메뉴 건너뛰기




Volumn 72, Issue 1, 2012, Pages 94-102

Inhibition of mitochondrial permeability transition pore opening is involved in the protective effects of mortalin overexpression against beta-amyloid-induced apoptosis in SH-SY5Y cells

Author keywords

Amyloid; Alzheimer's disease; Apoptosis; Mitochondrial permeability transition; Mortalin; SH SY5Y cells

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; CALCIUM; CASPASE 3; CYTOCHROME C; HEAT SHOCK PROTEIN 70; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MORTALIN; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 83155181415     PISSN: 01680102     EISSN: 18728111     Source Type: Journal    
DOI: 10.1016/j.neures.2011.09.009     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 2342431848 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I
    • Batandier C., Leverve X., Fontaine E. Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I. J. Biol. Chem. 2004, 279:17197-17204.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17197-17204
    • Batandier, C.1    Leverve, X.2    Fontaine, E.3
  • 3
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E., Newmeyer D.D., Green D.R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J. 1998, 17:37-49.
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 4
    • 7744224359 scopus 로고    scopus 로고
    • Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases
    • Breckenridge D.G., Xue D. Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases. Curr. Opin. Cell Biol. 2004, 16:647-652.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 647-652
    • Breckenridge, D.G.1    Xue, D.2
  • 5
    • 67649400331 scopus 로고    scopus 로고
    • Taurine protects transformed rat retinal ganglion cells from hypoxia-induced apoptosis by preventing mitochondrial dysfunction
    • Chen K., Zhang Q., Wang J., Liu F., Mi M., Xu H., Chen F., Zeng K. Taurine protects transformed rat retinal ganglion cells from hypoxia-induced apoptosis by preventing mitochondrial dysfunction. Brain Res. 2009, 1279:131-138.
    • (2009) Brain Res. , vol.1279 , pp. 131-138
    • Chen, K.1    Zhang, Q.2    Wang, J.3    Liu, F.4    Mi, M.5    Xu, H.6    Chen, F.7    Zeng, K.8
  • 6
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 1999, 341(Pt 2):233-249.
    • (1999) Biochem. J. , vol.341 , Issue.PART 2 , pp. 233-249
    • Crompton, M.1
  • 8
    • 33846019607 scopus 로고    scopus 로고
    • Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes
    • David D.C., Ittner L.M., Gehrig P., Nergenau D., Shepherd C., Halliday G., Gotz J. Beta-amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes. Proteomics 2006, 6:6566-6577.
    • (2006) Proteomics , vol.6 , pp. 6566-6577
    • David, D.C.1    Ittner, L.M.2    Gehrig, P.3    Nergenau, D.4    Shepherd, C.5    Halliday, G.6    Gotz, J.7
  • 9
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud A., Sharaf el dein O., Maillier E., Poncet D., Kroemer G., Lemaire C., Brenner C. Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 2008, 27:285-299.
    • (2008) Oncogene , vol.27 , pp. 285-299
    • Deniaud, A.1    Sharaf el dein, O.2    Maillier, E.3    Poncet, D.4    Kroemer, G.5    Lemaire, C.6    Brenner, C.7
  • 10
    • 72149118206 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta
    • Du H., Yan S.S. Mitochondrial permeability transition pore in Alzheimer's disease: cyclophilin D and amyloid beta. Biochim. Biophys. Acta 2010, 1802:198-204.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 198-204
    • Du, H.1    Yan, S.S.2
  • 11
    • 34247555454 scopus 로고    scopus 로고
    • Response to bistability in apoptosis: roles of bax, bcl-2, and mitochondrial permeability transition pores
    • Eissing T., Waldherr S., Allgower F., Scheurich P., Bullinger E. Response to bistability in apoptosis: roles of bax, bcl-2, and mitochondrial permeability transition pores. Biophys. J. 2007, 92:3332-3334.
    • (2007) Biophys. J. , vol.92 , pp. 3332-3334
    • Eissing, T.1    Waldherr, S.2    Allgower, F.3    Scheurich, P.4    Bullinger, E.5
  • 12
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • Ferreiro E., Oliveira C.R., Pereira C.M. The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol. Dis. 2008, 30:331-342.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.M.3
  • 13
    • 0032876784 scopus 로고    scopus 로고
    • Activation of caspase-3 in [beta]-amyloid-induced apoptosis of cultured rat cortical neurons
    • Harada J., Sugimoto M. Activation of caspase-3 in [beta]-amyloid-induced apoptosis of cultured rat cortical neurons. Brain Res. 1999, 842:311-323.
    • (1999) Brain Res. , vol.842 , pp. 311-323
    • Harada, J.1    Sugimoto, M.2
