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Volumn 10, Issue 4, 2014, Pages

Role of Calmodulin-Calmodulin Kinase II, cAMP/Protein Kinase A and ERK 1/2 on Aeromonas hydrophila-Induced Apoptosis of Head Kidney Macrophages

Author keywords

[No Author keywords available]

Indexed keywords

1, 4 DIAMINO 1, 4 BIS (2 AMINOPHENYLTHIO) 2, 3 DICYANOBUTADIENE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CHANNEL AFFECTING AGENT; CALMIDAZOLIUM CHLORIDE; CALMODULIN; CALPAIN 2; CASPASE 3; CYCLIC AMP DEPENDENT PROTEIN KINASE; EGTAZIC ACID; ESTER; KN 92; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO] METHYL] PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; NIFEDIPINE; PROTEIN KINASE INHIBITOR; UNCLASSIFIED DRUG; VERAPAMIL; [1 2 BIS (O AMINOPHENOXY) ETHANE N N N9 N9 TETRAACETIC ACID TETRA (ACETOXYMETHYL) ESTER]; FISH PROTEIN;

EID: 84901332229     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004018     Document Type: Article
Times cited : (35)

References (54)
  • 1
    • 4444273975 scopus 로고    scopus 로고
    • Aeromonas hydrophila cytotoxic enterotoxin activates mitogen-activated protein kinases and induces apoptosis in murine macrophages and human intestinal epithelial cells
    • Galindo CL, Fadl AA, Sha J, Gutierrez Jr C, Popov VL, et al. (2004) Aeromonas hydrophila cytotoxic enterotoxin activates mitogen-activated protein kinases and induces apoptosis in murine macrophages and human intestinal epithelial cells. J Biol Chem 279: 37597-37612.
    • (2004) J Biol Chem , vol.279 , pp. 37597-37612
    • Galindo, C.L.1    Fadl, A.A.2    Sha, J.3    Gutierrez Jr., C.4    Popov, V.L.5
  • 2
    • 0010230914 scopus 로고    scopus 로고
    • Aeromonas species in diseases of animals
    • In: Austin B, Altwegg M, Gosling PJ, Joseph SW, editors, First edition. Chicester: John Wiley & Sons, Ltd
    • Gosling PJ (1996) Aeromonas species in diseases of animals. In: Austin B, Altwegg M, Gosling PJ, Joseph SW, editors. The Genus: Aeromonas. First edition. Chicester: John Wiley & Sons, Ltd. p.175.
    • (1996) The Genus: Aeromonas , pp. 175
    • Gosling, P.J.1
  • 3
    • 1242343771 scopus 로고    scopus 로고
    • Calcium signalling during cell interactions with bacterial pathogens
    • Nhieu GTV, Clair C, Grompone G, Sansonetti P, (2004) Calcium signalling during cell interactions with bacterial pathogens. Biol Cell 96: 93-101.
    • (2004) Biol Cell , vol.96 , pp. 93-101
    • Nhieu, G.T.V.1    Clair, C.2    Grompone, G.3    Sansonetti, P.4
  • 4
    • 33744918768 scopus 로고    scopus 로고
    • Group B Streptococcus induces macrophage apoptosis by calpain activation
    • Fettucciari K, Fetriconi I, Mannucci R, Nicoletti I, Bartoli IA, et al. (2006) Group B Streptococcus induces macrophage apoptosis by calpain activation. J Immunol 176: 7542-7556.
    • (2006) J Immunol , vol.176 , pp. 7542-7556
    • Fettucciari, K.1    Fetriconi, I.2    Mannucci, R.3    Nicoletti, I.4    Bartoli, I.A.5
  • 5
    • 31944434700 scopus 로고    scopus 로고
    • Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality
    • Ikura AM, Ames JB, (2006) Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality. Proc Nat Aca Sci USA 103: 1159-1164.
