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Volumn 48, Issue 7, 2013, Pages 651-662

Acetate reduces PGE2 release and modulates phospholipase and cyclooxygenase levels in neuroglia stimulated with lipopolysaccharide

Author keywords

Acetate; Cyclooxygenase; Eicosanoid; Histone acetylation; Phospholipase

Indexed keywords

ACETIC ACID; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; HISTONE H3; INTERLEUKIN 1BETA; INTERLEUKIN 4; PHOSPHOLIPASE A2; PHOSPHOLIPASE C BETA1; PROSTAGLANDIN E2; SECRETORY PHOSPHOLIPASE A2; TRANSCRIPTION FACTOR RELA; HISTONE; LIPOPOLYSACCHARIDE; MEMBRANE PROTEIN; PHOSPHOLIPASE C BETA; PTGS1 PROTEIN, MOUSE; PTGS2 PROTEIN, MOUSE;

EID: 84879687458     PISSN: 00244201     EISSN: 15589307     Source Type: Journal    
DOI: 10.1007/s11745-013-3799-x     Document Type: Article
Times cited : (18)

References (59)
  • 4
    • 84868307408 scopus 로고    scopus 로고
    • Acetate supplementation reduces microglia activation and brain interleukin-1β levels in a rat model of Lyme neuroborreliosis
    • 23134838 10.1186/1742-2094-9-249 1:CAS:528:DC%2BC3sXlsVCjug%3D%3D
    • Brissette CA, Houdek HM, Floden AM, Rosenberger TA (2012) Acetate supplementation reduces microglia activation and brain interleukin-1β levels in a rat model of Lyme neuroborreliosis. J Neuroinflammation 9:249
    • (2012) J Neuroinflammation , vol.9 , pp. 249
    • Brissette, C.A.1    Houdek, H.M.2    Floden, A.M.3    Rosenberger, T.A.4
  • 5
    • 84873373580 scopus 로고    scopus 로고
    • Acetate supplementation increases brain phosphocreatine and reduces AMP levels with no effect on mitochondrial biogenesis
    • 23321384 10.1016/j.neuint.2013.01.004 1:CAS:528:DC%2BC3sXivFOqtbg%3D
    • Bhatt DP, Houdek HM, Watt JA, Rosenberger TA (2013) Acetate supplementation increases brain phosphocreatine and reduces AMP levels with no effect on mitochondrial biogenesis. Neurochem Int 62:296-305
    • (2013) Neurochem Int , vol.62 , pp. 296-305
    • Bhatt, D.P.1    Houdek, H.M.2    Watt, J.A.3    Rosenberger, T.A.4
  • 6
    • 79959196642 scopus 로고    scopus 로고
    • Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression
    • 21359531 10.1007/s11010-011-0751-3 1:CAS:528:DC%2BC3MXmtFSls7Y%3D
    • Soliman ML, Rosenberger TA (2011) Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression. Mol Cell Biochem 352:173-180
    • (2011) Mol Cell Biochem , vol.352 , pp. 173-180
    • Soliman, M.L.1    Rosenberger, T.A.2
  • 7
    • 84857935922 scopus 로고    scopus 로고
    • Acetate supplementation modulates brain histone acetylation and decreases interleukin-1beta expression in a rat model of neuroinflammation
    • 22413888 10.1186/1742-2094-9-51 1:CAS:528:DC%2BC38XmtFGisb4%3D
    • Soliman ML, Smith MD, Houdek HM, Rosenberger TA (2012) Acetate supplementation modulates brain histone acetylation and decreases interleukin-1beta expression in a rat model of neuroinflammation. J Neuroinflammation 9:51
    • (2012) J Neuroinflammation , vol.9 , pp. 51
    • Soliman, M.L.1    Smith, M.D.2    Houdek, H.M.3    Rosenberger, T.A.4
  • 8
    • 84867576303 scopus 로고    scopus 로고
    • Acetate reduces microglia inflammatory signaling in vitro
    • 22924711 10.1111/j.1471-4159.2012.07955.x 1:CAS:528:DC%2BC38XhsFSnsb7J
    • Soliman ML, Puig KL, Combs CK, Rosenberger TA (2012) Acetate reduces microglia inflammatory signaling in vitro. J Neurochem 123:555-567
    • (2012) J Neurochem , vol.123 , pp. 555-567
    • Soliman, M.L.1    Puig, K.L.2    Combs, C.K.3    Rosenberger, T.A.4
  • 9
    • 84874647437 scopus 로고    scopus 로고
