek M., Van Marle J., Jansen H.M., et al. Cytoskeletal architecture differentially controls post-transcriptional processing of IL-6 and IL-8 mRNA in airway epithelial-like cells. Exp Cell Res 312 9 (2006) 1496-1506
    • (2006) Exp Cell Res , vol.312 , Issue.9 , pp. 1496-1506
    • Van den Berg, A.1    Freitas, J.2    Keles, F.3    Snoek, M.4    Van Marle, J.5    Jansen, H.M.6
  • 7
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles F., Posern G., Zaromytidou A.I., and Treisman R. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113 3 (2003) 329-342
    • (2003) Cell , vol.113 , Issue.3 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 8
    • 0035808389 scopus 로고    scopus 로고
    • Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization
    • Mack C.P., Somlyo A.V., Hautmann M., Somlyo A.P., and Owens G.K. Smooth muscle differentiation marker gene expression is regulated by RhoA-mediated actin polymerization. J Biol Chem 276 1 (1999) 341-347
    • (1999) J Biol Chem , vol.276 , Issue.1 , pp. 341-347
    • Mack, C.P.1    Somlyo, A.V.2    Hautmann, M.3    Somlyo, A.P.4    Owens, G.K.5
  • 9
    • 0842325726 scopus 로고    scopus 로고
    • Actin cytoskeleton regulates calcium dynamics and NFAT nuclear duration
    • Rivas F.V., O'Keefe J.P., Alegre M.L., and Gajewski T.F. Actin cytoskeleton regulates calcium dynamics and NFAT nuclear duration. Mol Cell Biol 24 4 (2004) 1628-1639
    • (2004) Mol Cell Biol , vol.24 , Issue.4 , pp. 1628-1639
    • Rivas, F.V.1    O'Keefe, J.P.2    Alegre, M.L.3    Gajewski, T.F.4
  • 10
    • 0032493028 scopus 로고    scopus 로고
    • Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction
    • Holsinger L.J., Graef I.A., Swat W., Chi T., Bautista D.M., Davidson L., et al. Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction. Curr Biol 8 10 (1998) 563-572
    • (1998) Curr Biol , vol.8 , Issue.10 , pp. 563-572
    • Holsinger, L.J.1    Graef, I.A.2    Swat, W.3    Chi, T.4    Bautista, D.M.5    Davidson, L.6
  • 11
    • 1242316973 scopus 로고    scopus 로고
    • An actin-myosin complex on actively transcribing genes
    • Fomproix N., and Percipalle P. An actin-myosin complex on actively transcribing genes. Exp Cell Res 294 1 (2004) 140-148
    • (2004) Exp Cell Res , vol.294 , Issue.1 , pp. 140-148
    • Fomproix, N.1    Percipalle, P.2
  • 12
    • 10644294832 scopus 로고    scopus 로고
    • A role for beta-actin in RNA polymerase III transcription
    • Hu P., Wu S., and Hernandez N. A role for beta-actin in RNA polymerase III transcription. Genes Dev 18 24 (2004) 3010-3015
    • (2004) Genes Dev , vol.18 , Issue.24 , pp. 3010-3015
    • Hu, P.1    Wu, S.2    Hernandez, N.3
  • 13
    • 7944239067 scopus 로고    scopus 로고
    • Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II
    • Hofmann W.A., Stojiljkovic L., Fuchsova B., Vargas G.M., Mavrommatis E., Philimonenko V., et al. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat Cell Biol 6 11 (2004) 1094-1101
    • (2004) Nat Cell Biol , vol.6 , Issue.11 , pp. 1094-1101
    • Hofmann, W.A.1    Stojiljkovic, L.2    Fuchsova, B.3    Vargas, G.M.4    Mavrommatis, E.5    Philimonenko, V.6
  • 14
    • 0033556172 scopus 로고    scopus 로고
    • Multiple signal transduction pathways regulate TNF-induced actin reorganization in macrophages: inhibition of Cdc42-mediated filopodium formation by TNF
    • Peppelenbosch M., Boone E., Jones G.E., van Deventer S.J., Haegeman G., Fiers W., et al. Multiple signal transduction pathways regulate TNF-induced actin reorganization in macrophages: inhibition of Cdc42-mediated filopodium formation by TNF. J Immunol 162 2 (1999) 837-845
    • (1999) J Immunol , vol.162 , Issue.2 , pp. 837-845
    • Peppelenbosch, M.1    Boone, E.2    Jones, G.E.3    van Deventer, S.J.4    Haegeman, G.5    Fiers, W.6
  • 15
    • 0032702311 scopus 로고    scopus 로고
    • The IL-1 receptor and Rho directly associate to drive cell activation in inflammation