    • (2006) Proc Nat Aca Sci USA , vol.103 , pp. 1159-1164
    • Ikura, A.M.1    Ames, J.B.2
  • 6
    • 70349696241 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways
    • Timmins JM, Oczan L, Seimon TA, Li G, Malagelada C, et al. (2009) Calcium/calmodulin-dependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways. J Clin Investig 119: 2925-2941.
    • (2009) J Clin Investig , vol.119 , pp. 2925-2941
    • Timmins, J.M.1    Oczan, L.2    Seimon, T.A.3    Li, G.4    Malagelada, C.5
  • 7
    • 13944278759 scopus 로고    scopus 로고
    • Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation
    • Schmitt JM, Guire ES, Saneyoshi T, Soderling TR, (2005) Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation. J Neurosci 25: 1281-1290.
    • (2005) J Neurosci , vol.25 , pp. 1281-1290
    • Schmitt, J.M.1    Guire, E.S.2    Saneyoshi, T.3    Soderling, T.R.4
  • 8
    • 33746341792 scopus 로고    scopus 로고
    • Activity-dependent gating of CaMKII autonomous activity by Drosophila CASK
    • Hodge JJL, Mullasseril P, Griffith LC, (2006) Activity-dependent gating of CaMKII autonomous activity by Drosophila CASK. Neuron 51: 327-337.
    • (2006) Neuron , vol.51 , pp. 327-337
    • Hodge, J.J.L.1    Mullasseril, P.2    Griffith, L.C.3
  • 9
    • 84856269574 scopus 로고    scopus 로고
    • CaMKII-γ mediates phosphorylation of BAD at Ser170 to regulate cytokine-dependent survival and proliferation
    • Hojabrpour P, Waissbluth I, Ghaffari M, Cox ME, Duronio V, (2012) CaMKII-γ mediates phosphorylation of BAD at Ser170 to regulate cytokine-dependent survival and proliferation. Biochem J 442: 139-149.
    • (2012) Biochem J , vol.442 , pp. 139-149
    • Hojabrpour, P.1    Waissbluth, I.2    Ghaffari, M.3    Cox, M.E.4    Duronio, V.5
  • 10
    • 50049106530 scopus 로고    scopus 로고
    • Charting calcium-regulated apoptosis pathways using chemical biology: role of calmodulin kinase II
    • doi:10.1186/1472-6769-8-2
    • Oloffsson MH, Havelka AM, Brnjic S, Shoshan MC, Linder S, (2008) Charting calcium-regulated apoptosis pathways using chemical biology: role of calmodulin kinase II. BMC Chem Biol 8: 2 doi: 10.1186/1472-6769-8-2.
    • (2008) BMC Chem Biol , vol.8 , pp. 2
    • Oloffsson, M.H.1    Havelka, A.M.2    Brnjic, S.3    Shoshan, M.C.4    Linder, S.5
  • 11
    • 84855350974 scopus 로고    scopus 로고
    • Cyclic AMP is both a pro-apoptotic and anti-apoptotic second messenger
    • doi:10.1111/j.1748-1716.2011.02273.x
    • Insel PA, Zhang L, Murray F, Yokouchi H, Zambon AC, (2011) Cyclic AMP is both a pro-apoptotic and anti-apoptotic second messenger. Acta Physiol 204: 277-287 doi: 10.1111/j.1748-1716.2011.02273.x.
    • (2011) Acta Physiol , vol.204 , pp. 277-287
    • Insel, P.A.1    Zhang, L.2    Murray, F.3    Yokouchi, H.4    Zambon, A.C.5
  • 12
    • 33947256514 scopus 로고    scopus 로고
    • Manipulation of host signalling pathways by anthrax toxins
    • Turk BE, (2007) Manipulation of host signalling pathways by anthrax toxins. Biochem J 402: 405-417.
    • (2007) Biochem J , vol.402 , pp. 405-417
    • Turk, B.E.1
  • 13
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R, Krebs EG, (1995) The MAPK signaling cascade. FASEB J 9: 726-735.