    • Modulation of inflammatory cytokines and mitogen-activated protein kinases by acetate in primary astrocytes
    • 23233245 10.1007/s11481-012-9426-4
    • Soliman ML, Combs CK, Rosenberger TA (2013) Modulation of inflammatory cytokines and mitogen-activated protein kinases by acetate in primary astrocytes. J Neuroimmune Pharmacol 8:287-300
    • (2013) J Neuroimmune Pharmacol , vol.8 , pp. 287-300
    • Soliman, M.L.1    Combs, C.K.2    Rosenberger, T.A.3
  • 11
    • 1642534405 scopus 로고    scopus 로고
    • A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders
    • 14739001 10.1016/j.brainresrev.2003.10.002 1:CAS:528: DC%2BD2cXltVygtA%3D%3D
    • Phillis JW, O'Regan MH (2004) A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders. Brain Res Brain Res Rev 44:13-47
    • (2004) Brain Res Brain Res Rev , vol.44 , pp. 13-47
    • Phillis, J.W.1    O'Regan, M.H.2
  • 13
    • 0028338536 scopus 로고
    • 2
    • 8175726 1:CAS:528:DyaK2cXkt12lsrk%3D
    • 2. J Biol Chem 269:13057-13060
    • (1994) J Biol Chem , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 14
    • 0037201952 scopus 로고    scopus 로고
    • Expression and function of phospholipase A2 in brain
    • 12401195 10.1016/S0014-5793(02)03481-6 1:CAS:528:DC%2BD38XotVOjt7c%3D
    • Balboa MA, Varela-Nieto I, Killermann Lucas K, Dennis EA (2002) Expression and function of phospholipase A2 in brain. FEBS Lett 531:12-17
    • (2002) FEBS Lett , vol.531 , pp. 12-17
    • Balboa, M.A.1    Varela-Nieto, I.2    Killermann Lucas, K.3    Dennis, E.A.4
  • 15
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • 10966456 10.1146/annurev.biochem.69.1.145 1:CAS:528:DC%2BD3cXnt1ajtLg%3D
    • Smith WL, DeWitt DL, Garavito RM (2000) Cyclooxygenases: structural, cellular, and molecular biology. Annu Rev Biochem 69:145-182
    • (2000) Annu Rev Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    Dewitt, D.L.2    Garavito, R.M.3
  • 16
    • 77956393025 scopus 로고    scopus 로고
    • Phospholipases A2 and inflammatory responses in the central nervous system
    • 19855947 10.1007/s12017-009-8092-z 1:CAS:528:DC%2BC3cXmslSns7c%3D
    • Sun GY, Shelat PB, Jensen MB, He Y, Sun AY, Simonyi A (2010) Phospholipases A2 and inflammatory responses in the central nervous system. Neuromolecular Med 12:133-148
    • (2010) Neuromolecular Med , vol.12 , pp. 133-148
    • Sun, G.Y.1    Shelat, P.B.2    Jensen, M.B.3    He, Y.4    Sun, A.Y.5    Simonyi, A.6
  • 17
    • 0026558774 scopus 로고
    • Immunochemical detection of arachidonoyl-preferential phospholipase A2
    • 1607364 1:CAS:528:DyaK38XitlSnu7o%3D
    • Fujimori Y, Murakami M, Kim DK, Hara S, Takayama K, Kudo I, Inoue K (1992) Immunochemical detection of arachidonoyl-preferential phospholipase A2. J Biochem 111:54-60
    • (1992) J Biochem , vol.111 , pp. 54-60
    • Fujimori, Y.1    Murakami, M.2    Kim, D.K.3    Hara, S.4    Takayama, K.5    Kudo, I.6    Inoue, K.7
  • 18
    • 0028238064 scopus 로고
    • Expression of group II phospholipase A2 in rat brain after severe forebrain ischemia and in endotoxic shock
    • 7922587 10.1016/0006-8993(94)90719-6 1:CAS:528:DyaK2cXltlWnurs%3D
    • Lauritzen I, Heurteaux C, Lazdunski M (1994) Expression of group II phospholipase A2 in rat brain after severe forebrain ischemia and in endotoxic shock. Brain Res 651:353-356
    • (1994) Brain Res , vol.651 , pp. 353-356
    • Lauritzen, I.1    Heurteaux, C.2    Lazdunski, M.3
  • 19
    • 27244434601 scopus 로고    scopus 로고
    • Signaling and interplay mediated by phospholipases A2, C, and D in LA-N-1 cell nuclei