    • Singh R., Wang B., Shirvaikar A., Khan S., Kamat S., Schelling J.R., et al. The IL-1 receptor and Rho directly associate to drive cell activation in inflammation. J Clin Invest 103 11 (1999) 1561-1570
    • (1999) J Clin Invest , vol.103 , Issue.11 , pp. 1561-1570
    • Singh, R.1    Wang, B.2    Shirvaikar, A.3    Khan, S.4    Kamat, S.5    Schelling, J.R.6
  • 16
    • 0033990255 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces cytoskeletal rearrangement in small intestinal lamina propria fibroblasts: actin assembly is essential for lipopolysaccharide signaling
    • Chakravortty D., and Nanda Kumar K.S. Bacterial lipopolysaccharide induces cytoskeletal rearrangement in small intestinal lamina propria fibroblasts: actin assembly is essential for lipopolysaccharide signaling. Biochim Biophys Acta 1500 1 (2000) 125-136
    • (2000) Biochim Biophys Acta , vol.1500 , Issue.1 , pp. 125-136
    • Chakravortty, D.1    Nanda Kumar, K.S.2
  • 17
    • 0037852065 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 4 by lipopolysaccharide during cellular invasion by live Salmonella typhimurium is a critical but not exclusive event leading to macrophage responses
    • Royle M.C., Totemeyer S., Alldridge L.C., Maskell D.J., and Bryant C.E. Stimulation of Toll-like receptor 4 by lipopolysaccharide during cellular invasion by live Salmonella typhimurium is a critical but not exclusive event leading to macrophage responses. J Immunol 170 11 (2003) 5445-5454
    • (2003) J Immunol , vol.170 , Issue.11 , pp. 5445-5454
    • Royle, M.C.1    Totemeyer, S.2    Alldridge, L.C.3    Maskell, D.J.4    Bryant, C.E.5
  • 18
    • 0037089033 scopus 로고    scopus 로고
    • beta1 and beta2 integrins activate different signalling pathways in monocytes
    • Reyes-Reyes M., Mora N., Gonzalez G., and Rosales C. beta1 and beta2 integrins activate different signalling pathways in monocytes. Biochem J 363 Pt2 (2002) 273-280
    • (2002) Biochem J , vol.363 , Issue.PART 2 , pp. 273-280
    • Reyes-Reyes, M.1    Mora, N.2    Gonzalez, G.3    Rosales, C.4
  • 19
    • 0035798543 scopus 로고    scopus 로고
    • Chemoattractant-stimulated NF-kappaB activation is dependent on the low molecular weight GTPase RhoA
    • Huang S., Chen L.Y., Zuraw B.L., Ye R.D., and Pan Z.K. Chemoattractant-stimulated NF-kappaB activation is dependent on the low molecular weight GTPase RhoA. J Biol Chem 276 44 (2001) 40977-40981
    • (2001) J Biol Chem , vol.276 , Issue.44 , pp. 40977-40981
    • Huang, S.1    Chen, L.Y.2    Zuraw, B.L.3    Ye, R.D.4    Pan, Z.K.5
  • 20
    • 17644371672 scopus 로고    scopus 로고
    • Perturbation of actin dynamics induces NF-kappaB activation in myelomonocytic cells through an NADPH oxidase-dependent pathway
    • Kustermans G., El Benna J., Piette J., and Legrand-Poels S. Perturbation of actin dynamics induces NF-kappaB activation in myelomonocytic cells through an NADPH oxidase-dependent pathway. Biochem J 387 Pt2 (2005) 531-540
    • (2005) Biochem J , vol.387 , Issue.PART 2 , pp. 531-540
    • Kustermans, G.1    El Benna, J.2    Piette, J.3    Legrand-Poels, S.4
  • 21
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses
    • Ghosh S., May M.J., and Kopp E.B. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16 (1998) 225-260
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 22
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden M.S., and Ghosh S. Signaling to NF-kappaB. Genes Dev 18 18 (2004) 2195-2224
    • (2004) Genes Dev , vol.18 , Issue.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 23
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • Martin M.U., and Wesche H. Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim Biophys Acta 1592 3 (2002) 265-280
    • (2002) Biochim Biophys Acta , vol.1592 , Issue.3 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 24
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A., Cook A., Lin Y., Rodriguez Y., Kelliher M., and Liu Z. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12 4 (2000) 419-429
    • (2000) Immunity , vol.12 , Issue.4 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 25