    • (1995) FASEB J , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 14
    • 2342562556 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in apoptosis regulation
    • Wada T, Penninger JM, (2004) Mitogen-activated protein kinases in apoptosis regulation. Oncogene 23: 2838-2849.
    • (2004) Oncogene , vol.23 , pp. 2838-2849
    • Wada, T.1    Penninger, J.M.2
  • 15
    • 84862908207 scopus 로고    scopus 로고
    • Cell death and infection: A double-edged sword for host and pathogen survival
    • Ashida H, Mimuro H, Ogawa M, Kobayashi T, Sanada T, et al. (2011) Cell death and infection: A double-edged sword for host and pathogen survival. J Cell Biol 195: 931-942.
    • (2011) J Cell Biol , vol.195 , pp. 931-942
    • Ashida, H.1    Mimuro, H.2    Ogawa, M.3    Kobayashi, T.4    Sanada, T.5
  • 16
    • 0348037573 scopus 로고    scopus 로고
    • Cytological ontogenesis and involution of the thymus and head-kidney in juvenile and old domestic carp: Is ageing in fish a chronological or growth-related phenomenon?
    • Becker BK, Fishelson L, Amselgruber WM, (2001) Cytological ontogenesis and involution of the thymus and head-kidney in juvenile and old domestic carp: Is ageing in fish a chronological or growth-related phenomenon? J Appl Ichthyol 17: 1-13.
    • (2001) J Appl Ichthyol , vol.17 , pp. 1-13
    • Becker, B.K.1    Fishelson, L.2    Amselgruber, W.M.3
  • 17
    • 79955739827 scopus 로고    scopus 로고
    • Neuroendocrine-immune interaction in fish: Differential regulation of phagocyte activity by neuroendocrine factors
    • Verburg-van Kemenade BML, Ribeiro CMS, Chadzinska M, (2011) Neuroendocrine-immune interaction in fish: Differential regulation of phagocyte activity by neuroendocrine factors. Gen Comp Immunol 172: 31-38.
    • (2011) Gen Comp Immunol , vol.172 , pp. 31-38
    • Verburg-van Kemenade, B.M.L.1    Ribeiro, C.M.S.2    Chadzinska, M.3
  • 18
    • 34247336456 scopus 로고    scopus 로고
    • An attenuated plasmid-cured strain of Aeromonas hydrophila elicits protective immunity in Clarias batrachus L
    • Majumdar T, Ghosh D, Datta S, Sahoo C, Pal J, et al. (2007) An attenuated plasmid-cured strain of Aeromonas hydrophila elicits protective immunity in Clarias batrachus L. Fish Shellfish Immunol. 23: 223-230.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 223-230
    • Majumdar, T.1    Ghosh, D.2    Datta, S.3    Sahoo, C.4    Pal, J.5
  • 19
    • 84862135101 scopus 로고    scopus 로고
    • Aeromonas hydrophila induced head kidney macrophage apoptosis in Clarias batrachus involves the activation of calpain and is caspase-3 mediated
    • Banerjee C, Goswami R, Verma G, Datta M, Mazumder S, (2012) Aeromonas hydrophila induced head kidney macrophage apoptosis in Clarias batrachus involves the activation of calpain and is caspase-3 mediated. Dev Comp Immunol 37: 323-333.
    • (2012) Dev Comp Immunol , vol.37 , pp. 323-333
    • Banerjee, C.1    Goswami, R.2    Verma, G.3    Datta, M.4    Mazumder, S.5
  • 20
    • 0026688138 scopus 로고
    • Calmidazolium, a calmodulin inhibitor, inhibits endothelium-dependent relaxations resistant to nitro-L-arginine in the canine coronary artery
    • Illiano S, Nagao T, Vanhoutte PM, (1992) Calmidazolium, a calmodulin inhibitor, inhibits endothelium-dependent relaxations resistant to nitro-L-arginine in the canine coronary artery. Br J Pharmacol 107: 387-392.