    • 16188211 10.1051/rnd:2005049 1:CAS:528:DC%2BD2MXht1CmurbE
    • Farooqui AA, Horrocks LA (2005) Signaling and interplay mediated by phospholipases A2, C, and D in LA-N-1 cell nuclei. Reprod Nutr Dev 45:613-631
    • (2005) Reprod Nutr Dev , vol.45 , pp. 613-631
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 20
    • 73549104499 scopus 로고    scopus 로고
    • Suppression of PLCbeta2 by endotoxin plays a role in the adenosine A(2A) receptor-mediated switch of macrophages from an inflammatory to an angiogenic phenotype
    • 19850892 10.2353/ajpath.2009.090290 1:CAS:528:DC%2BC3cXkt12mug%3D%3D
    • Grinberg S, Hasko G, Wu D, Leibovich SJ (2009) Suppression of PLCbeta2 by endotoxin plays a role in the adenosine A(2A) receptor-mediated switch of macrophages from an inflammatory to an angiogenic phenotype. Am J Pathol 175:2439-2453
    • (2009) Am J Pathol , vol.175 , pp. 2439-2453
    • Grinberg, S.1    Hasko, G.2    Wu, D.3    Leibovich, S.J.4
  • 21
    • 33846359049 scopus 로고    scopus 로고
    • Secretory phospholipase A2 IIA is up-regulated by TNF-alpha and IL-1alpha/beta after transient focal cerebral ischemia in rat
    • 17204250 10.1016/j.brainres.2006.11.080 1:CAS:528:DC%2BD2sXpvV2qsA%3D%3D
    • Adibhatla RM, Hatcher JF (2007) Secretory phospholipase A2 IIA is up-regulated by TNF-alpha and IL-1alpha/beta after transient focal cerebral ischemia in rat. Brain Res 1134:199-205
    • (2007) Brain Res , vol.1134 , pp. 199-205
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 22
    • 0032805694 scopus 로고    scopus 로고
    • Activation of arachidonate release and cytosolic phospholipase A2 via extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in macrophages stimulated by bacteria or zymosan
    • 10659994 10.1016/S0898-6568(99)00058-3 1:CAS:528:DyaK1MXotVOju7s%3D
    • Hiller G, Sundler R (1999) Activation of arachidonate release and cytosolic phospholipase A2 via extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in macrophages stimulated by bacteria or zymosan. Cell Signal 11:863-869
    • (1999) Cell Signal , vol.11 , pp. 863-869
    • Hiller, G.1    Sundler, R.2
  • 23
    • 0029911368 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase phosphorylates cytosolic phospholipase A2 (cPLA2) in thrombin-stimulated platelets. Evidence that proline-directed phosphorylation is not required for mobilization of arachidonic acid by cPLA2
    • 8910365 10.1074/jbc.271.37.22915 1:CAS:528:DyaK28XmvVWksL4%3D
    • Kramer RM, Roberts EF, Um SL, Borsch-Haubold AG, Watson SP, Fisher MJ, Jakubowski JA (1996) p38 mitogen-activated protein kinase phosphorylates cytosolic phospholipase A2 (cPLA2) in thrombin-stimulated platelets. Evidence that proline-directed phosphorylation is not required for mobilization of arachidonic acid by cPLA2. J Biol Chem 271:27723-27729
    • (1996) J Biol Chem , vol.271 , pp. 27723-27729
    • Kramer, R.M.1    Roberts, E.F.2    Um, S.L.3    Borsch-Haubold, A.G.4    Watson, S.P.5    Fisher, M.J.6    Jakubowski, J.A.7
  • 24
    • 30544442161 scopus 로고    scopus 로고
    • Histone acetylation increases chromatin accessibility
    • 16317046 10.1242/jcs.02689
    • Gorisch SM, Wachsmuth M, Toth KF, Lichter P, Rippe K (2005) Histone acetylation increases chromatin accessibility. J Cell Sci 118:5825-5834
    • (2005) J Cell Sci , vol.118 , pp. 5825-5834
    • Gorisch, S.M.1    Wachsmuth, M.2    Toth, K.F.3    Lichter, P.4    Rippe, K.5
  • 25
    • 0035815105 scopus 로고    scopus 로고
    • Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites
