메뉴 건너뛰기




Volumn 111, Issue 5, 2009, Pages 1094-1103

Zn2+ mediates ischemia-induced impairment of the ubiquitin-proteasome system in the rat hippocampus

Author keywords

Global ischemia; Hippocampus; Neurodegeneration; Proteasome; Ubiquitination

Indexed keywords

PHOSPHORYLASE PHOSPHATASE; PROTEASOME; SYNAPTOPHYSIN; UBIQUITIN; ZINC; ZINC CHLORIDE; 4 [4 (4 FLUOROPHENYL) 5 (2 METHOXY 4 PYRIMIDINYL) 1 IMIDAZOLYL]CYCLOHEXANOL; ACTIN; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CHELATING AGENT; COUMARIN DERIVATIVE; EDETIC ACID; ENZYME INHIBITOR; FLUORESCENT DYE; GREEN FLUORESCENT PROTEIN; IMIDAZOLE DERIVATIVE; LEUPEPTIN; MICROTUBULE ASSOCIATED PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; OLIGOPEPTIDE; PYRIMIDINE DERIVATIVE; SUCCINYL LEUCYL LEUCYL VALYL TYROSYL METHYLCOUMARINAMIDE; SUCCINYL-LEUCYL-LEUCYL-VALYL-TYROSYL-METHYLCOUMARINAMIDE;

EID: 70350786959     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06401.x     Document Type: Article
Times cited : (14)