    • (1992) Br J Pharmacol , vol.107 , pp. 387-392
    • Illiano, S.1    Nagao, T.2    Vanhoutte, P.M.3
  • 21
    • 0037013222 scopus 로고    scopus 로고
    • STO-609, a specific inhibitor of the Ca2+/calmodulin-dependent protein kinase kinase
    • Tokumitsu H, Inuzuka H, Ishikawa Y, Ikeda M, Saji I, et al. (2002) STO-609, a specific inhibitor of the Ca2+/calmodulin-dependent protein kinase kinase. J Biol Chem 277: 15813-15818.
    • (2002) J Biol Chem , vol.277 , pp. 15813-15818
    • Tokumitsu, H.1    Inuzuka, H.2    Ishikawa, Y.3    Ikeda, M.4    Saji, I.5
  • 22
    • 0032239112 scopus 로고    scopus 로고
    • KN-93, an inhibitor of multifunctional Ca2+/calmodulin-dependent protein kinase, decreases early after depolarizations in rabbit heart
    • Anderson ME, Braun AP, Wu Y, Lu T, Wu Y, et al. (1998) KN-93, an inhibitor of multifunctional Ca2+/calmodulin-dependent protein kinase, decreases early after depolarizations in rabbit heart. J Pharmacol Exp Ther 287: 996-1006.
    • (1998) J Pharmacol Exp Ther , vol.287 , pp. 996-1006
    • Anderson, M.E.1    Braun, A.P.2    Wu, Y.3    Lu, T.4    Wu, Y.5
  • 23
    • 13844272287 scopus 로고    scopus 로고
    • Cellular bioterrorism: how Brucella corrupts macrophage physiology to promote invasion and proliferation
    • de Bagues Maria-Pilar J, Dudal S, Dornan J, Gross A, (2005) Cellular bioterrorism: how Brucella corrupts macrophage physiology to promote invasion and proliferation. Clin Immunol 114: 227-238.
    • (2005) Clin Immunol , vol.114 , pp. 227-238
    • de Bagues Maria-Pilar, J.1    Dudal, S.2    Dornan, J.3    Gross, A.4
  • 24
    • 85047687056 scopus 로고    scopus 로고
    • Coxiella burnetii alters cyclic AMP-dependent protein kinase signaling during growth in macrophages
    • MacDonald LJ, Kurten RC, Voth DE, (2012) Coxiella burnetii alters cyclic AMP-dependent protein kinase signaling during growth in macrophages. Infect Immun 80: 1980-1986.
    • (2012) Infect Immun , vol.80 , pp. 1980-1986
    • MacDonald, L.J.1    Kurten, R.C.2    Voth, D.E.3
  • 26
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken K, Aandahl EM, (2004) Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol Rev. 84: 137-167.
    • (2004) Physiol Rev , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 27
    • 48849116430 scopus 로고    scopus 로고
    • Pharmacological PKA inhibition: All may not be what it seems
    • doi:10.1126/scisignal.122re4
    • Murray AJ, (2008) Pharmacological PKA inhibition: All may not be what it seems. Science Signal 1 (22): re4 doi: 10.1126/scisignal.122re4.
    • (2008) Science Signal 1 , vol.22
    • Murray, A.J.1
  • 28
    • 2142763090 scopus 로고    scopus 로고
    • Increased mitogen-activated protein kinase activity and TNF-α production associated with Mycobacterium smegmatis-but not Mycobacterium avium-infected macrophages requires prolonged stimulation of the calmodulin/calmodulin kinase and cyclic AMP/Protein Kinase A pathways
    • Yadav M, Roach SK, Schorey JS, (2004) Increased mitogen-activated protein kinase activity and TNF-α production associated with Mycobacterium smegmatis-but not Mycobacterium avium-infected macrophages requires prolonged stimulation of the calmodulin/calmodulin kinase and cyclic AMP/Protein Kinase A pathways. J Immunol 172: 5588-5597.