    • 11286549 10.1006/jmbi.2001.4528 1:CAS:528:DC%2BD3MXitlOisr8%3D
    • Anderson JD, Lowary PT, Widom J (2001) Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA target sites. J Mol Biol 307:977-985
    • (2001) J Mol Biol , vol.307 , pp. 977-985
    • Anderson, J.D.1    Lowary, P.T.2    Widom, J.3
  • 26
    • 0034724562 scopus 로고    scopus 로고
    • Effects of core histone tail domains on the equilibrium constants for dynamic DNA site accessibility in nucleosomes
    • 10764592 10.1006/jmbi.2000.3644 1:CAS:528:DC%2BD3cXitl2ru7w%3D
    • Polach KJ, Lowary PT, Widom J (2000) Effects of core histone tail domains on the equilibrium constants for dynamic DNA site accessibility in nucleosomes. J Mol Biol 298:211-223
    • (2000) J Mol Biol , vol.298 , pp. 211-223
    • Polach, K.J.1    Lowary, P.T.2    Widom, J.3
  • 27
    • 0032539694 scopus 로고    scopus 로고
    • Reconstitution of hyperacetylated, DNase I-sensitive chromatin characterized by high conformational flexibility of nucleosomal DNA
    • 9465051 10.1073/pnas.95.4.1540 1:CAS:528:DyaK1cXht1Wqt70%3D
    • Krajewski WA, Becker PB (1998) Reconstitution of hyperacetylated, DNase I-sensitive chromatin characterized by high conformational flexibility of nucleosomal DNA. Proc Natl Acad Sci U S A 95:1540-1545
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1540-1545
    • Krajewski, W.A.1    Becker, P.B.2
  • 28
    • 34547322880 scopus 로고    scopus 로고
    • The modification and variants of histone
    • 10.1134/S0026893307030028
    • Mu C, Liu H, Zheng GC (2007) The modification and variants of histone. Mol Biol (Mosk) 41:395-407
    • (2007) Mol Biol (Mosk) , vol.41 , pp. 395-407
    • Mu, C.1    Liu, H.2    Zheng, G.C.3
  • 29
    • 0036211013 scopus 로고    scopus 로고
    • Histone acetylation: A switch between repressive and permissive chromatin. Second in review series on chromatin dynamics
    • 11882541 10.1093/embo-reports/kvf053 1:CAS:528:DC%2BD38XitlCmtrk%3D
    • Eberharter A, Becker PB (2002) Histone acetylation: a switch between repressive and permissive chromatin. Second in review series on chromatin dynamics. EMBO Rep 3:224-229
    • (2002) EMBO Rep , vol.3 , pp. 224-229
    • Eberharter, A.1    Becker, P.B.2
  • 30
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • 16289629 10.1016/j.gene.2005.09.010 1:CAS:528:DC%2BD2MXht1Klu7%2FN
    • Glozak MA, Sengupta N, Zhang X, Seto E (2005) Acetylation and deacetylation of non-histone proteins. Gene 363:15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 31
    • 0036261826 scopus 로고    scopus 로고
    • The diversity of acetylated proteins
    • 10.1186/gb-2002-3-5-reviews0006
    • Polevoda B, Sherman F (2002) The diversity of acetylated proteins. Genome Biol 3:6.1-6.6
    • (2002) Genome Biol , vol.3 , pp. 61-66
    • Polevoda, B.1    Sherman, F.2
  • 32
    • 34248530339 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: Multiple mechanisms of action
    • 17371805 10.1124/jpet.107.120188 1:CAS:528:DC%2BD2sXmsFeru7o%3D
    • Kim HJ, Rowe M, Ren M, Hong JS, Chen PS, Chuang DM (2007) Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: multiple mechanisms of action. J Pharmacol Exp Ther 321:892-901
    • (2007) J Pharmacol Exp Ther , vol.321 , pp. 892-901
    • Kim, H.J.1    Rowe, M.2    Ren, M.3    Hong, J.S.4    Chen, P.S.5    Chuang, D.M.6
  • 33
    • 34250612194 scopus 로고    scopus 로고
    • Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model
    • 17522299 10.1523/JNEUROSCI.1139-07.2007 1:CAS:528:DC%2BD2sXmsVWnsro%3D
