메뉴 건너뛰기




Volumn 1817, Issue 3, 2012, Pages 401-409

Silencing of nicotinamide nucleotide transhydrogenase impairs cellular redox homeostasis and energy metabolism in PC12 cells

Author keywords

Apoptosis; Bioenergetics; JNK; Mitochondrion; Nicotinamide nucleotide transhydrogenase; Redox status

Indexed keywords

3 OXOACID COENZYME A TRANSFERASE; GLUTATHIONE; MITOCHONDRIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PYRUVATE DEHYDROGENASE; SMALL INTERFERING RNA; STRESS ACTIVATED PROTEIN KINASE; SUCCINYL COENZYME A;

EID: 84855815901     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.12.004     Document Type: Article
Times cited : (66)

References (40)
  • 1
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • DOI 10.1016/j.bbabio.2006.03.010, PII S000527280600065X
    • J. Rydstrom Mitochondrial NADPH, transhydrogenase and disease Biochim. Biophys. Acta 1757 2006 721 726 (Pubitemid 43993846)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 721-726
    • Rydstrom, J.1
  • 2
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • J.B. Hoek, and J. Rydstrom Physiological roles of nicotinamide nucleotide transhydrogenase Biochem. J. 254 1988 1 10
    • (1988) Biochem. J. , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydstrom, J.2
  • 3
    • 37549068090 scopus 로고    scopus 로고
    • NAD+/NADH and NADP+/NADPH in cellular functions and cell death: Regulation and biological consequences
    • W. Ying NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences Antioxid. Redox Signal. 10 2008 179 206
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 179-206
    • Ying, W.1
  • 4
    • 18844415919 scopus 로고    scopus 로고
    • A Caenorhabditis elegans mutant lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress
    • DOI 10.1016/j.freeradbiomed.2005.02.012, PII S0891584905000845
    • E.L. Arkblad, S. Tuck, N.B. Pestov, R.I. Dmitriev, M.B. Kostina, J. Stenvall, M. Tranberg, and J. Rydstrom A Caenorhabditis elegans mutant lacking functional nicotinamide nucleotide transhydrogenase displays increased sensitivity to oxidative stress Free Radic. Biol. Med. 38 2005 1518 1525 (Pubitemid 40693836)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.11 , pp. 1518-1525
    • Arkblad, E.L.1    Tuck, S.2    Pestov, N.B.3    Dmitriev, R.I.4    Kostina, M.B.5    Stenvall, J.6    Tranberg, M.7    Rydstrom, J.8
  • 6
    • 33645088824 scopus 로고    scopus 로고
    • Nicotinamide nucleotide transhydrogenase: A key role in insulin secretion
    • H. Freeman, K. Shimomura, E. Horner, R.D. Cox, and F.M. Ashcroft Nicotinamide nucleotide transhydrogenase: a key role in insulin secretion Cell Metab. 3 2006 35 45
    • (2006) Cell Metab. , vol.3 , pp. 35-45
    • Freeman, H.1    Shimomura, K.2    Horner, E.3    Cox, R.D.4    Ashcroft, F.M.5
  • 7
    • 37349081929 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons
    • DOI 10.1111/j.1471-4159.2007.04957.x
    • Q. Zhou, P.Y. Lam, D. Han, and E. Cadenas c-Jun N-terminal kinase regulates mitochondrial bioenergetics by modulating pyruvate dehydrogenase activity in primary cortical neurons J. Neurochem. 104 2008 325 335 (Pubitemid 350293865)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.2 , pp. 325-335
    • Zhou, Q.1    Lam, P.Y.2    Han, D.3    Cadenas, E.4
  • 8
    • 0037010847 scopus 로고    scopus 로고
    • Mitochondrial damage by nitric oxide is potentiated by dopamine in PC12 cells
    • DOI 10.1016/S0005-2728(02)00365-1, PII S0005272802003651
    • F. Antunes, D. Han, D. Rettori, and E. Cadenas Mitochondrial damage by nitric oxide is potentiated by dopamine in PC12 cells Biochim. Biophys. Acta 1556 2002 233 238 (Pubitemid 35379682)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1556 , Issue.2-3 , pp. 233-238