    • (2004) J Immunol , vol.172 , pp. 5588-5597
    • Yadav, M.1    Roach, S.K.2    Schorey, J.S.3
  • 29
    • 67649836777 scopus 로고    scopus 로고
    • 1,4-diamino-2,3-dicyano-1,4-bis (methylthio) butadiene (U0126) enhances the cytotoxicity of combretastatin A4 independently of mitogen-activated protein kinase kinase
    • Quan H, Liu H, Li C, Lou L, (2009) 1,4-diamino-2,3-dicyano-1,4-bis (methylthio) butadiene (U0126) enhances the cytotoxicity of combretastatin A4 independently of mitogen-activated protein kinase kinase. J Pharmacol Exp Ther 330: 326-333.
    • (2009) J Pharmacol Exp Ther , vol.330 , pp. 326-333
    • Quan, H.1    Liu, H.2    Li, C.3    Lou, L.4
  • 30
    • 12444288064 scopus 로고    scopus 로고
    • The importance of calcium influx, calpain and calmodulin for the activation of CaCo-2 cell death pathways by Clostridium perfringens enterotoxin
    • Chakrabarti G, McClane MA, (2005) The importance of calcium influx, calpain and calmodulin for the activation of CaCo-2 cell death pathways by Clostridium perfringens enterotoxin. Cell Microbiol 7: 129-146.
    • (2005) Cell Microbiol , vol.7 , pp. 129-146
    • Chakrabarti, G.1    McClane, M.A.2
  • 31
    • 67651211895 scopus 로고    scopus 로고
    • Effects of decreased calmodulin protein on the survival mechanisms of alveolar macrophages during Pneumocystis pneumonia
    • Lasbury ME, Durant PJ, Liao CP, Lee CH, (2009) Effects of decreased calmodulin protein on the survival mechanisms of alveolar macrophages during Pneumocystis pneumonia. Infect Immun 79: 3344-3354.
    • (2009) Infect Immun , vol.79 , pp. 3344-3354
    • Lasbury, M.E.1    Durant, P.J.2    Liao, C.P.3    Lee, C.H.4
  • 32
    • 0034747998 scopus 로고    scopus 로고
    • Nitric oxide synthase sequences in the marine fish Stenotomus chrysops and the sea urchin Arbacia punctulata, and phylogenetic analysis of nitric oxide synthase calmodulin-binding domains
    • Cox RL, Mariano T, Heck DE, Laskin JD, Stegeman JJ, (2001) Nitric oxide synthase sequences in the marine fish Stenotomus chrysops and the sea urchin Arbacia punctulata, and phylogenetic analysis of nitric oxide synthase calmodulin-binding domains. Comp Biochem Physiol Part B 130: 479-491.
    • (2001) Comp Biochem Physiol Part B , vol.130 , pp. 479-491
    • Cox, R.L.1    Mariano, T.2    Heck, D.E.3    Laskin, J.D.4    Stegeman, J.J.5
  • 33
    • 18444384524 scopus 로고    scopus 로고
    • Calmodulin genes in zebrafish (revisited)
    • Friedberg F, Taliaferro LT, (2005) Calmodulin genes in zebrafish (revisited). Mol Biol Rep 32: 55-60.
    • (2005) Mol Biol Rep , vol.32 , pp. 55-60
    • Friedberg, F.1    Taliaferro, L.T.2
  • 34
    • 84858439862 scopus 로고    scopus 로고
    • Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
    • Vogel C, Marcotte EM, (2012) Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nat Rev Genet 13: 227.
    • (2012) Nat Rev Genet , vol.13 , pp. 227
    • Vogel, C.1    Marcotte, E.M.2
  • 35
    • 0024407571 scopus 로고
    • Calmodulin-binding proteins as calpain substrates
    • Wang KKW, Villalobo A, Roufogalis BD, (1989) Calmodulin-binding proteins as calpain substrates. Biochem J 262: 693-706.
