Cysteine Modifications in the Pathogenesis of ALS
Tóm tắt
Từ khóa
Tài liệu tham khảo
Antinone, 2013, Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants, J. Biol. Chem., 288, 21606, 10.1074/jbc.M113.487231
Atkin, 2006, Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1, J. Biol. Chem., 281, 30152, 10.1074/jbc.M603393200
Atkin, 2008, Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis, Neurobiol. Dis., 30, 400, 10.1016/j.nbd.2008.02.009
Banci, 2012, Interaction of cisplatin with human superoxide dismutase, J. Am. Chem. Soc., 134, 7009, 10.1021/ja211591n
Banci, 2008, SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization, PLoS One, 3, e1677, 10.1371/journal.pone.0001677
Barber, 2010, Oxidative stress in ALS: key role in motor neuron injury and therapeutic target, Free Radic. Biol. Med., 48, 629, 10.1016/j.freeradbiomed.2009.11.018
Benhar, 2006, Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases, ACS Chem. Biol., 1, 355, 10.1021/cb600244c
Bernardoni, 2013, Reticulon1-C modulates protein disulphide isomerase function, Cell Death Dis., 4, e581, 10.1038/cddis.2013.113
Bozzo, 2016, Structural insights into the multi-determinant aggregation of TDP-43 in motor neuron-like cells, Neurobiol. Dis., 94, 63, 10.1016/j.nbd.2016.06.006
Cai, 1994, Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds, J. Biol. Chem., 269, 24550, 10.1016/S0021-9258(17)31426-6
Cardaci, 2012, Redox implications of AMPK-mediated signal transduction beyond energetic clues, J. Cell Sci., 125, 2115, 10.1242/jcs.095216
Chambers, 2014, Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress, Am. J. Physiol. Cell Physiol., 307, C657, 10.1152/ajpcell.00183.2014
Chang, 2013, Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function, FEBS Lett., 587, 575, 10.1016/j.febslet.2013.01.038
Chatzi, 2016, Oxidative folding in the mitochondrial intermembrane space: a regulated process important for cell physiology and disease, Biochim. Biophys. Acta, 1863, 1298, 10.1016/j.bbamcr.2016.03.023
Chen, 2013, S-nitrosylated protein disulfide isomerase contributes to mutant SOD1 aggregates in amyotrophic lateral sclerosis, J. Neurochem., 124, 45, 10.1111/jnc.12046
Cohen, 2012, Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking, EMBO J., 31, 1241, 10.1038/emboj.2011.471
Cozzolino, 2008, Amyotrophic lateral sclerosis: from current developments in the laboratory to clinical implications, Antioxid. Redox Signal., 10, 405, 10.1089/ars.2007.1760
Cozzolino, 2009, Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity, Antioxid. Redox Signal., 11, 1547, 10.1089/ARS.2009.2545
Ellgaard, 2005, The human protein disulphide isomerase family: substrate interactions and functional properties, EMBO Rep., 6, 28, 10.1038/sj.embor.7400311
Farg, 2012, Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase, Neurobiol. Aging, 33, 2855, 10.1016/j.neurobiolaging.2012.02.009
Feige, 2011, Disulfide bonds in ER protein folding and homeostasis, Curr. Opin. Cell Biol., 23, 167, 10.1016/j.ceb.2010.10.012
Ferguson, 2016, Glutamate cysteine ligase and the age-related decline in cellular glutathione: the therapeutic potential of γ-glutamylcysteine, Arch. Biochem. Biophys., 593, 12, 10.1016/j.abb.2016.01.017
Ferri, 2006, Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials, Proc. Natl. Acad. Sci. U S A, 103, 13860, 10.1073/pnas.0605814103
Ferri, 2010, Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity, Hum. Mol. Genet., 19, 4529, 10.1093/hmg/ddq383
Forman, 2016, Redox signaling: an evolution from free radicals to aging, Free Radic. Biol. Med., 97, 398, 10.1016/j.freeradbiomed.2016.07.003
Di Giacomo, 2012, Established principles and emerging concepts on the interplay between mitochondrial physiology and S-(De)nitrosylation: implications in cancer and neurodegeneration, Int. J. Cell Biol., 2012, 361872, 10.1155/2012/361872