    • Rouaux C, Panteleeva I, Rene F, Gonzalez de Aguilar JL, Echaniz-Laguna A, Dupuis L, Menger Y, Boutillier AL, Loeffler JP (2007) Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model. J Neurosci 27:5535-5545
    • (2007) J Neurosci , vol.27 , pp. 5535-5545
    • Rouaux, C.1    Panteleeva, I.2    Rene, F.3    Gonzalez De Aguilar, J.L.4    Echaniz-Laguna, A.5    Dupuis, L.6    Menger, Y.7    Boutillier, A.L.8    Loeffler, J.P.9
  • 34
    • 48849095167 scopus 로고    scopus 로고
    • HDAC inhibitor increases histone H3 acetylation and reduces microglia inflammatory response following traumatic brain injury in rats
    • 18582446 10.1016/j.brainres.2008.05.085 1:CAS:528:DC%2BD1cXpvFGmtr0%3D
    • Zhang B, West EJ, Van KC, Gurkoff GG, Zhou J, Zhang XM, Kozikowski AP, Lyeth BG (2008) HDAC inhibitor increases histone H3 acetylation and reduces microglia inflammatory response following traumatic brain injury in rats. Brain Res 1226:181-191
    • (2008) Brain Res , vol.1226 , pp. 181-191
    • Zhang, B.1    West, E.J.2    Van, K.C.3    Gurkoff, G.G.4    Zhou, J.5    Zhang, X.M.6    Kozikowski, A.P.7    Lyeth, B.G.8
  • 38
    • 20844438031 scopus 로고    scopus 로고
    • Remodeling chromatin and stress resistance in the central nervous system: Histone deacetylase inhibitors as novel and broadly effective neuroprotective agents
    • 15723612 10.2174/1568007053005091 1:CAS:528:DC%2BD2MXhsVKmsbk%3D
    • Langley B, Gensert JM, Beal MF, Ratan RR (2005) Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents. Curr Drug Targets CNS Neurol Disord 4:41-50
    • (2005) Curr Drug Targets CNS Neurol Disord , vol.4 , pp. 41-50
    • Langley, B.1    Gensert, J.M.2    Beal, M.F.3    Ratan, R.R.4
  • 39
    • 13544265432 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: New drugs for the treatment of inflammatory diseases?
    • 15708534 10.1016/S1359-6446(04)03309-4 1:CAS:528:DC%2BD2MXhtlajsbY%3D
    • Blanchard F, Chipoy C (2005) Histone deacetylase inhibitors: new drugs for the treatment of inflammatory diseases? Drug Discov Today 10:197-204
    • (2005) Drug Discov Today , vol.10 , pp. 197-204
    • Blanchard, F.1    Chipoy, C.2
  • 40
    • 34047218122 scopus 로고    scopus 로고
    • HDAC inhibitors as anti-inflammatory agents
    • 17325655 10.1038/sj.bjp.0707166 1:CAS:528:DC%2BD2sXjs12ntL8%3D
    • Adcock IM (2007) HDAC inhibitors as anti-inflammatory agents. Br J Pharmacol 150:829-831
    • (2007) Br J Pharmacol , vol.150 , pp. 829-831
    • Adcock, I.M.1
  • 41
    • 84864389497 scopus 로고    scopus 로고
    • Amyloid-beta oligomers stimulate microglia through a tyrosine kinase dependent mechanism
    • 22133278 10.1016/j.neurobiolaging.2011.10.027 1:CAS:528: DC%2BC38XhtFeiur%2FL
    • Dhawan G, Floden AM, Combs CK (2012) Amyloid-beta oligomers stimulate microglia through a tyrosine kinase dependent mechanism. Neurobiol Aging 33:2247-2261
    • (2012) Neurobiol Aging , vol.33 , pp. 2247-2261
    • Dhawan, G.1    Floden, A.M.2    Combs, C.K.3
  • 42
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • 10638745 10.1038/47412 1:STN:280:DC%2BD3c7gt1arsQ%3D%3D
    • Strahl BD, Allis CD (2000) The language of covalent histone modifications. Nature 403:41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 43
    • 0035370439 scopus 로고    scopus 로고
    • Histone methylation versus histone acetylation: New insights into epigenetic regulation
    • 11343896 10.1016/S0955-0674(00)00208-8 1:CAS:528:DC%2BD3MXktVajurY%3D
    • Rice JC, Allis CD (2001) Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr Opin Cell Biol 13:263-273