    • Antunes, F.1    Han, D.2    Rettori, D.3    Cadenas, E.4
  • 9
    • 77956210798 scopus 로고    scopus 로고
    • Determination of GSH, GSSG, and GSNO using HPLC with electrochemical detection
    • L.P. Yap, H. Sancheti, M.D. Ybanez, J. Garcia, E. Cadenas, and D. Han Determination of GSH, GSSG, and GSNO using HPLC with electrochemical detection Methods Enzymol. 473 2010 137 147
    • (2010) Methods Enzymol. , vol.473 , pp. 137-147
    • Yap, L.P.1    Sancheti, H.2    Ybanez, M.D.3    Garcia, J.4    Cadenas, E.5    Han, D.6
  • 10
    • 0029056469 scopus 로고
    • High-performance liquid chromatography analysis of oxidized and reduced pyridine dinucleotides in specific brain regions
    • L.K. Klaidman, A.C. Leung, and J.D. Adams Jr. High-performance liquid chromatography analysis of oxidized and reduced pyridine dinucleotides in specific brain regions Anal. Biochem. 228 1995 312 317
    • (1995) Anal. Biochem. , vol.228 , pp. 312-317
    • Klaidman, L.K.1    Leung, A.C.2    Adams, Jr.J.D.3
  • 11
    • 0036372619 scopus 로고    scopus 로고
    • Redox potential of GSH/GSSG couple: Assay and biological significance
    • DOI 10.1016/S0076-6879(02)48630-2, 11, Part B: Protein Sensors and Reactive Oxygen Species
    • D.P. Jones Redox potential of GSH/GSSG couple: assay and biological significance Methods Enzymol. 348 2002 93 112 (Pubitemid 41103102)
    • (2002) Methods in Enzymology , vol.348 , pp. 93-112
    • Jones, D.P.1
  • 12
    • 0030612749 scopus 로고    scopus 로고
    • 6(3) or rhodamine 123, is a reliable fluorescent probe to assess ΔΨ changes in intact cells: Implications for studies on mitochondrial functionality during apoptosis
    • DOI 10.1016/S0014-5793(97)00669-8, PII S0014579397006698
    • S. Salvioli, A. Ardizzoni, C. Franceschi, and A. Cossarizza JC-1, but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis FEBS Lett. 411 1997 77 82 (Pubitemid 27298375)
    • (1997) FEBS Letters , vol.411 , Issue.1 , pp. 77-82
    • Salvioli, S.1    Ardizzoni, A.2    Franceschi, C.3    Cossarizza, A.4
  • 13
    • 0014972144 scopus 로고
    • Activities of enzymes involved in acetoacetate utilization in adult mammalian tissues
    • D.H. Williamson, M.W. Bates, M.A. Page, and H.A. Krebs Activities of enzymes involved in acetoacetate utilization in adult mammalian tissues Biochem. J. 121 1971 41 47
    • (1971) Biochem. J. , vol.121 , pp. 41-47
    • Williamson, D.H.1    Bates, M.W.2    Page, M.A.3    Krebs, H.A.4
  • 14
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • A. Boveris, N. Oshino, and B. Chance The cellular production of hydrogen peroxide Biochem. J. 128 1972 617 630
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 15
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • A. Boveris, and B. Chance The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134 1973 707 716
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 18
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 1979 527 605 (Pubitemid 9236599)
    • (1979) Physiological Reviews , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 19
    • 0028971469 scopus 로고
    • The Pasteur effect in human platelets: Implications for storage and metabolic control
    • M. Guppy, L. Abas, P.G. Arthur, and M.E. Whisson The Pasteur effect in human platelets: implications for storage and metabolic control Br. J. Haematol. 91 1995 752 757
    • (1995) Br. J. Haematol. , vol.91 , pp. 752-757
    • Guppy, M.1    Abas, L.2    Arthur, P.G.3    Whisson, M.E.4
  • 20
    • 77953447516 scopus 로고    scopus 로고
    • Role of nitric oxide-mediated glutathionylation in neuronal function: Potential regulation of energy utilization
