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Volumn 35, Issue 2, 2014, Pages 421-430

Uncoupling protein 2 deficiency aggravates astrocytic endoplasmic reticulum stress and nod-like receptor protein 3 inflammasome activation

Author keywords

Astrocyte; Endoplasmic reticulum stress; Neuroinflammation; Parkinson's disease; Uncoupling protein 2

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; 1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; CASPASE 12; CCAAT ENHANCER BINDING PROTEIN; INFLAMMASOME; NOD LIKE RECEPTOR PROTEIN 3 INFLAMMASOME; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 2;

EID: 84887227883     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2013.08.015     Document Type: Article
Times cited : (85)

References (54)
  • 1
    • 79551591722 scopus 로고    scopus 로고
    • Astrocyte-neuron metabolic relationships: for better and for worse
    • Allaman I., Belanger M., Magistretti P.J. Astrocyte-neuron metabolic relationships: for better and for worse. Trends Neurosci. 2011, 34:76-87.
    • (2011) Trends Neurosci. , vol.34 , pp. 76-87
    • Allaman, I.1    Belanger, M.2    Magistretti, P.J.3
  • 2
    • 77953749940 scopus 로고    scopus 로고
    • Uncoupling protein-2 and the potential link between metabolism and longevity
    • Andrews Z.B. Uncoupling protein-2 and the potential link between metabolism and longevity. Curr. Aging Sci. 2010, 3:102-112.
    • (2010) Curr. Aging Sci. , vol.3 , pp. 102-112
    • Andrews, Z.B.1
  • 3
    • 27644448810 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the CNS: in support of function and survival
    • Andrews Z.B., Diano S., Horvath T.L. Mitochondrial uncoupling proteins in the CNS: in support of function and survival. Nat. Rev. Neurosci. 2005, 6:829-840.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 829-840
    • Andrews, Z.B.1    Diano, S.2    Horvath, T.L.3
  • 5
    • 67649342203 scopus 로고    scopus 로고
    • Endoplasmic reticulum and mitochondria interplay mediates apoptotic cell death: relevance to Parkinson's disease
    • Arduino D.M., Esteves A.R., Cardoso S.M., Oliveira C.R. Endoplasmic reticulum and mitochondria interplay mediates apoptotic cell death: relevance to Parkinson's disease. Neurochem. Int. 2009, 55:341-348.
    • (2009) Neurochem. Int. , vol.55 , pp. 341-348
    • Arduino, D.M.1    Esteves, A.R.2    Cardoso, S.M.3    Oliveira, C.R.4
  • 7
    • 77952559481 scopus 로고    scopus 로고
    • The on-off switches of the mitochondrial uncoupling proteins
    • Azzu V., Brand M.D. The on-off switches of the mitochondrial uncoupling proteins. Trends Biochem. Sci. 2010, 35:298-307.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 298-307
    • Azzu, V.1    Brand, M.D.2
  • 8
    • 78650878363 scopus 로고    scopus 로고
    • NF-kappaB, inflammation, and metabolic disease
    • Baker R.G., Hayden M.S., Ghosh S. NF-kappaB, inflammation, and metabolic disease. Cell Metab. 2011, 13:11-22.
    • (2011) Cell Metab. , vol.13 , pp. 11-22
    • Baker, R.G.1    Hayden, M.S.2    Ghosh, S.3
  • 9
    • 46549090129 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program in mouse melanoma cells: effect of curcumin
    • Bakhshi J., Weinstein L., Poksay K.S., Nishinaga B., Bredesen D.E., Rao R.V. Coupling endoplasmic reticulum stress to the cell death program in mouse melanoma cells: effect of curcumin. Apoptosis 2008, 13:904-914.