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S., and Takeda K. Toll-like receptor signalling. Nat Rev Immunol 4 7 (2004) 499-511
    • (2004) Nat Rev Immunol , vol.4 , Issue.7 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 26
    • 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 18 1 (2006) 3-9
    • (2006) Curr Opin Immunol , vol.18 , Issue.1 , pp. 3-9
    • O'Neill, L.A.1
  • 27
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakaw M., and Karin M. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91 2 (1997) 243-252
    • (1997) Cell , vol.91 , Issue.2 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakaw, M.4    Karin, M.5
  • 28
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93 7 (1998) 1231-1240
    • (1998) Cell , vol.93 , Issue.7 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6
  • 29
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
    • Karin M., and Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 18 (2000) 621-663
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 30
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S., and Karin M. Missing pieces in the NF-kappaB puzzle. Cell (Cambridge, Mass) 109 (2002) S81-S96
    • (2002) Cell (Cambridge, Mass) , vol.109
    • Ghosh, S.1    Karin, M.2
  • 31
    • 0034080318 scopus 로고    scopus 로고
    • The biology of chemokines and their receptors
    • Rossi D., and Zlotnik A. The biology of chemokines and their receptors. Annu Rev Immunol 18 (2000) 217-242
    • (2000) Annu Rev Immunol , vol.18 , pp. 217-242
    • Rossi, D.1    Zlotnik, A.2
  • 32
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen L.F., and Greene W.C. Shaping the nuclear action of NF-kappaB. Nat Rev Mol Cell Biol 5 5 (2004) 392-401
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 33
    • 33750457370 scopus 로고    scopus 로고
    • Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
    • Perkins N.D. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 25 51 (2006) 6717-6730
    • (2006) Oncogene , vol.25 , Issue.51 , pp. 6717-6730
    • Perkins, N.D.1
  • 34
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen L.F., Mu Y., and Greene W.C. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 21 23 (2002) 6539-6548
    • (2002) EMBO J , vol.21 , Issue.23 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 35
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H., Voll R.E., and Gosh S. Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell 1 5 (1998) 661-671
    • (1998) Mol Cell , vol.1 , Issue.5 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Gosh, S.3
  • 37
    • 0033837634 scopus 로고    scopus 로고
    • Regulation of gene expression by transcription factor acetylation
    • Bannister A.J., and Miska E.A. Regulation of gene expression by transcription factor acetylation. Cell Mol Life Sci 57 8-9 (2000) 1184-1192
    • (2000) Cell Mol Life Sci , vol.57 , Issue.8-9 , pp. 1184-1192
    • Bannister, A.J.1    Miska, E.A.2
  • 38
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., and Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20 8 (1998) 615-626
    • (1998) Bioessays , vol.20 , Issue.8 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 40
    • 0035629777 scopus 로고    scopus 로고
    • Importance of post-transcriptional regulation of chemokine genes by oxidative stress
    • Josse C., Boelaert J.R., Best-Belpomme M., and Piette J. Importance of post-transcriptional regulation of chemokine genes by oxidative stress. Biochem J 360 2 (2001) 321-333
    • (2001) Biochem J , vol.360 , Issue.2 , pp. 321-333
    • Josse, C.1    Boelaert, J.R.2    Best-Belpomme, M.3    Piette, J.4
  • 41
    • 34248226821 scopus 로고    scopus 로고
    • Modulation of Nod2-dependent NF-kappaB signaling by the actin cytoskeleton
    • Legrand-Poels S., Kustermans G., Bex F., Kremmer E., Kufer T.A., and Piette J. Modulation of Nod2-dependent NF-kappaB signaling by the actin cytoskeleton. J Cell Sci 120 Pt7 (2007) 1299-1310
    • (2007) J Cell Sci , vol.120 , Issue.PART 7 , pp. 1299-1310
