메뉴 건너뛰기




Volumn 41, Issue 6, 2006, Pages 960-972

Cyclooxygenase-2-dependent neuronal death proceeds via superoxide anion generation

Author keywords

COX 2; MnTBAP; Neuronal death; NS398; SOD; Superoxide

Indexed keywords

5 (4 CHLOROPHENYL) 1 (4 METHOXYPHENYL) 3 TRIFLUOROMETHYL 1H PYRAZOLE; ALLOPURINOL; ASCORBIC ACID; CYCLOOXYGENASE 1 INHIBITOR; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; ENZYME INHIBITOR; GLUTATHIONE; HYDROGEN PEROXIDE; IRON COMPLEX; LIPOPOLYSACCHARIDE; MANGANESE TETRAKIS(4 BENZOIC ACID)PORPHYRIN; MONOAMINE OXIDASE INHIBITOR; N (2 CYCLOHEXYLOXY 4 NITROPHENYL)METHANESULFONAMIDE; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE SYNTHASE INHIBITOR; NITROPRUSSIDE SODIUM; PARGYLINE; PORPHYRIN DERIVATIVE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE INHIBITOR; SUPEROXIDE; TROLOX C; UNCLASSIFIED DRUG; ZINC;

EID: 33747348720     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.06.001     Document Type: Article
Times cited : (83)

References (61)
  • 1
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59 (1992) 1609-1623
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 2
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies H. Strategies of antioxidant defense. Eur. J. Biochem. 215 (1993) 213-219
    • (1993) Eur. J. Biochem. , vol.215 , pp. 213-219
    • Sies, H.1
  • 3
    • 0033789565 scopus 로고    scopus 로고
    • Free radical pathways in CNS injury
    • Lewen A., Matz P., and Chan P.H. Free radical pathways in CNS injury. J. Neurotrauma 17 (2000) 871-890
    • (2000) J. Neurotrauma , vol.17 , pp. 871-890
    • Lewen, A.1    Matz, P.2    Chan, P.H.3
  • 4
    • 0033551847 scopus 로고    scopus 로고
    • Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition
    • Marnett L.J., Rowlinson S.W., Goodwin D.C., Kalgutkar A.S., and Lanzo C.A. Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition. J. Biol. Chem. 274 (1999) 22903-22906
    • (1999) J. Biol. Chem. , vol.274 , pp. 22903-22906
    • Marnett, L.J.1    Rowlinson, S.W.2    Goodwin, D.C.3    Kalgutkar, A.S.4    Lanzo, C.A.5
  • 5
    • 0035149749 scopus 로고    scopus 로고
    • Reactive oxygen radicals in signaling and damage in the ischemic brain
    • Chan P.H. Reactive oxygen radicals in signaling and damage in the ischemic brain. J. Cereb. Blood Flow Metab. 21 (2001) 2-14
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 2-14
    • Chan, P.H.1
  • 6
    • 0035970509 scopus 로고    scopus 로고
    • Cyclooxygenase-1 participates in selected vasodilator responses of the cerebral circulation
    • Niwa K., Haensel S., Ross M.E., and Iadecola C. Cyclooxygenase-1 participates in selected vasodilator responses of the cerebral circulation. Circ. Res. 88 (2001) 600-608
    • (2001) Circ. Res. , vol.88 , pp. 600-608
    • Niwa, K.1    Haensel, S.2    Ross, M.E.3    Iadecola, C.4
  • 7
    • 0034799564 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibitor ns-398 protects neuronal cultures from lipopolysaccharide-induced neurotoxicity
    • Araki E., Forster C., Dubinsky J.M., Ross M.E., and Iadecola C. Cyclooxygenase-2 inhibitor ns-398 protects neuronal cultures from lipopolysaccharide-induced neurotoxicity. Stroke 32 (2001) 2370-2375
    • (2001) Stroke , vol.32 , pp. 2370-2375
    • Araki, E.1    Forster, C.2    Dubinsky, J.M.3    Ross, M.E.4    Iadecola, C.5
  • 9
    • 14944352071 scopus 로고    scopus 로고
    • Inflammation and the degenerative diseases of aging
    • McGeer P.L., and McGeer E.F. Inflammation and the degenerative diseases of aging. Ann. N.Y. Acad. Sci. 1035 (2004) 104-116
    • (2004) Ann. N.Y. Acad. Sci. , vol.1035 , pp. 104-116
    • McGeer, P.L.1    McGeer, E.F.2
  • 11
    • 0031957090 scopus 로고    scopus 로고
    • Cyanide-induced generation of oxidative species: involvement of nitric oxide synthase and cyclooxygenase-2
