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Volumn 18, Issue 2, 2008, Pages 136-145

Proteasome inhibition: An early or late event in nitric oxide-induced neuronal death?

Author keywords

Neuronal cell death; Nitric oxide; Oxidative stress; Proteasome activity; Proteasome subunit gene; Ubiquitin proteasome system

Indexed keywords

3,3 BIS(2 AMINOETHYL) 1 HYDROXY 2 OXOTRIAZENE; LACTACYSTIN; NITRIC OXIDE; PROTEASOME; PROTEASOME INHIBITOR;

EID: 38749144760     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2007.11.002     Document Type: Article
Times cited : (14)

References (44)
  • 5
    • 0037330339 scopus 로고    scopus 로고
    • Up-regulation of inducible nitric oxide synthase in the substantia nigra by lipopolysaccharide causes microglial activation and neurodegeneration
    • Arimoto T., and Bing G. Up-regulation of inducible nitric oxide synthase in the substantia nigra by lipopolysaccharide causes microglial activation and neurodegeneration. Neurobiology of Disease 12 (2003) 35-45
    • (2003) Neurobiology of Disease , vol.12 , pp. 35-45
    • Arimoto, T.1    Bing, G.2
  • 8
    • 0028796770 scopus 로고
    • Inhibition of neuronal nitric oxide synthase by 7-nitroindazole protects against MPTP-induced neurotoxicity in mice
    • Schulz J.B., Matthews R.T., Muqit M.M., Browne S.E., and Beal M.F. Inhibition of neuronal nitric oxide synthase by 7-nitroindazole protects against MPTP-induced neurotoxicity in mice. Journal of Neurochemistry 64 (1995) 936-939
    • (1995) Journal of Neurochemistry , vol.64 , pp. 936-939
    • Schulz, J.B.1    Matthews, R.T.2    Muqit, M.M.3    Browne, S.E.4    Beal, M.F.5
  • 11
    • 3242733689 scopus 로고    scopus 로고
    • D. Yao, Z. Gu, T. Nakamura, Z.Q. Shi, Y. Ma, B. Gaston, L.A. Palmer, E.M. Rockenstein, Z. Zhang, E. Masliah, T. Uehara, S.A. Lipton, Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity, Proceedings of the National Academy of Sciences USA 101 (2004) 10810-10814.
    • D. Yao, Z. Gu, T. Nakamura, Z.Q. Shi, Y. Ma, B. Gaston, L.A. Palmer, E.M. Rockenstein, Z. Zhang, E. Masliah, T. Uehara, S.A. Lipton, Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity, Proceedings of the National Academy of Sciences USA 101 (2004) 10810-10814.
  • 13
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • Lipton S.A., Choi Y.B., Pan Z.H., Lei S.Z., Chen H.S., Sucher N.J., Loscalzo J., Singel D.J., and Stamler J.S. A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature 364 (1993) 626-632
    • (1993) Nature , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.B.2    Pan, Z.H.3    Lei, S.Z.4    Chen, H.S.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 14
    • 0028998421 scopus 로고
    • S-Nitrosothiols and the bioregulatory actions of nitrogen oxides through reactions with thiol groups
    • Stamler J.S. S-Nitrosothiols and the bioregulatory actions of nitrogen oxides through reactions with thiol groups. Current Topics in Microbiology and Immunology 196 (1995) 19-36
    • (1995) Current Topics in Microbiology and Immunology , vol.196 , pp. 19-36
    • Stamler, J.S.1
  • 15
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: translocation, regulation, and a consensus motif
    • Stamler J.S., Toone E.J., Lipton S.A., and Sucher N.J. (S)NO signals: translocation, regulation, and a consensus motif. Neuron 18 (1997) 691-696
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 16
    • 0033538443 scopus 로고    scopus 로고
    • Activation of the cell death program by nitric oxide involves inhibition of the proteasome
    • Glockzin S., von Knethen A., Scheffner M., and Brune B. Activation of the cell death program by nitric oxide involves inhibition of the proteasome. Journal of Biological Chemistry 274 (1999) 19581-19586
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 19581-19586