    • (2008) Apoptosis , vol.13 , pp. 904-914
    • Bakhshi, J.1    Weinstein, L.2    Poksay, K.S.3    Nishinaga, B.4    Bredesen, D.E.5    Rao, R.V.6
  • 10
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 11
    • 44049097234 scopus 로고    scopus 로고
    • Regulation of glial cell functions by PPAR-gamma natural and synthetic agonists
    • Bernardo A., Minghetti L. Regulation of glial cell functions by PPAR-gamma natural and synthetic agonists. PPAR Res. 2008, 2008:864140.
    • (2008) PPAR Res. , vol.2008 , pp. 864140
    • Bernardo, A.1    Minghetti, L.2
  • 12
    • 25144476923 scopus 로고    scopus 로고
    • Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
    • Brand M.D., Esteves T.C. Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3. Cell Metab. 2005, 2:85-93.
    • (2005) Cell Metab. , vol.2 , pp. 85-93
    • Brand, M.D.1    Esteves, T.C.2
  • 14
    • 67649756320 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
    • Bueler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp. Neurol. 2009, 218:235-246.
    • (2009) Exp. Neurol. , vol.218 , pp. 235-246
    • Bueler, H.1
  • 15
    • 26944461180 scopus 로고    scopus 로고
    • Reactive astrocytes as potential manipulation targets in novel cell replacement therapy of Parkinson's disease
    • Chen L.W., Yung K.L., Chan Y.S. Reactive astrocytes as potential manipulation targets in novel cell replacement therapy of Parkinson's disease. Curr. Drug Targets 2005, 6:821-833.
    • (2005) Curr. Drug Targets , vol.6 , pp. 821-833
    • Chen, L.W.1    Yung, K.L.2    Chan, Y.S.3
  • 17
    • 0242712492 scopus 로고    scopus 로고
    • Endoplasmic reticulum signaling as a determinant of recombinant protein expression
    • Cudna R.E., Dickson A.J. Endoplasmic reticulum signaling as a determinant of recombinant protein expression. Biotechnol. Bioeng. 2003, 81:56-65.
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 56-65
    • Cudna, R.E.1    Dickson, A.J.2
  • 18
    • 0035852755 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3 are highly active H(+) transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
    • Echtay K.S., Winkler E., Frischmuth K., Klingenberg M. Uncoupling proteins 2 and 3 are highly active H(+) transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone). Proc. Natl. Acad. Sci. U.S.A 2001, 98:1416-1421.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 1416-1421
    • Echtay, K.S.1    Winkler, E.2    Frischmuth, K.3    Klingenberg, M.4
  • 19
    • 83555160909 scopus 로고    scopus 로고
    • Proinflammatory cytokines, IL-1beta and TNF-alpha, induce expression of interleukin-34 mRNA via JNK- and p44/42 MAPK-NF-kappaB pathway but not p38 pathway in osteoblasts
    • Eda H., Shimada H., Beidler D.R., Monahan J.B. Proinflammatory cytokines, IL-1beta and TNF-alpha, induce expression of interleukin-34 mRNA via JNK- and p44/42 MAPK-NF-kappaB pathway but not p38 pathway in osteoblasts. Rheumatol. Int. 2010, 31:1525-1530.
    • (2010) Rheumatol. Int. , vol.31 , pp. 1525-1530
    • Eda, H.1    Shimada, H.2    Beidler, D.R.3    Monahan, J.B.4
  • 20
    • 79953148080 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death
    • Egawa N., Yamamoto K., Inoue H., Hikawa R., Nishi K., Mori K., Takahashi R. The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death. J.Biol. Chem. 2011, 286:7947-7957.