Gonzalez-Perez, 2015, Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients, Gene, 566, 158, 10.1016/j.gene.2015.04.035
Grek, 2013, Causes and consequences of cysteine S-glutathionylation, J. Biol. Chem., 288, 26497, 10.1074/jbc.r113.461368
Hess, 2005, Protein S-nitrosylation: purview and parameters, Nat. Rev. Mol. Cell Biol., 6, 150, 10.1038/nrm1569
Hoffstrom, 2010, Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins, Nat. Chem. Biol., 6, 900, 10.1038/nchembio.467
Honjo, 2011, Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis, Amyotroph. Lateral Scler., 12, 444, 10.3109/17482968.2011.594055
Iguchi, 2012, Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies, Neurobiol. Dis., 45, 862, 10.1016/j.nbd.2011.12.002
Jeon, 2015, The double-edged sword of AMPK signaling in cancer and its therapeutic implications, Arch. Pharm. Res., 38, 346, 10.1007/s12272-015-0549-z
Jeon, 2014, Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis, Mol. Neurobiol., 49, 796, 10.1007/s12035-013-8562-z
Jones, 2008, Radical-free biology of oxidative stress, Am. J. Physiol. Cell Physiol., 295, C849, 10.1152/ajpcell.00283.2008
Karch, 2009, Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS, Proc. Natl. Acad. Sci. U S A, 106, 7774, 10.1073/pnas.0902505106
Kawamata, 2010, Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space, Antioxid. Redox Signal., 13, 1375, 10.1089/ars.2010.3212
Kwok, 2013, Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis, Free Radic. Biol. Med., 58, 81, 10.1016/j.freeradbiomed.2013.01.001
Lee, 2011, Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration, Nat. Rev. Neurosci., 13, 38, 10.1038/nrn3121
Levental, 2010, Palmitoylation regulates raft affinity for the majority of integral raft proteins, Proc. Natl. Acad. Sci. U S A, 107, 22050, 10.1073/pnas.1016184107
Li, 2013, Oxidative stress and neurodegenerative disorders, Int. J. Mol. Sci., 14, 24438, 10.3390/ijms141224438
Lim, 2012, Reduced activity of AMP-activated protein kinase protects against genetic models of motor neuron disease, J. Neurosci., 32, 1123, 10.1523/JNEUROSCI.6554-10.2012
Liu, 2015, Activation of AMP-activated protein kinase α1 mediates mislocalization of TDP-43 in amyotrophic lateral sclerosis, Hum. Mol. Genet., 24, 787, 10.1093/hmg/ddu497
Liu, 2005, Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system, Protein Expr. Purif., 44, 155, 10.1016/j.pep.2005.03.030
Mårtensson, 1990, Glutathione is required for intestinal function, Proc. Natl. Acad. Sci. U S A, 87, 1715, 10.1073/pnas.87.5.1715
Matus, 2013, ER dysfunction and protein folding stress in ALS, Int. J. Cell Biol., 2013, 674751, 10.1155/2013/674751
McAlary, 2013, Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis, Sci. Rep., 3, 3275, 10.1038/srep03275
Meister, 1988, Glutathione metabolism and its selective modification, J. Biol. Chem., 263, 17205, 10.1016/S0021-9258(19)77815-6
Mieyal, 2008, Molecular mechanisms and clinical implications of reversible protein S-glutathionylation, Antioxid. Redox Signal., 10, 1941, 10.1089/ars.2008.2089
Mordas, 2015, The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis, Acc. Chem. Res., 48, 2191, 10.1021/acs.accounts.5b00150
Nakamura, 2013, Aberrant protein S-nitrosylation in neurodegenerative diseases, Neuron, 78, 596, 10.1016/j.neuron.2013.05.005
Nardo, 2011, Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells, PLoS One, 6, e25545, 10.1371/journal.pone.0025545
Neumann, 2006, Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis, Science, 314, 130, 10.1126/science.1134108
Niwa, 2007, Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1, J. Biol. Chem., 282, 28087, 10.1074/jbc.m704465200
Oka, 2013, Forming disulfides in the endoplasmic reticulum, Biochim. Biophys. Acta, 1833, 2425, 10.1016/j.bbamcr.2013.02.007