    • L.P. Yap, J.V. Garcia, D.S. Han, and E. Cadenas Role of nitric oxide-mediated glutathionylation in neuronal function: potential regulation of energy utilization Biochem. J. 428 2010 85 93
    • (2010) Biochem. J. , vol.428 , pp. 85-93
    • Yap, L.P.1    Garcia, J.V.2    Han, D.S.3    Cadenas, E.4
  • 21
    • 62849111251 scopus 로고    scopus 로고
    • Activation of c-Jun-N-terminal kinase and decline of mitochondrial pyruvate dehydrogenase activity during brain aging
    • Q. Zhou, P.Y. Lam, D. Han, and E. Cadenas Activation of c-Jun-N-terminal kinase and decline of mitochondrial pyruvate dehydrogenase activity during brain aging FEBS Lett. 583 2009 1132 1140
    • (2009) FEBS Lett. , vol.583 , pp. 1132-1140
    • Zhou, Q.1    Lam, P.Y.2    Han, D.3    Cadenas, E.4
  • 23
    • 0035905754 scopus 로고    scopus 로고
    • Down-regulation of the c-Jun N-terminal kinase (JNK) phosphatase M3/6 and activation of JNK by hydrogen peroxide and pyrrolidine
    • DOI 10.1038/sj.onc.1204105
    • Y.R. Chen, A. Shrivastava, and T.H. Tan Down-regulation of the c-Jun N-terminal kinase (JNK) phosphatase M3/6 and activation of JNK by hydrogen peroxide and pyrrolidine dithiocarbamate Oncogene 20 2001 367 374 (Pubitemid 32142326)
    • (2001) Oncogene , vol.20 , Issue.3 , pp. 367-374
    • Chen, Y.-R.1    Shrivastava, A.2    Tan, T.-H.3
  • 25
    • 0033826520 scopus 로고    scopus 로고
    • Role for mitochondrial oxidants as regulators of cellular metabolism
    • S. Nemoto, K. Takeda, Z.X. Yu, V.J. Ferrans, and T. Finkel Role for mitochondrial oxidants as regulators of cellular metabolism Mol. Cell. Biol. 20 2000 7311 7318
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7311-7318
    • Nemoto, S.1    Takeda, K.2    Yu, Z.X.3    Ferrans, V.J.4    Finkel, T.5
  • 26
    • 0036139987 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase signaling pathway by the mixed lineage kinase inhibitor CEP-1347 (KT7515) preserves metabolism and growth of trophic factor-deprived neurons
    • C.A. Harris, M. Deshmukh, B. Tsui-Pierchala, A.C. Maroney, and E.M.J. Johnson Inhibition of the c-Jun N-terminal kinase signaling pathway by the mixed lineage kinase inhibitor CEP-1347 (KT7515) preserves metabolism and growth of trophic factor-deprived neurons J. Neurosci. 22 2002 103 113 (Pubitemid 34033488)
    • (2002) Journal of Neuroscience , vol.22 , Issue.1 , pp. 103-113
    • Harris, C.A.1    Deshmukh, M.2    Tsui-Pierchala, B.3    Maroney, A.C.4    Johnson Jr., E.M.5
  • 27
    • 0033198217 scopus 로고    scopus 로고
    • BAX translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, BCL-2, and caspases
    • G.V. Putcha, M. Deshmukh, and E.M.J. Johnson BAX translocation is a critical event in neuronal apoptosis: regulation by neuroprotectants, BCL-2, and caspases J. Neurosci. 19 1999 7476 7485 (Pubitemid 29404604)
    • (1999) Journal of Neuroscience , vol.19 , Issue.17 , pp. 7476-7485
    • Putcha, G.V.1    Deshmukh, M.2    Johnson Jr., E.M.3
  • 29
    • 0038677013 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK)-mediated modulation of brain mitochondria function: New target proteins for JNK signalling in mitochondrion-dependent apoptosis
    • DOI 10.1042/BJ20030201
    • H. Schroeter, C.S. Boyd, R. Ahmed, J.P. Spencer, R.F. Duncan, C. Rice-Evans, and E. Cadenas c-Jun N-terminal kinase (JNK)-mediated modulation of brain mitochondria function: new target proteins for JNK signalling in mitochondrion-dependent apoptosis Biochem. J. 372 2003 359 369 (Pubitemid 36723881)
    • (2003) Biochemical Journal , vol.372 , Issue.2 , pp. 359-369
    • Schroeter, H.1    Boyd, C.S.2    Ahmed, R.3    Spencer, J.P.E.4    Duncan, R.F.5    Rice-Evans, C.6    Cadenas, E.7
  • 30
    • 77953810393 scopus 로고    scopus 로고