    • Gunasekar P.G., Borowitz J.L., and Isom G.E. Cyanide-induced generation of oxidative species: involvement of nitric oxide synthase and cyclooxygenase-2. J. Pharmacol. Exp. Ther. 285 (1998) 236-241
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 236-241
    • Gunasekar, P.G.1    Borowitz, J.L.2    Isom, G.E.3
  • 12
    • 0036447440 scopus 로고    scopus 로고
    • Oxidative stress and cyclooxygenase-2 induction mediate cyanide-induced apoptosis of cortical cells
    • Li L., Prabhakaran K., Shou Y., Borowitz J.L., and Isom G.E. Oxidative stress and cyclooxygenase-2 induction mediate cyanide-induced apoptosis of cortical cells. Toxicol. Appl. Pharmacol. 185 (2002) 55-63
    • (2002) Toxicol. Appl. Pharmacol. , vol.185 , pp. 55-63
    • Li, L.1    Prabhakaran, K.2    Shou, Y.3    Borowitz, J.L.4    Isom, G.E.5
  • 13
    • 0141739581 scopus 로고    scopus 로고
    • Delayed treatment with nimesulide reduces measures of oxidative stress following global ischemic brain injury in gerbils
    • Candelario-Jalil E., Alvarez D., Merino N., and Leon O.S. Delayed treatment with nimesulide reduces measures of oxidative stress following global ischemic brain injury in gerbils. Neurosci. Res. 47 (2003) 245-253
    • (2003) Neurosci. Res. , vol.47 , pp. 245-253
    • Candelario-Jalil, E.1    Alvarez, D.2    Merino, N.3    Leon, O.S.4
  • 14
    • 0036319108 scopus 로고    scopus 로고
    • In vivo activation of N-methyl-D-aspartate receptors in the rat hippocampus increases prostaglandin E(2) extracellular levels and triggers lipid peroxidation through cyclooxygenase-mediated mechanisms
    • Pepicelli O., Fedele E., Bonanno G., Raiteri M., Ajmone-Cat M.A., Greco A., Levi G., and Minghetti L. In vivo activation of N-methyl-D-aspartate receptors in the rat hippocampus increases prostaglandin E(2) extracellular levels and triggers lipid peroxidation through cyclooxygenase-mediated mechanisms. J. Neurochem. 81 (2002) 1028-1034
    • (2002) J. Neurochem. , vol.81 , pp. 1028-1034
    • Pepicelli, O.1    Fedele, E.2    Bonanno, G.3    Raiteri, M.4    Ajmone-Cat, M.A.5    Greco, A.6    Levi, G.7    Minghetti, L.8
  • 16
    • 0029927787 scopus 로고    scopus 로고
    • Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice
    • Dawson V.L., Kizushi V.M., Huang P.L., Snyder S.H., and Dawson T.M. Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice. J. Neurosci. 16 (1996) 2479-2487
    • (1996) J. Neurosci. , vol.16 , pp. 2479-2487
    • Dawson, V.L.1    Kizushi, V.M.2    Huang, P.L.3    Snyder, S.H.4    Dawson, T.M.5
  • 17
    • 0032902146 scopus 로고    scopus 로고
    • Prostaglandin E receptor subtypes in cultured rat microglia and their role in reducing lipopolysaccharide-induced interleukin-1beta production
    • Caggiano A.O., and Kraig R.P. Prostaglandin E receptor subtypes in cultured rat microglia and their role in reducing lipopolysaccharide-induced interleukin-1beta production. J. Neurochem. 72 (1999) 565-575
    • (1999) J. Neurochem. , vol.72 , pp. 565-575
    • Caggiano, A.O.1    Kraig, R.P.2
  • 18
    • 0035449358 scopus 로고    scopus 로고
    • Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity
    • Bal-Price A., and Brown G.C. Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity. J. Neurosci. 21 (2001) 6480-6491
    • (2001) J. Neurosci. , vol.21 , pp. 6480-6491
    • Bal-Price, A.1    Brown, G.C.2
  • 19
    • 0037150792 scopus 로고    scopus 로고
    • Effects of peroxisome proliferator-activated receptor agonists on LPS-induced neuronal death in mixed cortical neurons: associated with iNOS and COX-2
    • Kim E.J., Kwon K.J., Park J.Y., Lee S.H., Moon C.H., and Baik E.J. Effects of peroxisome proliferator-activated receptor agonists on LPS-induced neuronal death in mixed cortical neurons: associated with iNOS and COX-2. Brain Res. 941 (2002) 1-10
    • (2002) Brain Res. , vol.941 , pp. 1-10