References (46)
  • 2
    • 0021287299 scopus 로고
    • Release of endogenous Zn2+ from brain tissue during activity
    • Assaf S. Y. Chung S. H. (1984) Release of endogenous Zn2+ from brain tissue during activity. Nature 308, 734 736.
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 3
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's diseases
    • Barnham K. J. Bush A. I. (2008) Metals in Alzheimer's and Parkinson's diseases. Curr. Opin. Chem. Biol. 12, 222 228.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F., Sampat R. M. Kopito R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552 1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 8
    • 4143083990 scopus 로고    scopus 로고
    • Distinct requirements for p38alpha and c-Jun N-terminal kinase stress-activated protein kinases in different forms of apoptotic neuronal death
    • Cao J., Semenova M. M., Solovyan V. T., Han J., Coffey E. T. Courtney M. J. (2004) Distinct requirements for p38alpha and c-Jun N-terminal kinase stress-activated protein kinases in different forms of apoptotic neuronal death. J. Biol. Chem. 279, 35903 35913.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35903-35913
    • Cao, J.1    Semenova, M.M.2    Solovyan, V.T.3    Han, J.4    Coffey, E.T.5    Courtney, M.J.6
  • 9
    • 33846456236 scopus 로고    scopus 로고
    • Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain-derived neurotrophic factor gene regulation and limbic epileptogenesis
    • Chen Q., He S., Hu X. L., Yu J., Zhou Y., Zheng J., Zhang S., Zhang C., Duan W. H. Xiong Z. Q. (2007) Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain-derived neurotrophic factor gene regulation and limbic epileptogenesis. J. Neurosci. 27, 542 552.
    • (2007) J. Neurosci. , vol.27 , pp. 542-552
    • Chen, Q.1    He, S.2    Hu, X.L.3    Yu, J.4    Zhou, Y.5    Zheng, J.6    Zhang, S.7    Zhang, C.8    Duan, W.H.9    Xiong, Z.Q.10
  • 10
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson T. M. Dawson V. L. (2003) Molecular pathways of neurodegeneration in Parkinson's disease. Science 302, 819 822.
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 11
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers M. D. (2003) Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 6, 231 242.
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 12
    • 0024477326 scopus 로고
    • Translocation of zinc may contribute to seizure-induced death of neurons
    • Frederickson C. J., Hernandez M. D. McGinty J. F. (1989) Translocation of zinc may contribute to seizure-induced death of neurons. Brain Res. 480, 317 321.
    • (1989) Brain Res. , vol.480 , pp. 317-321
    • Frederickson, C.J.1    Hernandez, M.D.2    McGinty, J.F.3
  • 13
    • 4444358048 scopus 로고    scopus 로고
    • Method for identifying neuronal cells suffering zinc toxicity by use of a novel fluorescent sensor
    • Frederickson C. J., Burdette S. C., Frederickson C. J. et al. (2004) Method for identifying neuronal cells suffering zinc toxicity by use of a novel fluorescent sensor. J. Neurosci. Methods 139, 79 89.
    • (2004) J. Neurosci. Methods , vol.139 , pp. 79-89
    • Frederickson, C.J.1    Burdette, S.C.2    Frederickson, C.J.3
  • 14
    • 33645743410 scopus 로고    scopus 로고
    • Concentrations of extracellular free zinc (pZn)e in the central nervous system during simple anesthetization, ischemia and reperfusion
    • Frederickson C. J., Giblin L. J., Krezel A. et al. (2006) Concentrations of extracellular free zinc (pZn)e in the central nervous system during simple anesthetization, ischemia and reperfusion. Exp. Neurol. 198, 285 293.
    • (2006) Exp. Neurol. , vol.198 , pp. 285-293
    • Frederickson, C.J.1    Giblin, L.J.2    Krezel, A.3
  • 15
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • Ge P., Luo Y., Liu C. L. Hu B. (2007) Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 38, 3230 3236.
    • (2007) Stroke , vol.38 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.L.3    Hu, B.4
  • 16
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon T., Chomsky O. Kulka R. G. (1998) Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J. 17, 2759 2766.
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 17
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • Gilon T., Chomsky O. Kulka R. G. (2000) Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair. Mol. Cell. Biol. 20, 7214 7219.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 18