    • Legrand-Poels, S.1    Kustermans, G.2    Bex, F.3    Kremmer, E.4    Kufer, T.A.5    Piette, J.6
  • 42
    • 0036363622 scopus 로고    scopus 로고
    • Involvement of oxidative stress in NF-kappaB activation in endothelial cells treated by photodynamic therapy
    • Volanti C., Matroule J.Y., and Piette J. Involvement of oxidative stress in NF-kappaB activation in endothelial cells treated by photodynamic therapy. Photochem Photobiol 75 1 (2002) 36-45
    • (2002) Photochem Photobiol , vol.75 , Issue.1 , pp. 36-45
    • Volanti, C.1    Matroule, J.Y.2    Piette, J.3
  • 43
    • 18344364385 scopus 로고    scopus 로고
    • Distinct transduction mechanisms of cyclooxygenase 2 gene activation in tumour cells after photodynamic therapy
    • Volanti C., Hendrickx N., Van Lint C., Matroule J.Y., Agostinis P., and Piette J. Distinct transduction mechanisms of cyclooxygenase 2 gene activation in tumour cells after photodynamic therapy. Oncogene 24 18 (2005) 2981-2991
    • (2005) Oncogene , vol.24 , Issue.18 , pp. 2981-2991
    • Volanti, C.1    Hendrickx, N.2    Van Lint, C.3    Matroule, J.Y.4    Agostinis, P.5    Piette, J.6
  • 44
    • 34447509891 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor trichostatin A sustains sodium pervanadate-induced NF-kappaB activation by delaying IkappaBalpha mRNA resynthesis: comparison with tumor necrosis factor alpha
    • Horion J., Gloire G., El Mjiyad N., Quivy V., Vermeulen L., Vanden Berghe W., et al. Histone deacetylase inhibitor trichostatin A sustains sodium pervanadate-induced NF-kappaB activation by delaying IkappaBalpha mRNA resynthesis: comparison with tumor necrosis factor alpha. J Biol Chem 282 21 (2007) 15383-15393
    • (2007) J Biol Chem , vol.282 , Issue.21 , pp. 15383-15393
    • Horion, J.1    Gloire, G.2    El Mjiyad, N.3    Quivy, V.4    Vermeulen, L.5    Vanden Berghe, W.6
  • 45
    • 0025731586 scopus 로고
    • Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments
    • Sampath P., and Pollard T.D. Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments. Biochemistry 30 7 (1991) 1073-1080
    • (1991) Biochemistry , vol.30 , Issue.7 , pp. 1073-1080
    • Sampath, P.1    Pollard, T.D.2
  • 46
    • 33847733962 scopus 로고    scopus 로고
    • Disassembly of actin filaments by botulinum C2 toxin and actin-filament-disrupting agents induces assembly of microtubules in human leukaemia cell lines
    • Uematsu Y., Kogo Y., and Ohishi I. Disassembly of actin filaments by botulinum C2 toxin and actin-filament-disrupting agents induces assembly of microtubules in human leukaemia cell lines. Biol Cell 99 3 (1999) 141-150
    • (1999) Biol Cell , vol.99 , Issue.3 , pp. 141-150
    • Uematsu, Y.1    Kogo, Y.2    Ohishi, I.3
  • 47
    • 7044269092 scopus 로고    scopus 로고
    • Chemokines: role in inflammation and immune surveillance
    • Moser B., and Willimann K. Chemokines: role in inflammation and immune surveillance. Ann Rheum Dis 63 Suppl 2 (2004) ii84-ii89
    • (2004) Ann Rheum Dis , vol.63 , Issue.SUPPL. 2
    • Moser, B.1    Willimann, K.2
  • 48
    • 0033192591 scopus 로고    scopus 로고
    • Key role of chemokines and chemokine receptors in inflammation, immunity, neoplasia, and infectious disease
    • Rottman J.B. Key role of chemokines and chemokine receptors in inflammation, immunity, neoplasia, and infectious disease. Vet Pathol 36 5 (1999) 357-367
    • (1999) Vet Pathol , vol.36 , Issue.5 , pp. 357-367
    • Rottman, J.B.1
  • 49
    • 0032738096 scopus 로고    scopus 로고
    • Chemokines and chemokine receptors in infectious diseases
    • Mahalingam S., and Karupiah G. Chemokines and chemokine receptors in infectious diseases. Immunol Cell Biol 77 (1999) 469-475
    • (1999) Immunol Cell Biol , vol.77 , pp. 469-475
    • Mahalingam, S.1    Karupiah, G.2
  • 50
    • 0029906571 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation of interleukin-8
    • Villarete L.H., and Remick D.G. Transcriptional and post-transcriptional regulation of interleukin-8. Am J Pathol 149 5 (1996) 1685-1693