Parakh, 2015, Novel roles for protein disulphide isomerase in disease states: a double edged sword?, Front. Cell Dev. Biol., 3, 30, 10.3389/fcell.2015.00030
Perera, 2014, Mutant TDP-43 deregulates AMPK activation by PP2A in ALS models, PLoS One, 9, e95549, 10.1371/journal.pone.0095549
Peters, 2015, Emerging mechanisms of molecular pathology in ALS, J. Clin. Invest., 125, 2548, 10.1172/JCI82693
Redler, 2011, Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers, Biochemistry, 50, 7057, 10.1021/bi200614y
Renton, 2014, State of play in amyotrophic lateral sclerosis genetics, Nat. Neurosci., 17, 17, 10.1038/nn.3584
Rizza, 2015, S-nitrosoglutathione reductase plays opposite roles in SH-SY5Y models of Parkinson’s disease and amyotrophic lateral sclerosis, Mediators Inflamm., 2015, 536238, 10.1155/2015/536238
Robberecht, 2013, The changing scene of amyotrophic lateral sclerosis, Nat. Rev. Neurosci., 14, 248, 10.1038/nrn3430
Rutkevich, 2010, Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins, Mol. Biol. Cell, 21, 3093, 10.1091/mbc.E10-04-0356
Sasaki, 1994, Synapse loss in anterior horn neurons in amyotrophic lateral sclerosis, Acta Neuropathol., 88, 222, 10.1007/s004010050153
Schonhoff, 2006, S-nitrosothiol depletion in amyotrophic lateral sclerosis, Proc. Natl. Acad. Sci. U S A, 103, 2404, 10.1073/pnas.0507243103
Shodai, 2013, Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43), J. Biol. Chem., 288, 14886, 10.1074/jbc.M113.451849
Stoica, 2014, ER–mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43, Nat. Commun., 5, 3996, 10.1038/ncomms4996
Stoica, 2016, ALS/FTD-associated FUS activates GSK-3β to disrupt the VAPB-PTPIP51 interaction and ER-mitochondria associations, EMBO Rep., 17, 1326, 10.15252/embr.201541726
Sui, 2014, Adenosine monophosphate-activated protein kinase activation enhances embryonic neural stem cell apoptosis in a mouse model of amyotrophic lateral sclerosis, Neural Regen. Res., 9, 1770, 10.4103/1673-5374.143421
Sun, 2006, Hypoxia facilitates Alzheimer’s disease pathogenesis by up-regulating BACE1 gene expression, Proc. Natl. Acad. Sci. U S A, 103, 18727, 10.1073/pnas.0606298103
Tsuda, 2008, The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors, Cell, 133, 963, 10.1016/j.cell.2008.04.039
Walker, 2010, Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis, J. Neurosci., 30, 3865, 10.1523/JNEUROSCI.0408-10.2010
Walker, 2010, Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis, Brain, 133, 105, 10.1093/brain/awp267
Walker, 2015, An insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic mice, Hum. Mol. Genet., 24, 7241, 10.1093/hmg/ddv424
Walter, 2011, The unfolded protein response: from stress pathway to homeostatic regulation, Science, 334, 1081, 10.1126/science.1209038
Wiedemann, 2002, Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients, J. Neurochem., 80, 616, 10.1046/j.0022-3042.2001.00731.x
Wilcox, 2009, Modifications of superoxide dismutase (SOD1) in human erythrocytes: a possible role in amyotrophic lateral sclerosis, J. Biol. Chem., 284, 13940, 10.1074/jbc.M809687200
Woehlbier, 2016, ALS-linked protein disulfide isomerase variants cause motor dysfunction, EMBO J., 35, 845, 10.15252/embj.201592224
Xiong, 2011, S-glutathionylation: from molecular mechanisms to health outcomes, Antioxid. Redox Signal., 15, 233, 10.1089/ars.2010.3540
Yang, 2016, Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population, Int. J. Neurosci., 126, 607, 10.3109/00207454.2015.1050098
Yang, 2009, Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis, J. Neurosci., 29, 13850, 10.1523/JNEUROSCI.2312-09.2009
Zhao, 2015, Proapoptotic activities of protein disulfide isomerase (PDI) and PDIA3 protein, a role of the Bcl-2 protein Bak, J. Biol. Chem., 290, 8949, 10.1074/jbc.M114.619353