    • Kim, E.J.1    Kwon, K.J.2    Park, J.Y.3    Lee, S.H.4    Moon, C.H.5    Baik, E.J.6
  • 20
    • 22244470745 scopus 로고    scopus 로고
    • Peroxynitrite generated by inducible nitric oxide synthase and NADPH oxidase mediates microglial toxicity to oligodendrocytes
    • Li J., Baud O., Vartanian T., Volpe J.J., and Rosenberg P.A. Peroxynitrite generated by inducible nitric oxide synthase and NADPH oxidase mediates microglial toxicity to oligodendrocytes. Proc. Natl. Acad. Sci. USA 102 (2005) 9936-9941
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9936-9941
    • Li, J.1    Baud, O.2    Vartanian, T.3    Volpe, J.J.4    Rosenberg, P.A.5
  • 21
    • 0345724974 scopus 로고    scopus 로고
    • Protective effects of extracellular glutathione against Zn2+-induced cell death in vitro and in vivo
    • Cho I.K., Im J.Y., Kim D., Kim K.S., Lee J.K., and Han P.L. Protective effects of extracellular glutathione against Zn2+-induced cell death in vitro and in vivo. J. Neurosci. Res. 74 (2003) 736-743
    • (2003) J. Neurosci. Res. , vol.74 , pp. 736-743
    • Cho, I.K.1    Im, J.Y.2    Kim, D.3    Kim, K.S.4    Lee, J.K.5    Han, P.L.6
  • 23
    • 4944244055 scopus 로고    scopus 로고
    • COX-2 Regulates the insulin-like growth factor I-induced potentiation of Zn(2+)-toxicity in primary cortical culture
    • Im J.Y., Kim D., Lee K.W., Kim J.B., Lee J.K., Kim D.S., Lee Y.I., Ha K.S., Joe C.O., and Han P.L. COX-2 Regulates the insulin-like growth factor I-induced potentiation of Zn(2+)-toxicity in primary cortical culture. Mol. Pharmacol. 66 (2004) 368-376
    • (2004) Mol. Pharmacol. , vol.66 , pp. 368-376
    • Im, J.Y.1    Kim, D.2    Lee, K.W.3    Kim, J.B.4    Lee, J.K.5    Kim, D.S.6    Lee, Y.I.7    Ha, K.S.8    Joe, C.O.9    Han, P.L.10
  • 24
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine
    • Bindokas V.P., Jordan J., Lee C.C., and Miller R.J. Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine. J. Neurosci. 16 (1996) 1324-1336
    • (1996) J. Neurosci. , vol.16 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 25
    • 0038368985 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide
    • Zhao H., Kalivendi S., Zhang H., Joseph J., Nithipatikom K., Vasquez-Vivar J., and Kalyanaraman B. Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide. Free Radic. Biol. Med. 34 (2003) 1359-1368
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 27
    • 0344559100 scopus 로고    scopus 로고
    • Extracellular and intracellular glutathione protects astrocytes from Zn2+-induced cell death
    • Kim D., Joe C.O., and Han P.L. Extracellular and intracellular glutathione protects astrocytes from Zn2+-induced cell death. Neuroreport 14 (2003) 187-190
    • (2003) Neuroreport , vol.14 , pp. 187-190
    • Kim, D.1    Joe, C.O.2    Han, P.L.3
  • 30
    • 0027351360 scopus 로고
    • The neurotoxicity of iron and nitric oxide. Relevance to the etiology of Parkinson's disease
    • Youdim M.B., Ben-Shachar D., Eshel G., Finberg J.P., and Riederer P. The neurotoxicity of iron and nitric oxide. Relevance to the etiology of Parkinson's disease. Adv. Neurol. 60 (1993) 259-266
    • (1993) Adv. Neurol. , vol.60 , pp. 259-266
    • Youdim, M.B.1    Ben-Shachar, D.2    Eshel, G.3    Finberg, J.P.4    Riederer, P.5
  • 31
    • 0032619789 scopus 로고    scopus 로고
    • The mechanism of "Fenton-like" reactions and their importance for biological systems. A biologist's view
    • Liochev S.I. The mechanism of "Fenton-like" reactions and their importance for biological systems. A biologist's view. Met. Ions. Biol. Syst. 36 (1999) 1-39
    • (1999) Met. Ions. Biol. Syst. , vol.36 , pp. 1-39
    • Liochev, S.I.1
  • 32
    • 0034648298 scopus 로고    scopus 로고
    • The Haber-Weiss reaction and mechanisms of toxicity
    • Kehrer J.P. The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 149 (2000) 43-50