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 263-273
    • Rice, J.C.1    Allis, C.D.2
  • 44
    • 36849052929 scopus 로고    scopus 로고
    • Prostaglandins are necessary and sufficient to induce contextual fear learning impairments after interleukin-1bata injections into the dorsal hippocampus
    • 18035502 10.1016/j.neuroscience.2007.10.003 1:CAS:528:DC%2BD2sXhsVCgs7fE
    • Hein AM, Stutzman DL, Bland ST, Barrientos RM, Watkins LR, Rudy JW, Maier SF (2007) Prostaglandins are necessary and sufficient to induce contextual fear learning impairments after interleukin-1bata injections into the dorsal hippocampus. Neuroscience 150:754-763
    • (2007) Neuroscience , vol.150 , pp. 754-763
    • Hein, A.M.1    Stutzman, D.L.2    Bland, S.T.3    Barrientos, R.M.4    Watkins, L.R.5    Rudy, J.W.6    Maier, S.F.7
  • 45
    • 24644511102 scopus 로고    scopus 로고
    • Phospholipase A2 in astrocytes: Responses to oxidative stress, inflammation, and G protein-coupled receptor agonists
    • 15953810 10.1385/MN:31:1-3:027 1:CAS:528:DC%2BD2MXmtFKltLc%3D
    • Sun GY, Xu J, Jensen MD, Yu S, Wood WG, Gonzalez FA, Simonyi A, Sun AY, Weisman GA (2005) Phospholipase A2 in astrocytes: responses to oxidative stress, inflammation, and G protein-coupled receptor agonists. Mol Neurobiol 31:27-41
    • (2005) Mol Neurobiol , vol.31 , pp. 27-41
    • Sun, G.Y.1    Xu, J.2    Jensen, M.D.3    Yu, S.4    Wood, W.G.5    Gonzalez, F.A.6    Simonyi, A.7    Sun, A.Y.8    Weisman, G.A.9
  • 46
    • 0344505863 scopus 로고    scopus 로고
    • Cyclooxygenase 2 mRNA expression in rat brain after peripheral injection of lipopolysaccharide
    • 9748570 10.1016/S0006-8993(98)00402-8 1:CAS:528:DyaK1cXkvFOmsL8%3D
    • Quan N, Whiteside M, Herkenham M (1998) Cyclooxygenase 2 mRNA expression in rat brain after peripheral injection of lipopolysaccharide. Brain Res 802:189-197
    • (1998) Brain Res , vol.802 , pp. 189-197
    • Quan, N.1    Whiteside, M.2    Herkenham, M.3
  • 47
    • 0033694033 scopus 로고    scopus 로고
    • Cyclooxygenases in the central nervous system: Implications for treatment of neurological disorders
    • 11203433 10.2174/1381612003398672 1:CAS:528:DC%2BD3cXosVGlt7k%3D
    • Yermakova A, O'Banion MK (2000) Cyclooxygenases in the central nervous system: implications for treatment of neurological disorders. Curr Pharm Des 6:1755-1776
    • (2000) Curr Pharm des , vol.6 , pp. 1755-1776
    • Yermakova, A.1    O'Banion, M.K.2
  • 49
    • 69849092027 scopus 로고    scopus 로고
    • Neuroinflammation and memory: The role of prostaglandins
    • 19365736 10.1007/s12035-009-8066-z 1:CAS:528:DC%2BD1MXnsVyiu7g%3D
    • Hein AM, O'Banion MK (2009) Neuroinflammation and memory: the role of prostaglandins. Mol Neurobiol 40:15-32
    • (2009) Mol Neurobiol , vol.40 , pp. 15-32
    • Hein, A.M.1    O'Banion, M.K.2
  • 50
    • 0036569812 scopus 로고    scopus 로고
    • Inhibition of COX-2 reduces the age-dependent increase of hippocampal inflammatory markers, corticosterone secretion, and behavioral impairments in the rat
    • 12111864 10.1002/jnr.10192 1:CAS:528:DC%2BD38XjslSis74%3D
    • Casolini P, Catalani A, Zuena AR, Angelucci L (2002) Inhibition of COX-2 reduces the age-dependent increase of hippocampal inflammatory markers, corticosterone secretion, and behavioral impairments in the rat. J Neurosci Res 68:337-343
    • (2002) J Neurosci Res , vol.68 , pp. 337-343
    • Casolini, P.1    Catalani, A.2    Zuena, A.R.3    Angelucci, L.4
  • 53
    • 0035970036 scopus 로고    scopus 로고