    • (1989) Biochem J , vol.262 , pp. 693-706
    • Wang, K.K.W.1    Villalobo, A.2    Roufogalis, B.D.3
  • 36
    • 0035914462 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the Ca2+/calmodulin-dependent protein kinase-like kinase facilitates neuronal apoptosis
    • Kruidering M, Schouten T, Evan GI, Vreugdenhil E, (2001) Caspase-mediated cleavage of the Ca2+/calmodulin-dependent protein kinase-like kinase facilitates neuronal apoptosis. J Biol Chem 42: 38417-38425.
    • (2001) J Biol Chem , vol.42 , pp. 38417-38425
    • Kruidering, M.1    Schouten, T.2    Evan, G.I.3    Vreugdenhil, E.4
  • 37
    • 12544251260 scopus 로고    scopus 로고
    • Nuclear calpain regulates Ca2+-dependent signaling via proteolysis of nuclear Ca2+/calmodulin-dependent protein kinase type IV in cultured neurons
    • Tremper-Wells B, Vallano ML, (2005) Nuclear calpain regulates Ca2+-dependent signaling via proteolysis of nuclear Ca2+/calmodulin-dependent protein kinase type IV in cultured neurons. J Biol Chem 280: 2165-2175.
    • (2005) J Biol Chem , vol.280 , pp. 2165-2175
    • Tremper-Wells, B.1    Vallano, M.L.2
  • 38
  • 39
    • 0038528218 scopus 로고    scopus 로고
    • Subversion and utilization of the host cell cyclic adenosine 5′ -monophosphate/protein kinase A pathway by Brucella during macrophage infection
    • Gross A, Bouaboula M, Casellas P, Liautard JP, Dornand J, (2003) Subversion and utilization of the host cell cyclic adenosine 5′-monophosphate/protein kinase A pathway by Brucella during macrophage infection. J Immunol 170: 5607-5614.
    • (2003) J Immunol , vol.170 , pp. 5607-5614
    • Gross, A.1    Bouaboula, M.2    Casellas, P.3    Liautard, J.P.4    Dornand, J.5
  • 40
    • 0027374664 scopus 로고
    • Bordetella pertussis induces apoptosis in macrophages: role of adenylate cyclase-hemolysin
    • Khelef N, Zychlinsky A, Guiso N, (1993) Bordetella pertussis induces apoptosis in macrophages: role of adenylate cyclase-hemolysin. Infect Immun 61: 4064-4071.
    • (1993) Infect Immun , vol.61 , pp. 4064-4071
    • Khelef, N.1    Zychlinsky, A.2    Guiso, N.3
  • 41
    • 33744914838 scopus 로고    scopus 로고
    • Bacillus anthracis toxins inhibit human neutrophil NADPH oxidase activity
    • Crawford MA, Aylott CV, Bourdeau RW, Bokoch GM, (2006) Bacillus anthracis toxins inhibit human neutrophil NADPH oxidase activity. J Immunol 176: 7557-7565.
    • (2006) J Immunol , vol.176 , pp. 7557-7565
    • Crawford, M.A.1    Aylott, C.V.2    Bourdeau, R.W.3    Bokoch, G.M.4
  • 42
    • 33845984522 scopus 로고    scopus 로고
    • Characterization of DNA-binding specificity and analysis of binding sites of the Pseudomonas aeruginosa global regulator, Vfr, a homologue of the Escherichia coli cAMP receptor protein
    • Kanack KJ, Runyen-Janecky LJ, Ferrell EP, Suh SJ, West SHE, (2006) Characterization of DNA-binding specificity and analysis of binding sites of the Pseudomonas aeruginosa global regulator, Vfr, a homologue of the Escherichia coli cAMP receptor protein. Microbiol 152: 3485-3496.