    • Glockzin, S.1    von Knethen, A.2    Scheffner, M.3    Brune, B.4
  • 18
    • 21344452761 scopus 로고    scopus 로고
    • Comment on "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function"
    • Lipton S.A., Nakamura T., Yao D., Shi Z.Q., Uehara T., and Gu Z. Comment on "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function". Science 308 (2005) 1870
    • (2005) Science , vol.308 , pp. 1870
    • Lipton, S.A.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Uehara, T.5    Gu, Z.6
  • 20
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.S., and Li L. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. Journal of Biological Chemistry 279 (2004) 13256-13264
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 22
    • 23944459100 scopus 로고    scopus 로고
    • Nitrosative and oxidative stress links dysfunctional ubiquitination to Parkinson's disease
    • Gu Z., Nakamura T., Yao D., Shi Z.Q., and Lipton S.A. Nitrosative and oxidative stress links dysfunctional ubiquitination to Parkinson's disease. Cell Death Differentiation 12 (2005) 1202-1204
    • (2005) Cell Death Differentiation , vol.12 , pp. 1202-1204
    • Gu, Z.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4    Lipton, S.A.5
  • 23
    • 33644858343 scopus 로고    scopus 로고
    • The unfolded protein response: a stress signaling pathway critical for health and disease
    • Zhang K., and Kaufman R.J. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology 66 (2006) S102-S109
    • (2006) Neurology , vol.66
    • Zhang, K.1    Kaufman, R.J.2
  • 24
    • 0032191207 scopus 로고    scopus 로고
    • Micromolar l-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurons
    • Cheung N.S., Pascoe C.J., Giardina S.F., John C.A., and Beart P.M. Micromolar l-glutamate induces extensive apoptosis in an apoptotic-necrotic continuum of insult-dependent, excitotoxic injury in cultured cortical neurons. Neuropharmacology 37 (1998) 1419-1429
    • (1998) Neuropharmacology , vol.37 , pp. 1419-1429
    • Cheung, N.S.1    Pascoe, C.J.2    Giardina, S.F.3    John, C.A.4    Beart, P.M.5
  • 27
    • 38749135301 scopus 로고    scopus 로고
    • Neuroprotective and pro-apoptotic responses of ubiquitin proteasome system
    • Di Napoli M., and Wójcik C. (Eds), Nova Science Publishers, Inc. (Chapter 24)
    • Choy M.S., and Cheung N.S. Neuroprotective and pro-apoptotic responses of ubiquitin proteasome system. In: Di Napoli M., and Wójcik C. (Eds). The UPS in the nervous system: from physiology to pathology (2006), Nova Science Publishers, Inc. 1-21 (Chapter 24)
    • (2006) The UPS in the nervous system: from physiology to pathology , pp. 1-21
    • Choy, M.S.1    Cheung, N.S.2
  • 28
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmics reticulum chaperones, and thermotolerance
    • Bush K.T., Goldberg A.L., and Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmics reticulum chaperones, and thermotolerance. Journal of Biological Chemistry 272 (1997) 9086-9092
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 29
    • 0035451913 scopus 로고    scopus 로고
    • Proteasome and proteasome inhibition in the central nervous system
    • Ding Q., and Keller J.N. Proteasome and proteasome inhibition in the central nervous system. Free Radical Biology & Medicine 31 (2001) 574-584
    • (2001) Free Radical Biology & Medicine , vol.31 , pp. 574-584
    • Ding, Q.1    Keller, J.N.2
  • 30
  • 33
    • 26644449682 scopus 로고    scopus 로고
    • Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels
    • Chen Y., Shertzer H.G., Schneider S.N., Nebert D.W., and Dalton T.P. Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels. Journal of Biological Chemistry 280 (2005) 33766-33774
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 33766-33774
    • Chen, Y.1    Shertzer, H.G.2    Schneider, S.N.3    Nebert, D.W.4    Dalton, T.P.5