    • (1996) Am J Pathol , vol.149 , Issue.5 , pp. 1685-1693
    • Villarete, L.H.1    Remick, D.G.2
  • 51
    • 34247532885 scopus 로고    scopus 로고
    • Mechanism regulating cell surface expression and activation of Toll-like receptor 4
    • Saitoh S.I., and Miyake K. Mechanism regulating cell surface expression and activation of Toll-like receptor 4. Chem Rec 6 6 (2006) 311-319
    • (2006) Chem Rec , vol.6 , Issue.6 , pp. 311-319
    • Saitoh, S.I.1    Miyake, K.2
  • 52
    • 0037033073 scopus 로고    scopus 로고
    • Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction
    • Latz E., Visintin A., Lien E., Fitzgerald K.A., Monks B.G., Kurt-Jones E.A., et al. Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction. J Biol Chem 277 38 (2002) 47834-47843
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 47834-47843
    • Latz, E.1    Visintin, A.2    Lien, E.3    Fitzgerald, K.A.4    Monks, B.G.5    Kurt-Jones, E.A.6
  • 53
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati T., and Schliwa M. Powering membrane traffic in endocytosis and recycling. Nat Rev Mol Cell Biol 7 12 (2006) 897-908
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.12 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 54
    • 33644508366 scopus 로고    scopus 로고
    • Endocytic pathways regulate Toll-like receptor 4 signaling and link innate and adaptive immunity
    • Husebye H., Halaas O., Stenmark H., Tunheim G., Sandanger O., Bogen B., et al. Endocytic pathways regulate Toll-like receptor 4 signaling and link innate and adaptive immunity. EMBO J 25 4 (2006) 683-692
    • (2006) EMBO J , vol.25 , Issue.4 , pp. 683-692
    • Husebye, H.1    Halaas, O.2    Stenmark, H.3    Tunheim, G.4    Sandanger, O.5    Bogen, B.6
  • 55
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
    • Kagan J.C., Su T., Horng T., Chow A., Akira S., and Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta. Nat Immunol 9 4 (2008) 361-368
    • (2008) Nat Immunol , vol.9 , Issue.4 , pp. 361-368
    • Kagan, J.C.1    Su, T.2    Horng, T.3    Chow, A.4    Akira, S.5    Medzhitov, R.6
  • 56
    • 34249289745 scopus 로고    scopus 로고
    • TNF-alpha-induced NF-kappaB/RelA Ser(276) phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway
    • Jamaluddin M., Wang S., Boldogh I., Tian B., and Brasier A.R. TNF-alpha-induced NF-kappaB/RelA Ser(276) phosphorylation and enhanceosome formation is mediated by an ROS-dependent PKAc pathway. Cell Signal 19 7 (2007) 1419-1433
    • (2007) Cell Signal , vol.19 , Issue.7 , pp. 1419-1433
    • Jamaluddin, M.1    Wang, S.2    Boldogh, I.3    Tian, B.4    Brasier, A.R.5
  • 57
    • 0037451357 scopus 로고    scopus 로고
    • Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)
    • Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., and Haegeman G. Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J 22 6 (2003) 1313-1324
    • (2003) EMBO J , vol.22 , Issue.6 , pp. 1313-1324
    • Vermeulen, L.1    De Wilde, G.2    Van Damme, P.3    Vanden Berghe, W.4    Haegeman, G.5
  • 58
    • 0037851769 scopus 로고    scopus 로고
    • IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide
    • Yang F., Tang E., Guan K., and Wang C.Y. IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide. J Immunol 170 11 (2003) 5630-5635
    • (2003) J Immunol , vol.170 , Issue.11 , pp. 5630-5635
    • Yang, F.1    Tang, E.2    Guan, K.3    Wang, C.Y.4
  • 59
    • 0032589462 scopus 로고    scopus 로고
    • IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H., Chiba H., Miyoshi H., Sugita T., and Toriumi W. IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 274 43 (1999) 30353-30356
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 60
    • 0037382605 scopus 로고    scopus 로고
    • Functional consequences of histone modifications
    • Iizuka M., and Smith M.M. Functional consequences of histone modifications. Curr Opin Genet Dev 13 2 (2003) 154-160
    • (2003) Curr Opin Genet Dev , vol.13 , Issue.2 , pp. 154-160