  • 14
    • 34547138950 scopus 로고    scopus 로고
    • Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis
    • Hua G., Zhang Q., Fan Z. Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis. J. Biol. Chem. 2007, 282:20553-20560.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20553-20560
    • Hua, G.1    Zhang, Q.2    Fan, Z.3
  • 15
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue
    • Kaneko I., Yamada N., Sakuraba Y., Kamenosono M., Tutumi S. Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue. J. Neurochem. 1995, 65:2585-2593.
    • (1995) J. Neurochem. , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Sakuraba, Y.3    Kamenosono, M.4    Tutumi, S.5
  • 16
    • 33847651284 scopus 로고    scopus 로고
    • Three faces of mortalin: a housekeeper, guardian and killer
    • Kaul S.C., Deocaris C.C., Wadhwa R. Three faces of mortalin: a housekeeper, guardian and killer. Exp. Gerontol. 2007, 42:263-274.
    • (2007) Exp. Gerontol. , vol.42 , pp. 263-274
    • Kaul, S.C.1    Deocaris, C.C.2    Wadhwa, R.3
  • 17
    • 0037427440 scopus 로고    scopus 로고
    • Mitochondrial permeability transition: a common pathway to necrosis and apoptosis
    • Kim J.S., He L., Lemasters J.J. Mitochondrial permeability transition: a common pathway to necrosis and apoptosis. Biochem. Biophys. Res. Commun. 2003, 304:463-470.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 463-470
    • Kim, J.S.1    He, L.2    Lemasters, J.J.3
  • 18
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu Q., D'Silva P., Walter W., Marszalek J., Craig E.A. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 2003, 300:139-141.
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 20
    • 0026570528 scopus 로고
    • Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 1992, 12:376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 21
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid beta-peptide promotes permeability transition pore in brain mitochondria
    • Moreira P.I., Santos M.S., Moreno A., Oliveira C. Amyloid beta-peptide promotes permeability transition pore in brain mitochondria. Biosci. Rep. 2001, 21:789-800.
    • (2001) Biosci. Rep. , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 22
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., Chittenden T., Lutz R.J., Matsuda H., Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:14681-14686.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 24
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon J.W., Olzmann J.A., Chin L.S., Li L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 2007, 5:e172.
    • (2007) PLoS Biol. , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 25
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells
    • Qu M., Zhou Z., Xu S., Chen C., Yu Z., Wang D. Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells. Brain Res. 2011, 1368:336-345.
    • (2011) Brain Res. , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5    Wang, D.6
  • 26
    • 79953716813 scopus 로고    scopus 로고
    • Effect of beta-amyloid (25-35) on mitochondrial function and expression of mitochondrial permeability transition pore proteins in rat hippocampal neurons
    • Ren R., Zhang Y., Li B., Wu Y. Effect of beta-amyloid (25-35) on mitochondrial function and expression of mitochondrial permeability transition pore proteins in rat hippocampal neurons. J. Cell Biochem. 2011.
    • (2011) J. Cell Biochem.
    • Ren, R.1    Zhang, Y.2    Li, B.3    Wu, Y.4
  • 27
    • 0036257364 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74
    • Schwarzer C., Barnikol-Watanabe S., Thinnes F.P., Hilschmann N. Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74. Int. J. Biochem. Cell Biol. 2002, 34:1059-1070.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1059-1070
    • Schwarzer, C.1    Barnikol-Watanabe, S.2    Thinnes, F.P.3    Hilschmann, N.4
  • 28
    • 0030923869 scopus 로고    scopus 로고
    • Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease
    • Sheehan J.P., Swerdlow R.H., Miller S.W., Davis R.E., Parks J.K., Parker W.D., Tuttle J.B. Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease. J. Neurosci. 1997, 17:4612-4622.
    • (1997) J. Neurosci. , vol.17 , pp. 4612-4622
    • Sheehan, J.P.1    Swerdlow, R.H.2    Miller, S.W.3    Davis, R.E.4    Parks, J.K.5    Parker, W.D.6    Tuttle, J.B.7
  • 31
    • 78649983748 scopus 로고    scopus 로고
    • Alzheimer's disease: effects of [beta]-amyloid on mitochondria
    • Tillement L., Lecanu L., Papadopoulos V. Alzheimer's disease: effects of [beta]-amyloid on mitochondria. Mitochondrion 2011, 11:13-21.
    • (2011) Mitochondrion , vol.11 , pp. 13-21
