메뉴 건너뛰기




Volumn 58, Issue 1, 2011, Pages 35-43

Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity

Author keywords

6 Hydroxydopamine; Heme oxygese 1; Oxidative stress ER stress; Preconditioning

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; DACTINOMYCIN; GLUCOSE REGULATED PROTEIN 78; HEME OXYGENASE 1; OXIDOPAMINE; THAPSIGARGIN; TUNICAMYCIN;

EID: 78650413857     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2010.10.006     Document Type: Article
Times cited : (38)

References (41)
  • 1
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • J. Alam, D. Stewart, C. Touchard, S. Boinapally, A.M. Choi, and J.L. Cook Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene J. Biol. Chem. 274 1999 26071 26078
    • (1999) J. Biol. Chem. , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 3
    • 0037127305 scopus 로고    scopus 로고
    • Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response
    • S.H. Chang, I. Barbosa-Tessmann, C. Chen, M.S. Kilberg, and A. Agarwal Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response J. Biol. Chem. 277 2002 1933 1940
    • (2002) J. Biol. Chem. , vol.277 , pp. 1933-1940
    • Chang, S.H.1    Barbosa-Tessmann, I.2    Chen, C.3    Kilberg, M.S.4    Agarwal, A.5
  • 4
    • 29644437160 scopus 로고    scopus 로고
    • 4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2
    • Z.H. Chen, Y. Saito, Y. Yoshida, A. Sekine, N. Noguchi, and E. Niki 4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2 J. Biol. Chem. 280 2005 41921 41927
    • (2005) J. Biol. Chem. , vol.280 , pp. 41921-41927
    • Chen, Z.H.1    Saito, Y.2    Yoshida, Y.3    Sekine, A.4    Noguchi, N.5    Niki, E.6
  • 5
    • 0016378870 scopus 로고
    • The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents
    • G. Cohen, and R.E. Heikkila The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents J. Biol. Chem. 249 1974 2447 2452
    • (1974) J. Biol. Chem. , vol.249 , pp. 2447-2452
    • Cohen, G.1    Heikkila, R.E.2
  • 7
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • S.B. Cullinan, and J.A. Diehl PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress J. Biol. Chem. 279 2004 20108 20117
    • (2004) J. Biol. Chem. , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 9
    • 0018095085 scopus 로고
    • Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones
    • D.G. Graham Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones Mol. Pharmacol. 14 1978 633 643
    • (1978) Mol. Pharmacol. , vol.14 , pp. 633-643
    • Graham, D.G.1
  • 10
    • 33748581394 scopus 로고    scopus 로고
    • Apomorphine protects against 6-hydroxydopamine-induced neuronal cell death through activation of the Nrf2-ARE pathway
    • H. Hara, M. Ohta, and T. Adachi Apomorphine protects against 6-hydroxydopamine-induced neuronal cell death through activation of the Nrf2-ARE pathway J. Neurosci. Res. 84 2006 860 866
    • (2006) J. Neurosci. Res. , vol.84 , pp. 860-866
    • Hara, H.1    Ohta, M.2    Adachi, T.3
  • 11
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • H.P. Harding, Y. Zhang, and D. Ron Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature 397 1999 271 274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 12
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • H.P. Harding, I. Novoa, Y. Zhang, H. Zeng, R. Wek, M. Schapira, and D. Ron Regulated translation initiation controls stress-induced gene expression in mammalian cells Mol. Cell 6 2000 1099 1108
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 14
    • 0028812293 scopus 로고
    • Enzymatic oxidation of dopamine: The role of prostaglandin H synthase
    • T.G. Hastings Enzymatic oxidation of dopamine: the role of prostaglandin H synthase J. Neurochem. 64 1995 919 924
    • (1995) J. Neurochem. , vol.64 , pp. 919-924
    • Hastings, T.G.1
  • 15
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • C.H. He, P. Gong, B. Hu, D. Stewart, M.E. Choi, A.M. Choi, and J. Alam Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation J. Biol. Chem. 276 2001 20858 20865
    • (2001) J. Biol. Chem. , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 16
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • W.A. Holtz, and K.L. O'Malley Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons J. Biol. Chem. 278 2003 19367 19377
    • (2003) J. Biol. Chem. , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 17
    • 0041853778 scopus 로고    scopus 로고
    • Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK1/2 activation
    • C.C. Hung, T. Ichimura, J.L. Stevens, and J.V. Bonventre Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK1/2 activation J. Biol. Chem. 278 2003 29317 29326
    • (2003) J. Biol. Chem. , vol.278 , pp. 29317-29326
    • Hung, C.C.1    Ichimura, T.2    Stevens, J.L.3    Bonventre, J.V.4
  • 18
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Y. Imai, M. Soda, H. Inoue, N. Hattori, Y. Mizuno, and R. Takahashi An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin Cell 105 2001 891 902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 20
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • P. Jenner Oxidative stress in Parkinson's disease Ann. Neurol. 53 2003 S26 38
    • (2003) Ann. Neurol. , vol.53 , pp. 26-38
    • Jenner, P.1
  • 23
    • 0037016759 scopus 로고    scopus 로고
    • Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells
    • J. Li, J.M. Lee, and J.A. Johnson Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells J. Biol. Chem. 277 2002 388 394
    • (2002) J. Biol. Chem. , vol.277 , pp. 388-394
    • Li, J.1    Lee, J.M.2    Johnson, J.A.3
  • 24
    • 0032524608 scopus 로고    scopus 로고
    • Role of calcium in the activation of erp72 and heme oxygenase-1 expression on depletion of endoplasmic reticulum calcium stores in rat neuronal cell culture
    • T. Linden, J. Doutheil, and W. Paschen Role of calcium in the activation of erp72 and heme oxygenase-1 expression on depletion of endoplasmic reticulum calcium stores in rat neuronal cell culture Neurosci. Lett. 247 1998 103 106
    • (1998) Neurosci. Lett. , vol.247 , pp. 103-106
    • Linden, T.1    Doutheil, J.2    Paschen, W.3
  • 26
    • 12544253089 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle. Role in cell survival
    • X.M. Liu, K.J. Peyton, D. Ensenat, H. Wang, A.I. Schafer, J. Alam, and W. Durante Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle. Role in cell survival J. Biol. Chem. 280 2005 872 877
    • (2005) J. Biol. Chem. , vol.280 , pp. 872-877
    • Liu, X.M.1    Peyton, K.J.2    Ensenat, D.3    Wang, H.4    Schafer, A.I.5    Alam, J.6    Durante, W.7
  • 28
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • K. Mori Tripartite management of unfolded proteins in the endoplasmic reticulum Cell 101 2000 451 454
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 29
    • 0026062165 scopus 로고
    • Enhanced NAD(P)H:quinone reductase activity prevents glutamate toxicity produced by oxidative stress
    • T.H. Murphy, M.J. De Long, and J.T. Coyle Enhanced NAD(P)H:quinone reductase activity prevents glutamate toxicity produced by oxidative stress J. Neurochem. 56 1991 990 995
    • (1991) J. Neurochem. , vol.56 , pp. 990-995
    • Murphy, T.H.1    De Long, M.J.2    Coyle, J.T.3
  • 30
    • 28844501852 scopus 로고    scopus 로고
    • Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins
    • K. Nakaso, C. Nakamura, H. Sato, K. Imamura, T. Takeshima, and K. Nakashima Novel cytoprotective mechanism of anti-parkinsonian drug deprenyl: PI3K and Nrf2-derived induction of antioxidative proteins Biochem. Biophys. Res. Commun. 339 2006 915 922
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 915-922
    • Nakaso, K.1    Nakamura, C.2    Sato, H.3    Imamura, K.4    Takeshima, T.5    Nakashima, K.6
  • 32
    • 20144378800 scopus 로고    scopus 로고
    • The oxidative stressor arsenite activates vascular endothelial growth factor mRNA transcription by an ATF4-dependent mechanism
    • C.N. Roybal, L.A. Hunsaker, O. Barbash, D.L. Vander Jagt, and S.F. Abcouwer The oxidative stressor arsenite activates vascular endothelial growth factor mRNA transcription by an ATF4-dependent mechanism J. Biol. Chem. 280 2005 20331 20339
    • (2005) J. Biol. Chem. , vol.280 , pp. 20331-20339
    • Roybal, C.N.1    Hunsaker, L.A.2    Barbash, O.3    Vander Jagt, D.L.4    Abcouwer, S.F.5
  • 33
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • E.J. Ryu, H.P. Harding, J.M. Angelastro, O.V. Vitolo, D. Ron, and L.A. Greene Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease J. Neurosci. 22 2002 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
  • 34
    • 0038529681 scopus 로고    scopus 로고
    • Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner
    • M. Salinas, R. Diaz, N.G. Abraham, C.M. Ruiz de Galarreta, and A. Cuadrado Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner J. Biol. Chem. 278 2003 13898 13904
    • (2003) J. Biol. Chem. , vol.278 , pp. 13898-13904
    • Salinas, M.1    Diaz, R.2    Abraham, N.G.3    Ruiz De Galarreta, C.M.4    Cuadrado, A.5
  • 37
    • 0035809930 scopus 로고    scopus 로고
    • Regulation of antioxidant metabolism by translation initiation factor 2α
    • S. Tan, N. Somia, P. Maher, and D. Schubert Regulation of antioxidant metabolism by translation initiation factor 2α J. Cell Biol. 152 2001 997 1006
    • (2001) J. Cell Biol. , vol.152 , pp. 997-1006
    • Tan, S.1    Somia, N.2    Maher, P.3    Schubert, D.4
  • 38
    • 0028171125 scopus 로고
    • EIF-2 kinases: Regulators of general and gene-specific translation initiation
    • R.C. Wek eIF-2 kinases: regulators of general and gene-specific translation initiation Trends Biochem. Sci. 19 1994 491 496
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 39
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of gamma-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • A.C. Wild, H.R. Moinova, and R.T. Mulcahy Regulation of gamma-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2 J. Biol. Chem. 274 1999 33627 33636
    • (1999) J. Biol. Chem. , vol.274 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 40
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • Z. Yu, H. Luo, W. Fu, and M.P. Mattson The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis Exp. Neurol. 155 1999 302 314
    • (1999) Exp. Neurol. , vol.155 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 41
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • DOI 10.1074/jbc.R400008200
    • K. Zhang, and R.J. Kaufman Signaling the unfolded protein response from the endoplasmic reticulum J. Biol. Chem. 279 2004 25935 25938 (Pubitemid 38798732)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.