Endoplasmic reticulum dysfunction in neurological disease

Roussel, Benoit D; Kruppa, Antonina J; Miranda, Elena; Crowther, Damian C; Lomas, David A; Marciniak, Stefan J

doi:10.1016/s1474-4422(12)70238-7

Cited by 448Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchGenetic Neurodegenerative Diseases

Endoplasmic reticulum dysfunction in neurological disease

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Roussel, Benoit D, Kruppa, Antonina J, Miranda, Elena, Crowther, Damian C, Lomas, David A, Marciniak, Stefan J·2013·The Lancet Neurology

DOI 10.1016/s1474-4422(12)70238-7

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Abstract

Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible.

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Autosomal-dominant mutations in neuroserpin cause familial encephalopathy with Neuroserpin inclusion bodies, a rare, early-onset neurodegenerative dementia caused by protein aggregation within the ER and associated ER stress.
“Autosomal-dominant mutations in neuroserpin cause familial encephalopathy with Neuroserpin inclusion bodies, a rare, early-onset neurodegenerative dementia caused by protein aggregation within the endoplasmic reticulum (ER) and associated ER stress (Roussel et al., 2013).”
From Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models (2020) · cites this paper as Roussel et al., 2013
Previous work has linked disruptions to autophagy and lysosomal biology with AD.
“Previous work has linked disruptions to autophagy and lysosomal biology with AD72–74.”
From APOE genotypes differentially remodel the astrocytic lipid droplet proteome to shape lipid droplet dynamics (2026) · cites this paper as [74]