    • (2006) Microbiol , vol.152 , pp. 3485-3496
    • Kanack, K.J.1    Runyen-Janecky, L.J.2    Ferrell, E.P.3    Suh, S.J.4    West, S.H.E.5
  • 43
    • 0026533289 scopus 로고
    • Porphyromonas gingivalis fimbriae induce expression of the neutrophil chemotactic factor KC gene of mouse peritoneal macrophages: role of protein kinase C
    • Hanazawa S, Murakami Y, Takeshita A, Kitami H, Ohta KA, et al. (1992) Porphyromonas gingivalis fimbriae induce expression of the neutrophil chemotactic factor KC gene of mouse peritoneal macrophages: role of protein kinase C. Infect Immun. 60: 1544-1549.
    • (1992) Infect Immun , vol.60 , pp. 1544-1549
    • Hanazawa, S.1    Murakami, Y.2    Takeshita, A.3    Kitami, H.4    Ohta, K.A.5
  • 44
    • 0034058065 scopus 로고    scopus 로고
    • The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages
    • Chopra AK, Xu XJ, Ribardo D, Gonzalez M, Kuhl K, et al. (2000) The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages. Infect Immun 68: 2808-2818.
    • (2000) Infect Immun , vol.68 , pp. 2808-2818
    • Chopra, A.K.1    Xu, X.J.2    Ribardo, D.3    Gonzalez, M.4    Kuhl, K.5
  • 45
    • 0035910523 scopus 로고    scopus 로고
    • Calmodulin Kinase II attenuation of gene transcription by preventing cAMP response element-binding protein (CREB) dimerization and binding of the CREB-binding protein
    • Wu X, McMurray CT, (2001) Calmodulin Kinase II attenuation of gene transcription by preventing cAMP response element-binding protein (CREB) dimerization and binding of the CREB-binding protein. J Biol Chem 276: 1735-1741.
    • (2001) J Biol Chem , vol.276 , pp. 1735-1741
    • Wu, X.1    McMurray, C.T.2
  • 46
    • 84856785397 scopus 로고    scopus 로고
    • Manipulation of kinase signaling by bacterial pathogens
    • Krachler AM, Woolery AR, Orth K, (2011) Manipulation of kinase signaling by bacterial pathogens. J Cell Biol 195: 1083-1092.
    • (2011) J Cell Biol , vol.195 , pp. 1083-1092
    • Krachler, A.M.1    Woolery, A.R.2    Orth, K.3
  • 47
    • 33645233855 scopus 로고    scopus 로고
    • Modulation of ERK 1/2 and p38 MAPK by lead in the cerebellum of Brazilian catfish Rhamdia quelen
    • Leal RB, Ribeiro SJ, Posser T, Cordova FM, Rigon Filho EZ, et al. (2006) Modulation of ERK 1/2 and p38 MAPK by lead in the cerebellum of Brazilian catfish Rhamdia quelen. Aqua Toxicol 77: 98-104.
    • (2006) Aqua Toxicol , vol.77 , pp. 98-104
    • Leal, R.B.1    Ribeiro, S.J.2    Posser, T.3    Cordova, F.M.4    Rigon Filho, E.Z.5
  • 48
    • 77957903728 scopus 로고    scopus 로고
    • Transcriptome and expression profiling analysis revealed changes of multiple signaling pathways involved in immunity in the large yellow croaker during Aeromonas hydrophila infection
    • doi:10.1186/1471-2164-11-506
    • Mu Y, Ding F, Cui P, Ao J, Hu S, Chen X, (2010) Transcriptome and expression profiling analysis revealed changes of multiple signaling pathways involved in immunity in the large yellow croaker during Aeromonas hydrophila infection. BMC Genomics 11: 506 doi: 10.1186/1471-2164-11-506.