    • (2000) Toxicology , vol.149 , pp. 43-50
    • Kehrer, J.P.1
  • 33
    • 0022884922 scopus 로고
    • PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH
    • Kukreja R.C., Kontos H.A., Hess M.L., and Ellis E.F. PGH synthase and lipoxygenase generate superoxide in the presence of NADH or NADPH. Circ. Res. 59 (1986) 612-619
    • (1986) Circ. Res. , vol.59 , pp. 612-619
    • Kukreja, R.C.1    Kontos, H.A.2    Hess, M.L.3    Ellis, E.F.4
  • 34
    • 0030479496 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2
    • Smith W.L., Garavito R.M., and DeWitt D.L. Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J. Biol. Chem. 271 (1996) 33157-33160
    • (1996) J. Biol. Chem. , vol.271 , pp. 33157-33160
    • Smith, W.L.1    Garavito, R.M.2    DeWitt, D.L.3
  • 35
    • 0032190264 scopus 로고    scopus 로고
    • Cyclooxygenase and inflammation in Alzheimer's disease: experimental approaches and clinical interventions
    • Pasinetti G.M. Cyclooxygenase and inflammation in Alzheimer's disease: experimental approaches and clinical interventions. J. Neurosci. Res. 54 (1998) 1-6
    • (1998) J. Neurosci. Res. , vol.54 , pp. 1-6
    • Pasinetti, G.M.1
  • 36
  • 37
    • 4444333049 scopus 로고    scopus 로고
    • Cyclooxygenase-2 (COX-2) in inflammatory and degenerative brain diseases
    • Minghetti L. Cyclooxygenase-2 (COX-2) in inflammatory and degenerative brain diseases. J. Neuropathol. Exp. Neurol. 63 (2004) 901-910
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 901-910
    • Minghetti, L.1
  • 38
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: structural, cellular, and molecular biology
    • Smith W.L., DeWitt D.L., and Garavito R.M. Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69 (2000) 145-182
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 40
    • 0030909616 scopus 로고    scopus 로고
    • Cyclo-oxygenase-2 gene expression in neurons contributes to ischemic brain damage
    • Nogawa S., Zhang F., Ross M.E., and Iadecola C. Cyclo-oxygenase-2 gene expression in neurons contributes to ischemic brain damage. J. Neurosci. 17 (1997) 2746-2755
    • (1997) J. Neurosci. , vol.17 , pp. 2746-2755
    • Nogawa, S.1    Zhang, F.2    Ross, M.E.3    Iadecola, C.4
  • 42
    • 0032167857 scopus 로고    scopus 로고
    • Interaction between inducible nitric oxide synthase and cyclooxygenase-2 after cerebral ischemia
    • Nogawa S., Forster C., Zhang F., Nagayama M., Ross M.E., and Iadecola C. Interaction between inducible nitric oxide synthase and cyclooxygenase-2 after cerebral ischemia. Proc. Natl. Acad. Sci. USA 95 (1998) 10966-10971
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10966-10971
    • Nogawa, S.1    Forster, C.2    Zhang, F.3    Nagayama, M.4    Ross, M.E.5    Iadecola, C.6
  • 44
    • 20744433041 scopus 로고    scopus 로고
    • Cyclo-oxygenase-1 and -2 differently contribute to prostaglandin E2 synthesis and lipid peroxidation after in vivo activation of N-methyl-D-aspartate receptors in rat hippocampus
    • Pepicelli O., Fedele E., Berardi M., Raiteri M., Levi G., Greco A., Ajmone-Cat M.A., and Minghetti L. Cyclo-oxygenase-1 and -2 differently contribute to prostaglandin E2 synthesis and lipid peroxidation after in vivo activation of N-methyl-D-aspartate receptors in rat hippocampus. J. Neurochem. 93 (2005) 1561-1567
    • (2005) J. Neurochem. , vol.93 , pp. 1561-1567
    • Pepicelli, O.1    Fedele, E.2    Berardi, M.3    Raiteri, M.4    Levi, G.5    Greco, A.6    Ajmone-Cat, M.A.7    Minghetti, L.8
  • 45
    • 0027505884 scopus 로고
    • Hydroxyl radical production and lipid peroxidation parallels selective post-ischemic vulnerability in gerbil brain
    • Hall E.D., Andrus P.K., Althaus J.S., and VonVoigtlander P.F. Hydroxyl radical production and lipid peroxidation parallels selective post-ischemic vulnerability in gerbil brain. J. Neurosci. Res. 34 (1993) 107-112