    • Iizuka, M.1    Smith, M.M.2
  • 61
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer D.A. Coupling actin dynamics and membrane dynamics during endocytosis. Curr Opin Cell Biol 14 1 (2002) 76-81
    • (2002) Curr Opin Cell Biol , vol.14 , Issue.1 , pp. 76-81
    • Schafer, D.A.1
  • 62
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze C., Fujimoto L.M., Yin H.L., and Schmid S.L. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J Biol Chem 272 33 (1997) 20332-20335
    • (1997) J Biol Chem , vol.272 , Issue.33 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 63
    • 0034139820 scopus 로고    scopus 로고
    • Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells
    • Fujimoto L.M., Roth R., Heuser J.E., and Schmid S.L. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells. Traffic 1 2 (2000) 161-171
    • (2000) Traffic , vol.1 , Issue.2 , pp. 161-171
    • Fujimoto, L.M.1    Roth, R.2    Heuser, J.E.3    Schmid, S.L.4
  • 64
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M., Clifton A.D., Lucocq L.M., and Alessi D.R. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J 17 15 (1998) 4426-4441
    • (1998) EMBO J , vol.17 , Issue.15 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 65
    • 0033215340 scopus 로고    scopus 로고
    • Two co-existing mechanisms for nuclear import of MAP kinase: passive diffusion of a monomer and active transport of a dimer
    • Adachi M., Fukuda M., and Nishida E. Two co-existing mechanisms for nuclear import of MAP kinase: passive diffusion of a monomer and active transport of a dimer. EMBO J 18 19 (1999) 5347-5358
    • (1999) EMBO J , vol.18 , Issue.19 , pp. 5347-5358
    • Adachi, M.1    Fukuda, M.2    Nishida, E.3
  • 66
    • 0034610996 scopus 로고    scopus 로고
    • Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism
    • Adachi M., Fukuda M., and Nishida E. Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism. J Cell Biol 148 5 (2000) 849-856
    • (2000) J Cell Biol , vol.148 , Issue.5 , pp. 849-856
    • Adachi, M.1    Fukuda, M.2    Nishida, E.3
  • 67
    • 1442309964 scopus 로고    scopus 로고
    • Regulation of Ras-MAPK pathway mitogenic activity by restricting nuclear entry of activated MAPK in endoderm differentiation of embryonic carcinoma and stem cells
    • Smith E.R., Smedberg J.L., Rula M.E., and Xu X.X. Regulation of Ras-MAPK pathway mitogenic activity by restricting nuclear entry of activated MAPK in endoderm differentiation of embryonic carcinoma and stem cells. J Cell Biol 164 (2004) 689-699
    • (2004) J Cell Biol , vol.164 , pp. 689-699
    • Smith, E.R.1    Smedberg, J.L.2    Rula, M.E.3    Xu, X.X.4
  • 68
    • 0033568608 scopus 로고    scopus 로고
    • The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism
    • Winzen R., Kracht M., Ritter B., Wilhelm A., Chen C.Y., Shyu A.B., et al. The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism. EMBO J 18 18 (1999) 4969-4980
    • (1999) EMBO J , vol.18 , Issue.18 , pp. 4969-4980
    • Winzen, R.1    Kracht, M.2    Ritter, B.3    Wilhelm, A.4    Chen, C.Y.5    Shyu, A.B.6
  • 69
    • 0028788194 scopus 로고
    • AU-rich elements: characterization and importance in mRNA degradation
    • Chen C.Y., and Shyu A.B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem Sci 20 11 (1995) 465-470
    • (1995) Trends Biochem Sci , vol.20 , Issue.11 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 70
    • 0038185346 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression by degradation of messenger RNAs
    • Bevilacqua A., Ceriani M.C., Capaccioli S., and Nicolin A. Post-transcriptional regulation of gene expression by degradation of messenger RNAs. J Cell Physiol 195 3 (2003) 356-372
    • (2003) J Cell Physiol , vol.195 , Issue.3 , pp. 356-372
    • Bevilacqua, A.1    Ceriani, M.C.2    Capaccioli, S.3    Nicolin, A.4
  • 71
    • 0032823313 scopus 로고    scopus 로고
    • Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways
    • Holtmann H., Winzen R., Holland P., Eickemeier S., Hoffmann E., Wallach D., et al. Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways. Mol Cell Biol 19 10 (1999) 6742-6753
    • (1999) Mol Cell Biol , vol.19 , Issue.10 , pp. 6742-6753
    • Holtmann, H.1    Winzen, R.2    Holland, P.3    Eickemeier, S.4    Hoffmann, E.5    Wallach, D.6
  • 72
    • 0032516626 scopus 로고    scopus 로고
    • Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin
    • Carballo E., Lai W.S., and Blackshear P.J. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 281 5379 (1998) 1001-1005
    • (1998) Science , vol.281 , Issue.5379 , pp. 1001-1005
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 74
    • 0034644837 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade
    • Brook M., Sully G., Clark A.R., and Saklatvala J. Regulation of tumour necrosis factor alpha mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett 483 1 (2000) 57-61
    • (2000) FEBS Lett , vol.483 , Issue.1 , pp. 57-61
    • Brook, M.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 75
    • 0034714265 scopus 로고    scopus 로고
    • Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability
    • Pages G., Berra E., Milanini J., Levy A.P., and Pouyssegur J. Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability. J Biol Chem 275 34 (2000) 26484-26491
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 26484-26491
    • Pages, G.1    Berra, E.2    Milanini, J.3    Levy, A.P.4    Pouyssegur, J.5
  • 76
    • 0035794225 scopus 로고    scopus 로고
    • Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts
    • Rutault K., Hazzalin C.A., and Mahadevan L.C. Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-alpha) mRNA induction. Evidence for selective destabilization of TNF-alpha transcripts. J Biol Chem 276 9 (2001) 6666-6674
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6666-6674
    • Rutault, K.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 77
    • 0034746363 scopus 로고    scopus 로고
    • The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR
    • Dean J.L., Wait R., Mahtani K.R., Sully G., Clark A.R., and Saklatvala J. The 3′ untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR. Mol Cell Biol 21 3 (2001) 721-730
    • (2001) Mol Cell Biol , vol.21 , Issue.3 , pp. 721-730
    • Dean, J.L.1    Wait, R.2    Mahtani, K.R.3    Sully, G.4    Clark, A.R.5    Saklatvala, J.6
  • 78
    • 0030882497 scopus 로고    scopus 로고
    • Interaction of AU-rich sequence binding proteins with actin: possible involvement of the actin cytoskeleton in lymphokine mRNA turnover
    • Henics T., Nagy E., and Szekeres-Bartho J. Interaction of AU-rich sequence binding proteins with actin: possible involvement of the actin cytoskeleton in lymphokine mRNA turnover. J Cell Physiol 173 1 (1997) 19-27
    • (1997) J Cell Physiol , vol.173 , Issue.1 , pp. 19-27
    • Henics, T.1    Nagy, E.2    Szekeres-Bartho, J.3
  • 79
    • 23344438447 scopus 로고    scopus 로고
    • Cell adhesion status-dependent histone acetylation is regulated through intracellular contractility-related signaling activities
    • Kim Y.B., Yu J., Lee S.Y., Lee M.S., Ko S.G., Ye S.K., et al. Cell adhesion status-dependent histone acetylation is regulated through intracellular contractility-related signaling activities. J Biol Chem 280 31 (2005) 28357-28364
    • (2005) J Biol Chem , vol.280 , Issue.31 , pp. 28357-28364
    • Kim, Y.B.1    Yu, J.2    Lee, S.Y.3    Lee, M.S.4    Ko, S.G.5    Ye, S.K.6
  • 80
    • 0027081132 scopus 로고
    • Tumor necrosis factor-alpha decreases neutrophil chemotaxis to N-formyl-1-methionyl-1-leucyl-1-phenylalanine: analysis of single cell movement
    • Vollmer K.L., Alberts J.S., Carper H.T., and Mandell G.L. Tumor necrosis factor-alpha decreases neutrophil chemotaxis to N-formyl-1-methionyl-1-leucyl-1-phenylalanine: analysis of single cell movement. J Leukoc Biol 52 6 (1992) 630-636
    • (1992) J Leukoc Biol , vol.52 , Issue.6 , pp. 630-636
    • Vollmer, K.L.1    Alberts, J.S.2    Carper, H.T.3    Mandell, G.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.