  • 34
    • 27544480481 scopus 로고    scopus 로고
    • Molecular implications of the human glutathione transferase A-4 gene (hGSTA4) polymorphisms in neurodegenerative diseases
    • Coppedè F., Armani C., Della Bidia D., Petrozzi L., Bonuccelli U., and Migliore L. Molecular implications of the human glutathione transferase A-4 gene (hGSTA4) polymorphisms in neurodegenerative diseases. Mutation Research 579 (2005) 107-114
    • (2005) Mutation Research , vol.579 , pp. 107-114
    • Coppedè, F.1    Armani, C.2    Della Bidia, D.3    Petrozzi, L.4    Bonuccelli, U.5    Migliore, L.6
  • 35
    • 12144265572 scopus 로고    scopus 로고
    • Microsomal glutathione S-transferase 1 in the retinal pigment epithelium: protection against oxidative stress and a potential role in aging
    • Maeda A., Crabb J.W., and Palczewski K. Microsomal glutathione S-transferase 1 in the retinal pigment epithelium: protection against oxidative stress and a potential role in aging. Biochemistry 44 (2005) 480-489
    • (2005) Biochemistry , vol.44 , pp. 480-489
    • Maeda, A.1    Crabb, J.W.2    Palczewski, K.3
  • 36
    • 8644263976 scopus 로고    scopus 로고
    • A proteasomal stress response: pre-treatment with proteasome inhibitors increases proteasome activity and reduces neuronal vulnerability to oxidative injury
    • Lee C.S., Tee L.Y., Warmke T., Vinjamoori A., Cai A., Fagan A.M., and Snider B.J. A proteasomal stress response: pre-treatment with proteasome inhibitors increases proteasome activity and reduces neuronal vulnerability to oxidative injury. Journal of Neurochemistry 91 (2004) 996-1006
    • (2004) Journal of Neurochemistry , vol.91 , pp. 996-1006
    • Lee, C.S.1    Tee, L.Y.2    Warmke, T.3    Vinjamoori, A.4    Cai, A.5    Fagan, A.M.6    Snider, B.J.7
  • 37
    • 33344465235 scopus 로고    scopus 로고
    • Comparative microarray analysis of programmed cell death induced by proteasome malfunction and hypersensitive response in plants
    • Kim M., Lee S., Park K., Jeong E.J., Ryu C.M., Choi D., and Pai H.S. Comparative microarray analysis of programmed cell death induced by proteasome malfunction and hypersensitive response in plants. Biochemical and Biophysical Research Communications 342 (2006) 514-521
    • (2006) Biochemical and Biophysical Research Communications , vol.342 , pp. 514-521
    • Kim, M.1    Lee, S.2    Park, K.3    Jeong, E.J.4    Ryu, C.M.5    Choi, D.6    Pai, H.S.7
  • 38
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners S., Heyken D., Weller A., Kudwig A., Stangl K., Kloetzel P.M., and Krüger E. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. Journal of Biological Chemistry 278 (2003) 21517-21525
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Kudwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Krüger, E.7
  • 40
    • 0025644201 scopus 로고    scopus 로고
    • Z. Chen, C.M. Pickart, A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin, Journal of Biological Chemistry 265 (1990) 21835-21842.
    • Z. Chen, C.M. Pickart, A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin, Journal of Biological Chemistry 265 (1990) 21835-21842.
  • 41
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker R.T., Tobias J.W., and Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. Journal of Biological Chemistry 267 (1992) 23364-23375
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 42
    • 0031463942 scopus 로고    scopus 로고
    • A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond
    • Gilchrist C.A., Gray D.A., and Baker R.T. A ubiquitin-specific protease that efficiently cleaves the ubiquitin-proline bond. Journal of Biological Chemistry 272 (1997) 32280-32285
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 32280-32285
    • Gilchrist, C.A.1    Gray, D.A.2    Baker, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.