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Xue, Y., Daly, A., Yngvadóttir, B., Liu, M., Coop, G., Kim, Y., Sabeti, P. C., Chen, Y., Stalker, J., Huckle, E. J., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/503116 · Cited by 159 · see citing works
Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
Reijonen, S., Putkonen, N., Nørremølle, A., Lindholm, D., & Korhonen, L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.12.025 · Cited by 155 · see citing works
Protective effect against Parkinson's disease-related insults through the activation of XBP1
Sado, M., Yamasaki, Y., Iwanaga, T., Onaka, Y., Ibuki, T., Nishihara, S., Mizuguchi, H., Momota, H., Kishibuchi, R., Hashimoto, T., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.11.104 · Cited by 153 · see citing works
ER stress is involved in Aβ‐induced GSK‐3β activation and tau phosphorylation
Resende, R., Ferreiro, E. B., Pereira, C., & Oliveira, C. R. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21648 · Cited by 142 · see citing works
Endoplasmic Reticulum-associated Degradation (ERAD) and Autophagy Cooperate to Degrade Polymerogenic Mutant Serpins
Kroeger, H., Miranda, E., Ian, M., Pérez, J., Crowther, D. C., Marciniak, S. J., & Lomas, D. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027102 · Cited by 141 · see citing works
Self-citation
The Endoplasmic Reticulum Stress Sensor, ATF6α, Protects against Neurotoxin-induced Dopaminergic Neuronal Death
Egawa, N., Yamamoto, K., Inoue, H., Hikawa, R., Nishi, K., Mori, K., & Takahashi, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156430 · Cited by 138 · see citing works
Dysfunction of the Unfolded Protein Response During Global Brain Ischemia and Reperfusion
Kumar, R., Krause, G. S., Yoshida, H., Mori, K., & DeGracia, D. J. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200304000-00010 · Cited by 133 · see citing works
Reduced Translocation of Nascent Prion Protein During ER Stress Contributes to Neurodegeneration
Rane, N. S., Kang, S., Chakrabarti, O., Feigenbaum, L., & Hegde, R. S. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.06.015 · Cited by 132 · see citing works
The unfolded protein response in familial amyotrophic lateral sclerosis
Wang, L., Popko, B., & Roos, R. P. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq546 · Cited by 132 · see citing works
Mutant Prion Protein Expression Causes Motor and Memory Deficits and Abnormal Sleep Patterns in a Transgenic Mouse Model
Dossena, S., Imeri, L., Mangieri, M., Garofoli, A., Ferrari, L. L., Senatore, A., Restelli, E., Balducci, C., Fiordaliso, F., Salio, M., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.09.008 · Cited by 131 · see citing works
Overloaded Endoplasmic Reticulum–Golgi Compartments, a Possible Pathomechanism of Peripheral Neuropathies Caused by Mutations of the Peripheral Myelin Protein PMP22
D’Urso, D., Prior, R., Greiner–Petter, R., Gabreëls‐Festen, A. A. W. M., & Müller, H. W. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-02-00731.1998 · Cited by 130 · see citing works
Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice
Kieran, D., Woods, I., Villunger, A., Strasser, A., & Prehn, J. H. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707906105 · Cited by 129 · see citing works
Endoplasmic Reticulum Stress in Motor Neurons of the Spinal Cord in Sporadic Amyotrophic Lateral Sclerosis
Sasaki, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181d44992 · Cited by 121 · see citing works
Overexpressing GRP78 influences Ca2+ handling and function of mitochondria in astrocytes after ischemia-like stress
Ouyang, Y., Xu, L., Emery, J. F., Lee, A. S., & Giffard, R. G. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.10.007 · Cited by 120 · see citing works
Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice
Shibata, M., Hattori, H., Sasaki, T., Gotoh, J., Hamada, J., & Fukuuchi, Y. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00910-7 · Cited by 118 · see citing works
The TSC1 and TSC2 tumor suppressors are required for proper ER stress response and protect cells from ER stress-induced apoptosis
Kang, Y. J., Lü, M., & Guan, K.-L. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.82 · Cited by 115 · see citing works
Mutations Causing Childhood Ataxia with Central Nervous System Hypomyelination Reduce Eukaryotic Initiation Factor 2B Complex Formation and Activity
Richardson, J. P., Mohammad, S. S., & Pavitt, G. D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2352-2363.2004 · Cited by 114 · see citing works
ER stress response plays an important role in aggregation of α-synuclein
Jiang, P., Gan, M., Ebrahim, A. S., Lin, W.-L., Melrose, H. L., & Yen, S.-H. C. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-56 · Cited by 110 · see citing works
CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation
Benavides, A., Pastor, M. D., Santos, P., Tranque, P., & Calvo, S. (2005) · Glia · doi:10.1002/glia.20242 · Cited by 107 · see citing works
Dantrolene is neuroprotective in Huntington's disease transgenic mouse model
Chen, X., Wu, J., Lvovskaya, S., Herndon, E., Supnet, C. B., & Борисович, Б. И. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-81 · Cited by 107 · see citing works
Changes in the phosphorylation of initiation factor eIF‐2α, elongation factor eEF‐2 and p70 S6 kinase after transient focal cerebral ischaemia in mice
Althausen, S., Mengesdorf, T., Mies, G., Oláh, L., Nairn, A. C., Proud, C. G., & Paschen, W. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00462.x · Cited by 105 · see citing works
Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco–Sjögren syndrome
Zhao, L., Rosales, C., Seburn, K. L., Ron, D., & Ackerman, S. L. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp464 · Cited by 101 · see citing works
The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response