    • Tillement, L.1    Lecanu, L.2    Papadopoulos, V.3
  • 32
    • 34247158550 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
    • Trushina E., McMurray C.T. Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases. Neuroscience 2007, 145:1233-1248.
    • (2007) Neuroscience , vol.145 , pp. 1233-1248
    • Trushina, E.1    McMurray, C.T.2
  • 33
    • 0036791842 scopus 로고    scopus 로고
    • Mortalin: a potential candidate for biotechnology and biomedicine
    • Wadhwa R., Taira K., Kaul S.C. Mortalin: a potential candidate for biotechnology and biomedicine. Histol. Histopathol. 2002, 17:1173-1177.
    • (2002) Histol. Histopathol. , vol.17 , pp. 1173-1177
    • Wadhwa, R.1    Taira, K.2    Kaul, S.C.3
  • 34
    • 0032877433 scopus 로고    scopus 로고
    • Bax:Bcl-2 ratio modulation by bryostatin 1 and novel antitubulin agents is important for susceptibility to drug induced apoptosis in the human early pre-B acute lymphoblastic leukemia cell line
    • Wall N.R., Mohammad R.M., Al-Katib A.M. Bax:Bcl-2 ratio modulation by bryostatin 1 and novel antitubulin agents is important for susceptibility to drug induced apoptosis in the human early pre-B acute lymphoblastic leukemia cell line. Reh. Leuk. Res. 1999, 23:881-888.
    • (1999) Reh. Leuk. Res. , vol.23 , pp. 881-888
    • Wall, N.R.1    Mohammad, R.M.2    Al-Katib, A.M.3
  • 35
    • 67651111698 scopus 로고    scopus 로고
    • Acteoside protects human neuroblastoma SH-SY5Y cells against [beta]-amyloid-induced cell injury
    • Wang H., Xu Y., Yan J., Zhao X., Sun X., Zhang Y., Guo J., Zhu C. Acteoside protects human neuroblastoma SH-SY5Y cells against [beta]-amyloid-induced cell injury. Brain Res. 2009, 1283:139-147.
    • (2009) Brain Res. , vol.1283 , pp. 139-147
    • Wang, H.1    Xu, Y.2    Yan, J.3    Zhao, X.4    Sun, X.5    Zhang, Y.6    Guo, J.7    Zhu, C.8
  • 37
    • 77950474141 scopus 로고    scopus 로고
    • Mitochondrial chaperone tumour necrosis factor receptor-associated protein 1 protects cardiomyocytes from hypoxic injury by regulating mitochondrial permeability transition pore opening
    • Xiang F., Huang Y.S., Shi X.H., Zhang Q. Mitochondrial chaperone tumour necrosis factor receptor-associated protein 1 protects cardiomyocytes from hypoxic injury by regulating mitochondrial permeability transition pore opening. FEBS J. 2010, 277:1929-1938.
    • (2010) FEBS J. , vol.277 , pp. 1929-1938
    • Xiang, F.1    Huang, Y.S.2    Shi, X.H.3    Zhang, Q.4
  • 38
    • 78651092395 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia
    • Xu L., Voloboueva L.A., Ouyang Y., Emery J.F., Giffard R.G. Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J. Cereb. Blood Flow Metab. 2008.
    • (2008) J. Cereb. Blood Flow Metab.
    • Xu, L.1    Voloboueva, L.A.2    Ouyang, Y.3    Emery, J.F.4    Giffard, R.G.5
  • 39
    • 77954318391 scopus 로고    scopus 로고
    • Melatonin protects against nickel-induced neurotoxicity in vitro by reducing oxidative stress and maintaining mitochondrial function
    • Xu S.C., He M.D., Zhong M., Zhang Y.W., Wang Y., Yang L., Yang J., Yu Z.P., Zhou Z. Melatonin protects against nickel-induced neurotoxicity in vitro by reducing oxidative stress and maintaining mitochondrial function. J. Pineal Res. 2010, 49:86-94.
    • (2010) J. Pineal Res. , vol.49 , pp. 86-94
    • Xu, S.C.1    He, M.D.2    Zhong, M.3    Zhang, Y.W.4    Wang, Y.5    Yang, L.6    Yang, J.7    Yu, Z.P.8    Zhou, Z.9
  • 40
    • 42449116100 scopus 로고    scopus 로고
    • Glucose-regulated protein 75 suppresses apoptosis induced by glucose deprivation in PC12 cells through inhibition of Bax conformational change
    • Yang L., Liu X.Y., Hao J.Y., Yang Y.L., Zhao M.X., Zuo J., Liu W. Glucose-regulated protein 75 suppresses apoptosis induced by glucose deprivation in PC12 cells through inhibition of Bax conformational change. Acta Biochim. Biophys. Sin. 2008, 40:339-348.
    • (2008) Acta Biochim. Biophys. Sin. , vol.40 , pp. 339-348
    • Yang, L.1    Liu, X.Y.2    Hao, J.Y.3    Yang, Y.L.4    Zhao, M.X.5    Zuo, J.6    Liu, W.7
  • 41
    • 0038359753 scopus 로고    scopus 로고
    • Involvement of cytochrome c release and caspase-3 activation in the oxidative stress-induced apoptosis in human tendon fibroblasts
    • Yuan J., Murrell G.A., Trickett A., Wang M.X. Involvement of cytochrome c release and caspase-3 activation in the oxidative stress-induced apoptosis in human tendon fibroblasts. Biochim. Biophys. Acta 2003, 1641:35-41.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 35-41
    • Yuan, J.1    Murrell, G.A.2    Trickett, A.3    Wang, M.X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.