    • (2011) J.Biol. Chem. , vol.286 , pp. 7947-7957
    • Egawa, N.1    Yamamoto, K.2    Inoue, H.3    Hikawa, R.4    Nishi, K.5    Mori, K.6    Takahashi, R.7
  • 21
    • 37649024444 scopus 로고    scopus 로고
    • Role of uncoupling protein UCP2 in cell-mediated immunity: how macrophage-mediated insulitis is accelerated in a model of autoimmune diabetes
    • Emre Y., Hurtaud C., Karaca M., Nubel T., Zavala F., Ricquier D. Role of uncoupling protein UCP2 in cell-mediated immunity: how macrophage-mediated insulitis is accelerated in a model of autoimmune diabetes. Proc. Natl. Acad. Sci. U.S.A 2007, 104:19085-19090.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 19085-19090
    • Emre, Y.1    Hurtaud, C.2    Karaca, M.3    Nubel, T.4    Zavala, F.5    Ricquier, D.6
  • 22
    • 0038044029 scopus 로고    scopus 로고
    • Critical role for microglial NADPH oxidase in rotenone-induced degeneration of dopaminergic neurons
    • Gao H.M., Liu B., Hong J.S. Critical role for microglial NADPH oxidase in rotenone-induced degeneration of dopaminergic neurons. J.Neurosci. 2003, 23:6181-6187.
    • (2003) J.Neurosci. , vol.23 , pp. 6181-6187
    • Gao, H.M.1    Liu, B.2    Hong, J.S.3
  • 23
    • 54949147176 scopus 로고    scopus 로고
    • New regulators of NF-kappaB in inflammation
    • Ghosh S., Hayden M.S. New regulators of NF-kappaB in inflammation. Nat. Rev. Immunol. 2008, 8:837-848.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 837-848
    • Ghosh, S.1    Hayden, M.S.2
  • 24
    • 78650413857 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity
    • Hara H., Kamiya T., Adachi T. Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity. Neurochem. Int. 2011, 58:35-43.
    • (2011) Neurochem. Int. , vol.58 , pp. 35-43
    • Hara, H.1    Kamiya, T.2    Adachi, T.3
  • 25
    • 33750974801 scopus 로고    scopus 로고
    • Time dependent alterations of co-localization of S100beta and GFAP in the MPTP-treated mice
    • Himeda T., Watanabe Y., Tounai H., Hayakawa N., Kato H., Araki T. Time dependent alterations of co-localization of S100beta and GFAP in the MPTP-treated mice. J.Neural. Transm. 2006, 113:1887-1894.
    • (2006) J.Neural. Transm. , vol.113 , pp. 1887-1894
    • Himeda, T.1    Watanabe, Y.2    Tounai, H.3    Hayakawa, N.4    Kato, H.5    Araki, T.6
  • 27
    • 0036499736 scopus 로고    scopus 로고
    • Involvement of inducible nitric oxide synthase in inflammation-induced dopaminergic neurodegeneration
    • Iravani M.M., Kashefi K., Mander P., Rose S., Jenner P. Involvement of inducible nitric oxide synthase in inflammation-induced dopaminergic neurodegeneration. Neuroscience 2002, 110:49-58.
    • (2002) Neuroscience , vol.110 , pp. 49-58
    • Iravani, M.M.1    Kashefi, K.2    Mander, P.3    Rose, S.4    Jenner, P.5
  • 28
    • 0034520395 scopus 로고    scopus 로고
    • Inflammatory regulators in Parkinson's disease: iNOS, lipocortin-1, and cyclooxygenases-1 and -2
    • Knott C., Stern G., Wilkin G.P. Inflammatory regulators in Parkinson's disease: iNOS, lipocortin-1, and cyclooxygenases-1 and -2. Mol. Cell. Neurosci. 2000, 16:724-739.
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 724-739
    • Knott, C.1    Stern, G.2    Wilkin, G.P.3
  • 30
    • 34249824628 scopus 로고    scopus 로고
    • Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
    • Lemasters J.J. Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism. J.Gastroenterol. Hepatol. 2007, 22(suppl 1):S31-S37.