Chen, P., Burdette, A. J., Porter, J. C., Ricketts, J. C., Fox, S. A., Nery, F. C., Hewett, J. W., Berkowitz, L. A., Breakefield, X. O., Caldwell, K. A., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq266 · Cited by 96 · see citing works
The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB
Miranda, E., MacLeod, I., Davies, M. J., Perez, J., Römisch, K., Crowther, D. C., & Lomas, D. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn041 · Cited by 95 · see citing works
Self-citation
E2-25K/Hip-2 regulates caspase-12 in ER stress–mediated Aβ neurotoxicity
Song, S., Lee, H., Kam, T., Tai, M. L., Lee, J., Noh, J.-Y., Shim, S. M., Seo, S. J., Kong, Y., Nakagawa, T., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711066 · Cited by 90 · see citing works
Involvement of endoplasmic reticulum stress after middle cerebral artery occlusion in mice
Morimoto, N., Oida, Y., Shimazawa, M., Miura, M., Kudo, T., Imaizumi, K., & Hara, H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.04.017 · Cited by 89 · see citing works
Edaravone Protects against Hypoxia/Ischemia-Induced Endoplasmic Reticulum Dysfunction
Qi, X., Okuma, Y., Hosoi, T., & Nomura, Y. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.069088 · Cited by 88 · see citing works
Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients
Kantor, L., Harding, H. P., Ron, D., Schiffmann, R., Kaneski, C. R., Kimball, S. R., & Elroy‐Stein, O. (2005) · Human Genetics · doi:10.1007/s00439-005-0024-x · Cited by 83 · see citing works
Eif-2a Protects Brainstem Motoneurons in a Murine Model of Sleep Apnea
Zhu, Y., Fenik, P., Zhan, G., Sanfillipo-Cohn, B., Naidoo, N. N., & Veasey, S. C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5232-07.2008 · Cited by 81 · see citing works
HMG CoA reductase inhibitors reduce ischemic brain injury of Wistar rats through decreasing oxidative stress on neurons
Hayashi, T., Hamakawa, K., Nagotani, S., Jin, G., Li, F., Deguchi, K., Sehara, Y., Zhang, H., Nagano, I., Shoji, M., et al. (2005) · Brain Research · doi:10.1016/j.brainres.2004.12.051 · Cited by 78 · see citing works
Depletion of intracellular calcium stores is toxic to SH-SY5Y neuronal cells
Nguyen, H. N., Wang, C., & Perry, D. C. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03229-2 · Cited by 78 · see citing works
Increased ER stress during motor neuron degeneration in a transgenic mouse model of amyotrophic lateral sclerosis
Nagata, T., Ilieva, H. S., Murakami, T., Shiote, M., Narai, H., Ohta, Y., Hayashi, T., Shoji, M., & Abe, K. (2007) · Neurological Research · doi:10.1179/016164107x229803 · Cited by 77 · see citing works
Valproate reduces CHOP levels and preserves oligodendrocytes and axons after spinal cord injury
Penas, C., Verdú, E., Asensio-Pinilla, E., Guzmán-Lenis, M.-S., Herrando‐Grabulosa, M., Navarro, X., & Casas, C. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.01.012 · Cited by 76 · see citing works
Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease
Honjo, Y., Ito, H., Horibe, T., Takahashi, R., & Kawakami, K. (2010) · Brain Research · doi:10.1016/j.brainres.2010.06.016 · Cited by 73 · see citing works
Neuroserpin Polymers Activate NF-κB by a Calcium Signaling Pathway That Is Independent of the Unfolded Protein Response
Davies, M. J., Miranda, E., Roussel, B. D., Kaufman, R. J., Marciniak, S. J., & Lomas, D. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010744 · Cited by 71 · see citing works
Self-citation
Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine
Dukes, A. A., Laar, V. S. V., Cascio, M., & Hastings, T. G. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05392.x · Cited by 70 · see citing works
The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers
Li, F., Hayashi, T., Jin, G., Deguchi, K., Nagotani, S., Nagano, I., Shoji, M., Chan, P. H., & Abe, K. (2005) · Brain Research · doi:10.1016/j.brainres.2005.04.058 · Cited by 68 · see citing works
PERK is responsible for the increased phosphorylation of eIF2α and the severe inhibition of protein synthesis after transient global brain ischemia
Owen, C. R., Kumar, R., Zhang, P., McGrath, B. C., Cavener, D. R., & Krause, G. S. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03276.x · Cited by 67 · see citing works
Involvement of Gadd153 in the pathogenic action of presenilin‐1 mutations
Milhavet, O., Martindale, J. L., Camandola, S., Chan, S. L., Gary, D. S., Cheng, A., Holbrook, N. J., & Mattson, M. P. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01165.x · Cited by 66 · see citing works
Proteasomal Dysfunction and Endoplasmic Reticulum Stress Enhance Trafficking of Prion Protein Aggregates through the Secretory Pathway and Increase Accumulation of Pathologic Prion Protein
Nunziante, M., Ackermann, K., Dietrich, K., Wolf, H., Gädtke, L., Gilch, S., Vorberg, I. M., Groschup, M. H., & Schätzl, H. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.272617 · Cited by 61 · see citing works
Irreversible aggregation of protein synthesis machinery after focal brain ischemia
Zhang, F., Liu, C., & Hu, B. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03838.x · Cited by 60 · see citing works
Involvement of endoplasmic reticulum stress in the neuronal death induced by transient forebrain ischemia in gerbil
Oida, Y., Shimazawa, M., Imaizumi, K., & Hara, H. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.047 · Cited by 59 · see citing works
Altered localization of amyloid precursor protein under endoplasmic reticulum stress
Kudo, T., Okumura, M., Imaizumi, K., Araki, W., Morihara, T., Tanimukai, H., Kamagata, E., Tabuchi, N., Kimura, R., Kanayama, D., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.173 · Cited by 58 · see citing works
The unfolded protein response affects neuronal cell cycle protein expression: Implications for Alzheimer's disease pathogenesis