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M. H. Ciechanover A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373 428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 20
    • 0026323448 scopus 로고
    • Changes in ubiquitin and ubiquitin-protein conjugates in the CA1 neurons after transient sublethal ischemia
    • Hayashi T., Takada K. Matsuda M. (1991) Changes in ubiquitin and ubiquitin-protein conjugates in the CA1 neurons after transient sublethal ischemia. Mol. Chem. Neuropathol. 15, 75 82.
    • (1991) Mol. Chem. Neuropathol. , vol.15 , pp. 75-82
    • Hayashi, T.1    Takada, K.2    Matsuda, M.3
  • 21
    • 0026663450 scopus 로고
    • Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion
    • Hayashi T., Takada K. Matsuda M. (1992) Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion. Neuroreport 3, 519 520.
    • (1992) Neuroreport , vol.3 , pp. 519-520
    • Hayashi, T.1    Takada, K.2    Matsuda, M.3
  • 22
    • 0021220724 scopus 로고
    • Stimulation-induced uptake and release of zinc in hippocampal slices
    • Howell G. A., Welch M. G. Frederickson C. J. (1984) Stimulation-induced uptake and release of zinc in hippocampal slices. Nature 308, 736 738.
    • (1984) Nature , vol.308 , pp. 736-738
    • Howell, G.A.1    Welch, M.G.2    Frederickson, C.J.3
  • 23
    • 0034192398 scopus 로고    scopus 로고
    • Protein aggregation after transient cerebral ischemia
    • Hu B. R., Martone M. E., Jones Y. Z. Liu C. L. (2000) Protein aggregation after transient cerebral ischemia. J. Neurosci. 20, 3191 3199.
    • (2000) J. Neurosci. , vol.20 , pp. 3191-3199
    • Hu, B.R.1    Martone, M.E.2    Jones, Y.Z.3    Liu, C.L.4
  • 24
    • 39449099067 scopus 로고    scopus 로고
    • Zinc-mediated transactivation of TrkB potentiates the hippocampal mossy fiber-CA3 pyramid synapse
    • Huang Y. Z., Pan E., Xiong Z. Q. McNamara J. O. (2008) Zinc-mediated transactivation of TrkB potentiates the hippocampal mossy fiber-CA3 pyramid synapse. Neuron 57, 546 558.
    • (2008) Neuron , vol.57 , pp. 546-558
    • Huang, Y.Z.1    Pan, E.2    Xiong, Z.Q.3    McNamara, J.O.4
  • 25
    • 0033502802 scopus 로고    scopus 로고
    • Ubiquitin stress response in postischemic hippocampal neurons under nontolerant and tolerant conditions
    • Ide T., Takada K., Qiu J. H., Saito N., Kawahara N., Asai A. Kirino T. (1999) Ubiquitin stress response in postischemic hippocampal neurons under nontolerant and tolerant conditions. J. Cereb. Blood Flow Metab. 19, 750 756.
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , pp. 750-756
    • Ide, T.1    Takada, K.2    Qiu, J.H.3    Saito, N.4    Kawahara, N.5    Asai, A.6    Kirino, T.7
  • 26
    • 33645989470 scopus 로고    scopus 로고
    • Influence of location of a fluorescent zinc probe in brain slices on its response to synaptic activation
    • Kay A. R. Toth K. (2006) Influence of location of a fluorescent zinc probe in brain slices on its response to synaptic activation. J. Neurophysiol. 95, 1949 1956.
    • (2006) J. Neurophysiol. , vol.95 , pp. 1949-1956
    • Kay, A.R.1    Toth, K.2
  • 28
    • 0028343364 scopus 로고
    • Zinc toxicity on cultured cortical neurons: Involvement of N-methyl-D-aspartate receptors
    • Koh J. Y. Choi D. W. (1994) Zinc toxicity on cultured cortical neurons: involvement of N-methyl-D-aspartate receptors. Neuroscience 60, 1049 1057.
    • (1994) Neuroscience , vol.60 , pp. 1049-1057
    • Koh, J.Y.1    Choi, D.W.2
  • 29
    • 0029777299 scopus 로고    scopus 로고
    • The role of zinc in selective neuronal death after transient global cerebral ischemia
    • Koh J. Y., Suh S. W., Gwag B. J., He Y. Y., Hsu C. Y. Choi D. W. (1996) The role of zinc in selective neuronal death after transient global cerebral ischemia. Science 272, 1013 1016.
    • (1996) Science , vol.272 , pp. 1013-1016
    • Koh, J.Y.1    Suh, S.W.2    Gwag, B.J.3    He, Y.Y.4    Hsu, C.Y.5    Choi, D.W.6
  • 30
    • 0033360169 scopus 로고    scopus 로고
    • Regulation of morphological postsynaptic silent synapses in developing hippocampal neurons
    • Liao D., Zhang X., O'Brien R., Ehlers M. D. Huganir R. L. (1999) Regulation of morphological postsynaptic silent synapses in developing hippocampal neurons. Nat. Neurosci. 2, 37 43.
    • (1999) Nat. Neurosci. , vol.2 , pp. 37-43
    • Liao, D.1    Zhang, X.2    O'Brien, R.3    Ehlers, M.D.4    Huganir, R.L.5
  • 31
    • 21744453627 scopus 로고    scopus 로고
    • Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia
    • DOI 10.1016/j.neuroscience.2005.03.036, PII S0306452205003350
    • Liu C., Chen S., Kamme F. Hu B. R. (2005) Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia. Neuroscience 134, 69 80. (Pubitemid 40943635)
    • (2005) Neuroscience , vol.134 , Issue.1 , pp. 69-80
    • Liu, C.1    Chen, S.2    Kamme, F.3    Hu, B.R.4
  • 32
    • 0030044329 scopus 로고    scopus 로고
    • Transient ischemia depletes free ubiquitin in the gerbil hippocampal CA1 neurons
    • Morimoto T., Ide T., Ihara Y., Tamura A. Kirino T. (1996) Transient ischemia depletes free ubiquitin in the gerbil hippocampal CA1 neurons. Am. J. Pathol. 148, 249 257.
    • (1996) Am. J. Pathol. , vol.148 , pp. 249-257
    • Morimoto, T.1    Ide, T.2    Ihara, Y.3    Tamura, A.4    Kirino, T.5
  • 33
    • 2942708228 scopus 로고    scopus 로고
    • Mechanism of neurodegenerative disease: Role of the ubiquitin proteasome system
    • Petrucelli L. Dawson T. M. (2004) Mechanism of neurodegenerative disease: role of the ubiquitin proteasome system. Ann. Med. 36, 315 320.
    • (2004) Ann. Med. , vol.36 , pp. 315-320
    • Petrucelli, L.1    Dawson, T.M.2
  • 34
    • 0018347695 scopus 로고
    • A new model of bilateral hemispheric ischemia in the unanesthetized rat
    • Pulsinelli W. A. Brierley J. B. (1979) A new model of bilateral hemispheric ischemia in the unanesthetized rat. Stroke 10, 267 272.
    • (1979) Stroke , vol.10 , pp. 267-272
    • Pulsinelli, W.A.1    Brierley, J.B.2
  • 35
    • 1942520949 scopus 로고    scopus 로고
    • Response to kainic acid injections: Changes in staining for zinc, FOS, cell death and glial response in the rat forebrain
    • Riba-Bosch A. Perez-Clausell J. (2004) Response to kainic acid injections: changes in staining for zinc, FOS, cell death and glial response in the rat forebrain. Neuroscience 125, 803 818.
    • (2004) Neuroscience , vol.125 , pp. 803-818
    • Riba-Bosch, A.1    Perez-Clausell, J.2
  • 36
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D. C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780 786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 37
    • 0033950543 scopus 로고    scopus 로고
    • Fluoro-Jade: Novel fluorochromes for detecting toxicant-induced neuronal degeneration
    • Schmued L. C. Hopkins K. J. (2000) Fluoro-Jade: novel fluorochromes for detecting toxicant-induced neuronal degeneration. Toxicol. Pathol. 28, 91 99.
    • (2000) Toxicol. Pathol. , vol.28 , pp. 91-99
    • Schmued, L.C.1    Hopkins, K.J.2
  • 41
    • 0037168111 scopus 로고    scopus 로고
    • Fleeting activation of ionotropic glutamate receptors sensitizes cortical neurons to complement attack
    • Xiong Z. Q. McNamara J. O. (2002) Fleeting activation of ionotropic glutamate receptors sensitizes cortical neurons to complement attack. Neuron 36, 363 374.
    • (2002) Neuron , vol.36 , pp. 363-374
    • Xiong, Z.Q.1    McNamara, J.O.2
  • 42
    • 0037322558 scopus 로고    scopus 로고
    • Formation of complement membrane attack complex in mammalian cerebral cortex evokes seizures and neurodegeneration
    • Xiong Z. Q., Qian W., Suzuki K. McNamara J. O. (2003) Formation of complement membrane attack complex in mammalian cerebral cortex evokes seizures and neurodegeneration. J. Neurosci. 23, 955 960.
    • (2003) J. Neurosci. , vol.23 , pp. 955-960
    • Xiong, Z.Q.1    Qian, W.2    Suzuki, K.3    McNamara, J.O.4
  • 43
    • 0042848910 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome system in the early stages of wallerian degeneration
    • Zhai Q., Wang J., Kim A., Liu Q., Watts R., Hoopfer E., Mitchison T., Luo L. He Z. (2003) Involvement of the ubiquitin-proteasome system in the early stages of wallerian degeneration. Neuron 39, 217 225.
    • (2003) Neuron , vol.39 , pp. 217-225
    • Zhai, Q.1    Wang, J.2    Kim, A.3    Liu, Q.4    Watts, R.5    Hoopfer, E.6    Mitchison, T.7    Luo, L.8    He, Z.9
  • 46
    • 0037222287 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase after focal cerebral ischemia stimulates neurogenesis in the adult rodent dentate gyrus
    • Zhu D. Y., Liu S. H., Sun H. S. Lu Y. M. (2003) Expression of inducible nitric oxide synthase after focal cerebral ischemia stimulates neurogenesis in the adult rodent dentate gyrus. J. Neurosci. 23, 223 229.
    • (2003) J. Neurosci. , vol.23 , pp. 223-229
    • Zhu, D.Y.1    Liu, S.H.2    Sun, H.S.3    Lu, Y.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.