    • (2007) J.Gastroenterol. Hepatol. , vol.22 , Issue.SUPPL. 1
    • Lemasters, J.J.1
  • 31
    • 65749109534 scopus 로고    scopus 로고
    • Bradykinin-induced astrocyte-neuron signalling: glutamate release is mediated by ROS-activated volume-sensitive outwardly rectifying anion channels
    • Liu H.T., Akita T., Shimizu T., Sabirov R.Z., Okada Y. Bradykinin-induced astrocyte-neuron signalling: glutamate release is mediated by ROS-activated volume-sensitive outwardly rectifying anion channels. J.Physiol. 2009, 587:2197-2209.
    • (2009) J.Physiol. , vol.587 , pp. 2197-2209
    • Liu, H.T.1    Akita, T.2    Shimizu, T.3    Sabirov, R.Z.4    Okada, Y.5
  • 32
    • 80051783174 scopus 로고    scopus 로고
    • Uncoupling proteins and the control of mitochondrial reactive oxygen species production
    • Mailloux R.J., Harper M.E. Uncoupling proteins and the control of mitochondrial reactive oxygen species production. Free Radic. Biol. Med. 2011, 51:1106-1115.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1106-1115
    • Mailloux, R.J.1    Harper, M.E.2
  • 33
    • 33644639853 scopus 로고    scopus 로고
    • The emerging functions of UCP2 in health, disease, and therapeutics
    • Mattiasson G., Sullivan P.G. The emerging functions of UCP2 in health, disease, and therapeutics. Antioxid. Redox Signal 2006, 8:1-38.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1-38
    • Mattiasson, G.1    Sullivan, P.G.2
  • 34
    • 1942454250 scopus 로고    scopus 로고
    • Inflammation and neurodegeneration in Parkinson's disease
    • McGeer P.L., McGeer E.G. Inflammation and neurodegeneration in Parkinson's disease. Parkinsonism Relat. Disord. 2004, 10(suppl 1):S3-S7.
    • (2004) Parkinsonism Relat. Disord. , vol.10 , Issue.SUPPL. 1
    • McGeer, P.L.1    McGeer, E.G.2
  • 35
    • 77956196141 scopus 로고    scopus 로고
    • Mitochondria dysfunction and neurodegenerative disorders: Cause or consequence
    • Morais V.A., De Strooper B. Mitochondria dysfunction and neurodegenerative disorders: Cause or consequence. J.Alzheimers Dis. 2010, 20(suppl 2):S255-S263.
    • (2010) J.Alzheimers Dis. , vol.20 , Issue.SUPPL. 2
    • Morais, V.A.1    De Strooper, B.2
  • 36
    • 0345118108 scopus 로고    scopus 로고
    • Immunolocalization of peroxisome proliferator-activated receptors and retinoid X receptors in the adult rat CNS
    • Moreno S., Farioli-Vecchioli S., Ceru M.P. Immunolocalization of peroxisome proliferator-activated receptors and retinoid X receptors in the adult rat CNS. Neuroscience 2004, 123:131-145.
    • (2004) Neuroscience , vol.123 , pp. 131-145
    • Moreno, S.1    Farioli-Vecchioli, S.2    Ceru, M.P.3
  • 37
    • 77957304618 scopus 로고    scopus 로고
    • Reactive oxygen species and uncoupling protein 2 in pancreatic beta-cell function
    • Pi J., Collins S. Reactive oxygen species and uncoupling protein 2 in pancreatic beta-cell function. Diabetes Obes. Metab. 2010, 12(suppl 2):141-148.
    • (2010) Diabetes Obes. Metab. , vol.12 , Issue.SUPPL. 2 , pp. 141-148
    • Pi, J.1    Collins, S.2
  • 38
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao R.V., Ellerby H.M., Bredesen D.E. Coupling endoplasmic reticulum stress to the cell death program. Cell. Death. Differ. 2004, 11:372-380.
    • (2004) Cell. Death. Differ. , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 42
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu E.J., Harding H.P., Angelastro J.M., Vitolo O.V., Ron D., Greene L.A. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J.Neurosci. 2002, 22:10690-10698.