Hoozemans, J. J. M., Stieler, J., van Haastert, E. S., Veerhuis, R., Rozemüller, A. J. M., Baas, F., Eikelenboom, P., Arendt, T., & Scheper, W. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.01.013 · Cited by 56 · see citing works
Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin
Lajoie, P., & Snapp, E. L. (2011) · Journal of Cell Science · doi:10.1242/jcs.087510 · Cited by 50 · see citing works
Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke
Rissanen, A., Sivenius, J., & Jolkkonen, J. (2006) · Brain Research · doi:10.1016/j.brainres.2006.02.095 · Cited by 49 · see citing works
The Homocysteine-inducible Endoplasmic Reticulum Stress Protein Counteracts Calcium Store Depletion and Induction of CCAAT Enhancer-binding Protein Homologous Protein in a Neurotoxin Model of Parkinson Disease
Chigurupati, S., Wei, Z., Belal, C., Vandermey, M., Kyriazis, G. A., Arumugam, T. V., & Chan, S. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.020891 · Cited by 48 · see citing works
Phosphoproteins in Stress-Induced Disease
Dalton, L. E., Healey, E., Irving, J. A., & Marciniak, S. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00003-1 · Cited by 47 · see citing works
Self-citation
β-Amyloid and Endoplasmic Reticulum Stress Reponses in Primary Neurons: Effects of Drugs That Interact With the Cytoskeleton
Seyb, K. I., Ansar, S., Bean, J. L., & Michaelis, M. L. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:28:2:111 · Cited by 46 · see citing works
Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity.
Hara, H., Kamiya, T., & Adachi, T. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.10.006 · Cited by 43 · see citing works
Characterization of neuronal and astroglial responses to ER stress in the hippocampal CA1 area in mice following transient forebrain ischemia
Osada, N., Kosuge, Y., Ishige, K., & Ito, Y. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.03.017 · Cited by 41 · see citing works
Increased vulnerability of hippocampal pyramidal neurons to the toxicity of kainic acid in OASIS‐deficient mice
Chihara, K., Saito, A., Murakami, T., Hino, S., Aoki, Y., Sekiya, H., Aikawa, Y., Wanaka, A., & Imaizumi, K. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06188.x · Cited by 36 · see citing works
Derlin-1 overexpression ameliorates mutant SOD1-induced endoplasmic reticulum stress by reducing mutant SOD1 accumulation
Mori, A., Yamashita, S., Uchino, K., Suga, T., Ikeda, T., Takamatsu, K., Ishizaki, M., Koide, T., Kimura, E., Mita, S., et al. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.010 · Cited by 35 · see citing works
Involvement of IRE1α signaling in the hippocampus in patients with mesial temporal lobe epilepsy
Liu, G., Guo, H., Guo, C., Zhao, S., Gong, D., & Zhao, Y. (2010) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2010.10.004 · Cited by 35 · see citing works
NF-κB activated by ER calcium release inhibits Aβ-mediated expression of CHOP protein: Enhancement by AD-linked mutant presenilin 1
Schapansky, J., Olson, K. L., der Ploeg, R. V., & Glazner, G. W. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.04.009 · Cited by 35 · see citing works
Presenilin-1 Holoprotein is an Interacting Partner of Sarco Endoplasmic Reticulum Calcium-ATPase and Confers Resistance to Endoplasmic Reticulum Stress
Jin, H., Sanjo, N., Uchihara, T., Watabe, K., George‐Hyslop, P. S., Fraser, P. E., & Mizusawa, H. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1360 · Cited by 33 · see citing works
Apolipoprotein E-deficient mice are more vulnerable to ER stress after transient forebrain ischemia
Osada, N., Kosuge, Y., Kihara, T., Ishige, K., & Ito, Y. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.01.010 · Cited by 33 · see citing works
Expression of Mutant or Cytosolic PrP in Transgenic Mice and Cells Is Not Associated with Endoplasmic Reticulum Stress or Proteasome Dysfunction
Quaglio, E., Restelli, E., Garofoli, A., Dossena, S., Luigi, A. D., Tagliavacca, L., Imperiale, D., Migheli, A., Salmona, M., Sitia, R., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019339 · Cited by 33 · see citing works
Ca2+ Homeostasis Modulation Enhances the Amenability of L444P Glucosylcerebrosidase to Proteostasis Regulation in Patient-Derived Fibroblasts
Wang, F., Agnello, G., Sotolongo, N., & Segatori, L. (2010) · ACS Chemical Biology · doi:10.1021/cb100321m · Cited by 30 · see citing works
A novel polymorphism in SEL1L confers susceptibility to Alzheimer's disease
Saltini, G., Dominici, R., Lovati, C., Cattaneo, M., Michelini, S., Malferrari, G., Caprera, A., Milanesi, L., Finazzi, D., Bertora, P., et al. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.12.038 · Cited by 25 · see citing works
Homocysteine induces X-box-binding protein 1 splicing in the mice brain
Hosoi, T., Ogawa, K., & Ozawa, K. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.12.005 · Cited by 23 · see citing works
GADD34 protein levels increase after transient ischemia in the cortex but not in the CA1 subfield: implications for post‐ischemic recovery of protein synthesis in ischemia‐resistant cells
Paschen, W., Hayashi, T., Saito, A., & Chan, P. H. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02555.x · Cited by 21 · see citing works
Proteomic insights into the protective mechanisms of an in vitro oxidative stress model of early stage Parkinson's disease
Bauereis, B., Haskins, W. E., LeBaron, R. G., & Renthal, R. D. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.10.071 · Cited by 20 · see citing works
Quinotrierixin Inhibited ER Stress-Induced XBP1 mRNA Splicing through Inhibition of Protein Synthesis
Yamamoto, K., Tashiro, E., & Imoto, M. (2011) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100622 · Cited by 16 · see citing works
Evolution of GADD34 expression after focal cerebral ischaemia
McCaig, D., Imai, H., Gallagher, L., Graham, D. I., Harland, J., Brown, S. M., & Macrae, I. M. (2005) · Brain Research · doi:10.1016/j.brainres.2004.11.058 · Cited by 14 · see citing works