    • Reduced susceptibility to ischemic brain injury and N-methyl-D-aspartate- mediated neurotoxicity in cyclooxygenase-2-deficient mice
    • 11158633 10.1073/pnas.98.3.1294 1:CAS:528:DC%2BD3MXht1SmtLc%3D
    • Iadecola C, Niwa K, Nogawa S, Zhao X, Nagayama M, Araki E, Morham S, Ross ME (2001) Reduced susceptibility to ischemic brain injury and N-methyl-D-aspartate-mediated neurotoxicity in cyclooxygenase-2-deficient mice. Proc Natl Acad Sci U S A 98:1294-1299
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1294-1299
    • Iadecola, C.1    Niwa, K.2    Nogawa, S.3    Zhao, X.4    Nagayama, M.5    Araki, E.6    Morham, S.7    Ross, M.E.8
  • 54
    • 0942287666 scopus 로고    scopus 로고
    • Additive neuroprotective effects of creatine and cyclooxygenase 2 inhibitors in a transgenic mouse model of amyotrophic lateral sclerosis
    • 14720207 10.1046/j.1471-4159.2003.02160.x 1:CAS:528:DC%2BD2cXhtVaisb4%3D
    • Klivenyi P, Kiaei M, Gardian G, Calingasan NY, Beal MF (2004) Additive neuroprotective effects of creatine and cyclooxygenase 2 inhibitors in a transgenic mouse model of amyotrophic lateral sclerosis. J Neurochem 88:576-582
    • (2004) J Neurochem , vol.88 , pp. 576-582
    • Klivenyi, P.1    Kiaei, M.2    Gardian, G.3    Calingasan, N.Y.4    Beal, M.F.5
  • 56
    • 80051984937 scopus 로고    scopus 로고
    • Sodium butyrate improves memory function in an Alzheimer's disease mouse model when administered at an advanced stage of disease progression
    • 21593570 1:CAS:528:DC%2BC3MXhtFWltbbF
    • Govindarajan N, Agis-Balboa RC, Walter J, Sananbenesi F, Fischer A (2011) Sodium butyrate improves memory function in an Alzheimer's disease mouse model when administered at an advanced stage of disease progression. J Alzheimers Dis 26:187-197
    • (2011) J Alzheimers Dis , vol.26 , pp. 187-197
    • Govindarajan, N.1    Agis-Balboa, R.C.2    Walter, J.3    Sananbenesi, F.4    Fischer, A.5
  • 57
    • 0035839557 scopus 로고    scopus 로고
    • Functional coupling between secretory and cytosolic phospholipase A2 modulates tumor necrosis factor-alpha- and interleukin-1beta-induced NF-kappa B activation
    • 11390371 10.1074/jbc.M008481200 1:CAS:528:DC%2BD3MXmtFehurk%3D
    • Anthonsen MW, Solhaug A, Johansen B (2001) Functional coupling between secretory and cytosolic phospholipase A2 modulates tumor necrosis factor-alpha- and interleukin-1beta-induced NF-kappa B activation. J Biol Chem 276:30527-30536
    • (2001) J Biol Chem , vol.276 , pp. 30527-30536
    • Anthonsen, M.W.1    Solhaug, A.2    Johansen, B.3
  • 58
    • 0041829104 scopus 로고    scopus 로고
    • Distinct regulation of cytosolic phospholipase A2 phosphorylation, translocation, proteolysis and activation by tumour necrosis factor-receptor subtypes
    • 12786601 10.1042/BJ20030705 1:CAS:528:DC%2BD3sXms1GksLs%3D
    • Jupp OJ, Vandenabeele P, MacEwan DJ (2003) Distinct regulation of cytosolic phospholipase A2 phosphorylation, translocation, proteolysis and activation by tumour necrosis factor-receptor subtypes. Biochem J 374:453-461
    • (2003) Biochem J , vol.374 , pp. 453-461
    • Jupp, O.J.1    Vandenabeele, P.2    Macewan, D.J.3
  • 59
    • 0038813706 scopus 로고    scopus 로고
    • Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation
    • 12471036 10.1074/jbc.M209286200 1:CAS:528:DC%2BD3sXhtVKls7s%3D
    • Deng WG, Zhu Y, Wu KK (2003) Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation. J Biol Chem 278:4770-4777
    • (2003) J Biol Chem , vol.278 , pp. 4770-4777
    • Deng, W.G.1    Zhu, Y.2    Wu, K.K.3


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