    • Diminished NADPH transhydrogenase activity and mitochondrial redox regulation in human failing myocardium
    • F.L. Sheeran, J. Rydstrom, M.I. Shakhparonov, N.B. Pestov, and S. Pepe Diminished NADPH transhydrogenase activity and mitochondrial redox regulation in human failing myocardium Biochim. Biophys. Acta 1797 2010 1138 1148
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1138-1148
    • Sheeran, F.L.1    Rydstrom, J.2    Shakhparonov, M.I.3    Pestov, N.B.4    Pepe, S.5
  • 31
    • 71549131281 scopus 로고    scopus 로고
    • The energy-redox axis in aging and age-related neurodegeneration
    • L.P. Yap, J.V. Garcia, D. Han, and E. Cadenas The energy-redox axis in aging and age-related neurodegeneration Adv. Drug Deliv. Rev. 61 2009 1283 1298
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 1283-1298
    • Yap, L.P.1    Garcia, J.V.2    Han, D.3    Cadenas, E.4
  • 32
    • 78650068036 scopus 로고    scopus 로고
    • Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates
    • J. Garcia, D. Han, H. Sancheti, L.P. Yap, N. Kaplowitz, and E. Cadenas Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates J. Biol. Chem. 285 2010 39646 39654
    • (2010) J. Biol. Chem. , vol.285 , pp. 39646-39654
    • Garcia, J.1    Han, D.2    Sancheti, H.3    Yap, L.P.4    Kaplowitz, N.5    Cadenas, E.6
  • 33
    • 67650134121 scopus 로고    scopus 로고
    • Elevated neuronal nitric oxide synthase expression during ageing and mitochondrial energy production
    • P.Y. Lam, F. Yin, R.T. Hamilton, A. Boveris, and E. Cadenas Elevated neuronal nitric oxide synthase expression during ageing and mitochondrial energy production Free. Radic. Res. 43 2009 431 439
    • (2009) Free. Radic. Res. , vol.43 , pp. 431-439
    • Lam, P.Y.1    Yin, F.2    Hamilton, R.T.3    Boveris, A.4    Cadenas, E.5
  • 34
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • J. Yao, R.W. Irwin, L. Zhao, J. Nilsen, R.T. Hamilton, and R.D. Brinton Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease Proc. Natl. Acad. Sci. U. S. A. 106 2009 14670 14675
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 35
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • M.T. Lin, and M.F. Beal Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases Nature 443 2006 787 795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 37
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • DOI 10.1126/science.1104343
    • B.B. Lowell, and G.I. Shulman Mitochondrial dysfunction and type 2 diabetes Science 307 2005 384 387 (Pubitemid 40139974)
    • (2005) Science , vol.307 , Issue.5708 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2
  • 38
    • 33645299025 scopus 로고    scopus 로고
    • Ageing and neuronal vulnerability
    • M.P. Mattson, and T. Magnus Ageing and neuronal vulnerability Nat. Rev. Neurosci. 7 2006 278 294
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 278-294
    • Mattson, M.P.1    Magnus, T.2
  • 39
    • 64949111531 scopus 로고    scopus 로고
    • Current thoughts on the role of mitochondria and free radicals in the biology of aging
    • H. Van Remmen, and D.P. Jones Current thoughts on the role of mitochondria and free radicals in the biology of aging J. Gerontol. A Biol. Sci. Med. Sci. 64 2009 171 174
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 171-174
    • Van Remmen, H.1    Jones, D.P.2
  • 40
    • 33847059997 scopus 로고    scopus 로고
    • The mitochondrial energy transduction system and the aging process
    • A. Navarro, and A. Boveris The mitochondrial energy transduction system and the aging process Am. J. Physiol. Cell Physiol. 292 2007 C670 C686
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Navarro, A.1    Boveris, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.