    • (2002) J.Neurosci. , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 43
    • 70449526441 scopus 로고    scopus 로고
    • Progressive dopaminergic degeneration in the chronic MPTPp mouse model of Parkinson's disease
    • Schintu N., Frau L., Ibba M., Garau A., Carboni E., Carta A.R. Progressive dopaminergic degeneration in the chronic MPTPp mouse model of Parkinson's disease. Neurotox. Res. 2009, 16:127-139.
    • (2009) Neurotox. Res. , vol.16 , pp. 127-139
    • Schintu, N.1    Frau, L.2    Ibba, M.3    Garau, A.4    Carboni, E.5    Carta, A.R.6
  • 45
    • 36049034344 scopus 로고    scopus 로고
    • Anti-inflammatory actions of PPAR ligands: new insights on cellular and molecular mechanisms
    • Straus D.S., Glass C.K. Anti-inflammatory actions of PPAR ligands: new insights on cellular and molecular mechanisms. Trends Immunol. 2007, 28:551-558.
    • (2007) Trends Immunol. , vol.28 , pp. 551-558
    • Straus, D.S.1    Glass, C.K.2
  • 46
    • 5444228135 scopus 로고    scopus 로고
    • Cellular pathology of Parkinson's disease: astrocytes, microglia and inflammation
    • Teismann P., Schulz J.B. Cellular pathology of Parkinson's disease: astrocytes, microglia and inflammation. Cell Tissue Res. 2004, 318:149-161.
    • (2004) Cell Tissue Res. , vol.318 , pp. 149-161
    • Teismann, P.1    Schulz, J.B.2
  • 47
    • 84880651157 scopus 로고    scopus 로고
    • The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
    • Triantafilou K., Hughes T.R., Triantafilou M., Morgan B.P. The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation. J.Cell Sci. 2013, 126:2903-2913.
    • (2013) J.Cell Sci. , vol.126 , pp. 2903-2913
    • Triantafilou, K.1    Hughes, T.R.2    Triantafilou, M.3    Morgan, B.P.4
  • 48
    • 67649760168 scopus 로고    scopus 로고
    • Mitochondrial dynamics in Parkinson's disease
    • Van Laar V.S., Berman S.B. Mitochondrial dynamics in Parkinson's disease. Exp. Neurol. 2009, 218:247-256.
    • (2009) Exp. Neurol. , vol.218 , pp. 247-256
    • Van Laar, V.S.1    Berman, S.B.2
  • 49
    • 12944314765 scopus 로고    scopus 로고
    • Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons
    • Verkhratsky A. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol. Rev. 2005, 85:201-279.
    • (2005) Physiol. Rev. , vol.85 , pp. 201-279
    • Verkhratsky, A.1
  • 50
    • 84858630049 scopus 로고    scopus 로고
    • Arole for the NLRP3 inflammasome in metabolic diseases-did Warburg miss inflammation?
    • Wen H., Ting J.P., O'Neill L.A. Arole for the NLRP3 inflammasome in metabolic diseases-did Warburg miss inflammation?. Nature Immunol. 2012, 13:352-357.
    • (2012) Nature Immunol. , vol.13 , pp. 352-357
    • Wen, H.1    Ting, J.P.2    O'Neill, L.A.3
  • 51
    • 0027194462 scopus 로고
    • New stereological methods for counting neurons
    • West M.J. New stereological methods for counting neurons. Neurobiol. Aging 1993, 14:275-285.
    • (1993) Neurobiol. Aging , vol.14 , pp. 275-285
    • West, M.J.1
  • 54
    • 57649155208 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance
    • Zhou C., Huang Y., Przedborski S. Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance. Ann. N. Y. Acad. Sci. 2008, 1147:93-104.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 93-104
    • Zhou, C.1    Huang, Y.2    Przedborski, S.3


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