    • (2010) BMC Genomics , vol.11 , pp. 506
    • Mu, Y.1    Ding, F.2    Cui, P.3    Ao, J.4    Hu, S.5    Chen, X.6
  • 49
    • 0038781803 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase-mediated signaling is essential for Pseudomonas aeruginosa ExoS-induced apoptosis
    • Jia J, Alaoui-El-Azher M, Chow M, Chambers TC, Baker H, et al. (2003) c-Jun NH2-terminal kinase-mediated signaling is essential for Pseudomonas aeruginosa ExoS-induced apoptosis. Infect Immun 71: 3361-3370.
    • (2003) Infect Immun , vol.71 , pp. 3361-3370
    • Jia, J.1    Alaoui-El-Azher, M.2    Chow, M.3    Chambers, T.C.4    Baker, H.5
  • 50
    • 0345170708 scopus 로고    scopus 로고
    • Activation of NF-κB and IL-8 by Yersinia enterocolitica invasin protein is conferred by engagement of Rac1 and MAP kinase cascades
    • Grassl GA, Kracht M, Wiedemann A, Hoffmann E, Aepfelbacher M, et al. (2003) Activation of NF-κB and IL-8 by Yersinia enterocolitica invasin protein is conferred by engagement of Rac1 and MAP kinase cascades. Cell Microbiol 5: 957-971.
    • (2003) Cell Microbiol , vol.5 , pp. 957-971
    • Grassl, G.A.1    Kracht, M.2    Wiedemann, A.3    Hoffmann, E.4    Aepfelbacher, M.5
  • 51
    • 9444270380 scopus 로고    scopus 로고
    • Hydrogen sulfide-induced apoptosis of human aorta smooth muscle cells via the activation of mitogen activated protein kinases and caspase-3
    • Yang G, Sun X, Wang R, (2004) Hydrogen sulfide-induced apoptosis of human aorta smooth muscle cells via the activation of mitogen activated protein kinases and caspase-3. FASEB J 18: 1782-1784.
    • (2004) FASEB J , vol.18 , pp. 1782-1784
    • Yang, G.1    Sun, X.2    Wang, R.3
  • 52
    • 0031954631 scopus 로고    scopus 로고
    • MEK kinase 1, a substrate for DEVD directed caspases, is involved in genotoxin-induced apoptosis
    • Widmann C, Gerwins P, Johnson NL, Jarpe MB, Johnson GL, (1998) MEK kinase 1, a substrate for DEVD directed caspases, is involved in genotoxin-induced apoptosis. Mol Cell Biol 18: 2416-2429.
    • (1998) Mol Cell Biol , vol.18 , pp. 2416-2429
    • Widmann, C.1    Gerwins, P.2    Johnson, N.L.3    Jarpe, M.B.4    Johnson, G.L.5
  • 53
    • 78751704538 scopus 로고    scopus 로고
    • Effect of acute and chronic arsenic exposure on growth, structure and virulence of Aeromonas hydrophila isolated from fish
    • Goswami R, Ghosh D, Saha DR, Padhy PK, Mazumder S, (2011) Effect of acute and chronic arsenic exposure on growth, structure and virulence of Aeromonas hydrophila isolated from fish. Microb Pathog 50: 63-69.
    • (2011) Microb Pathog , vol.50 , pp. 63-69
    • Goswami, R.1    Ghosh, D.2    Saha, D.R.3    Padhy, P.K.4    Mazumder, S.5
  • 54
    • 81155132565 scopus 로고    scopus 로고
    • Arsenic-induced alteration in intracellular calcium homeostasis induces head kidney macrophage apoptosis involving the activation of calpain-2 and ERK in Clarias batrachus
    • Banerjee C, Goswami R, Datta S, Rajagopal R, Mazumder S, (2011) Arsenic-induced alteration in intracellular calcium homeostasis induces head kidney macrophage apoptosis involving the activation of calpain-2 and ERK in Clarias batrachus. Toxicol Appl Pharmacol 256: 44-51.
    • (2011) Toxicol Appl Pharmacol , vol.256 , pp. 44-51
    • Banerjee, C.1    Goswami, R.2    Datta, S.3    Rajagopal, R.4    Mazumder, S.5


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