    • (1993) J. Neurosci. Res. , vol.34 , pp. 107-112
    • Hall, E.D.1    Andrus, P.K.2    Althaus, J.S.3    VonVoigtlander, P.F.4
  • 48
    • 0035839229 scopus 로고    scopus 로고
    • Vasopressin induced cyclooxygenase dependent superoxidegeneration contributes to K(+) channel function impairment after brain injury
    • Armstead W.M. Vasopressin induced cyclooxygenase dependent superoxidegeneration contributes to K(+) channel function impairment after brain injury. Brain Res. 910 (2001) 19-28
    • (2001) Brain Res. , vol.910 , pp. 19-28
    • Armstead, W.M.1
  • 49
    • 0036673683 scopus 로고    scopus 로고
    • Relationship between NOC/oFQ, dynorphin, and COX-2 activation in impaired NMDA cerebrovasodilation after brain injury
    • Kulkarni M., and Armstead W.M. Relationship between NOC/oFQ, dynorphin, and COX-2 activation in impaired NMDA cerebrovasodilation after brain injury. J. Neurotrauma 19 (2002) 965-973
    • (2002) J. Neurotrauma , vol.19 , pp. 965-973
    • Kulkarni, M.1    Armstead, W.M.2
  • 51
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith M.A., Harris P.L., Sayre L.M., and Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. USA 94 (1997) 9866-9868
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 52
    • 0027303808 scopus 로고
    • Stimlated decay of O2-* caused by ferritin-bound copper
    • Bolann B.J., and Ulvik R.J. Stimlated decay of O2-* caused by ferritin-bound copper. FEBS Lett. 328 (1993) 263-267
    • (1993) FEBS Lett. , vol.328 , pp. 263-267
    • Bolann, B.J.1    Ulvik, R.J.2
  • 53
    • 0024461666 scopus 로고
    • Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release
    • Prasad M.R., Engelman R.M., Jones R.M., and Das D.K. Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release. Biochem. J. 263 (1989) 731-736
    • (1989) Biochem. J. , vol.263 , pp. 731-736
    • Prasad, M.R.1    Engelman, R.M.2    Jones, R.M.3    Das, D.K.4
  • 54
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • Nagababu E., and Rifkind J.M. Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem. Biophys. Res. Commun. 247 (1998) 592-596
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 56
    • 0035952497 scopus 로고    scopus 로고
    • 15-deoxy-delta12,14-prostaglandin J2, a specific ligand for peroxisome proliferator-activated receptor-gamma, induces neuronal apoptosis
    • Rohn T.T., Wong S.M., Cotman C.W., and Cribbs D.H. 15-deoxy-delta12,14-prostaglandin J2, a specific ligand for peroxisome proliferator-activated receptor-gamma, induces neuronal apoptosis. Neuroreport 12 (2001) 839-843
    • (2001) Neuroreport , vol.12 , pp. 839-843
    • Rohn, T.T.1    Wong, S.M.2    Cotman, C.W.3    Cribbs, D.H.4
  • 57
    • 0037059399 scopus 로고    scopus 로고
    • Prostaglandin E(2) induces caspase-dependent apoptosis in rat cortical cells
    • Takadera T., Yumoto H., Tozuka Y., and Ohyashiki T. Prostaglandin E(2) induces caspase-dependent apoptosis in rat cortical cells. Neurosci. Lett. 317 (2002) 61-64
    • (2002) Neurosci. Lett. , vol.317 , pp. 61-64
    • Takadera, T.1    Yumoto, H.2    Tozuka, Y.3    Ohyashiki, T.4
  • 59
    • 0141504202 scopus 로고    scopus 로고
    • N-Acetylcysteine protects mice from lethal endotoxemia by regulating the redox state of immune cells
    • Victor V.M., Rocha M., and De la Fuente M. N-Acetylcysteine protects mice from lethal endotoxemia by regulating the redox state of immune cells. Free Radic. Res. 37 (2003) 919-929
    • (2003) Free Radic. Res. , vol.37 , pp. 919-929
    • Victor, V.M.1    Rocha, M.2    De la Fuente, M.3
  • 60
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola C. Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat. Rev. Neurosci. 5 (2004) 347-360
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 347-360
    • Iadecola, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.