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The Role of Endoplasmic Reticulum Stress in Human Pathology
Oakes, S. A., & Papa, F. R. (2014) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104649 · Cited by 1,589 · see citing works
Targeting the unfolded protein response in disease
Hetz, C. A., Chevet, É., & Harding, H. P. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3976 · Cited by 908 · see citing works
Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
Hetz, C., & Mollereau, B. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3689 · Cited by 684 · see citing works
Memory loss in Alzheimer's disease
Jahn, H. (2013) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2013.15.4/hjahn · Cited by 653 · see citing works
Pharmacological targeting of endoplasmic reticulum stress in disease
Marciniak, S. J., Chambers, J. E., & Ron, D. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00320-3 · Cited by 536 · see citing works
Self-citation
There's Something Wrong with my MAM; the ER–Mitochondria Axis and Neurodegenerative Diseases
Paillusson, S., Stoica, R., Gomez-Suaga, P., Lau, D. H. W., Mueller, S., Miller, T., & Miller, C. C. J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.008 · Cited by 439 · see citing works
Novel Stroke Therapeutics: Unraveling Stroke Pathophysiology and Its Impact on Clinical Treatments
George, P. M., & Steinberg, G. K. (2015) · Neuron · doi:10.1016/j.neuron.2015.05.041 · Cited by 394 · see citing works
The unfolded protein response in neurodegenerative diseases: a neuropathological perspective
Scheper, W., & Hoozemans, J. J. M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1462-8 · Cited by 369 · see citing works
Sleep and the single neuron: the role of global slow oscillations in individual cell rest
Vyazovskiy, V. V., & Harris, K. D. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3494 · Cited by 362 · see citing works
Targeting autophagy in ischemic stroke: From molecular mechanisms to clinical therapeutics
Ajoolabady, A., Wang, S., Kroemer, G., Penninger, J. M., Uversky, V. N., Praticò, D., Henninger, N., Reiter, R. J., Bruno, A., JOSHIPURA, K. J., et al. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107848 · Cited by 334 · see citing works
Role of the JAK/STAT signaling pathway in regulation of innate immunity in neuroinflammatory diseases
Yan, Z., Gibson, S. A., Buckley, J. A., Qin, H., & Benveniste, E. N. (2018) · Clinical Immunology · doi:10.1016/j.clim.2016.09.014 · Cited by 318 · see citing works
α1-Antitrypsin deficiency
Greene, C. M., Marciniak, S. J., Teckman, J. H., Ferrarotti, I., Brantly, M., Lomas, D. A., Stoller, J. K., & McElvaney, N. G. (2016) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2016.51 · Cited by 326 · see citing works
Self-citation
Cellular metabolic and autophagic pathways: Traffic control by redox signaling
Dodson, M. B., Darley-Usmar, V. M., & Zhang, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.014 · Cited by 325 · see citing works
Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models
Wan, Y.-W., Al-Ouran, R., Mangleburg, C. G., Perumal, T. M., Lee, T. V., Allison, K., Swarup, V., Funk, C. C., Gaiteri, C., Allen, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107908 · Cited by 295 · see citing works
“Autosomal-dominant mutations in neuroserpin cause familial encephalopathy with Neuroserpin inclusion bodies, a rare, early-onset neurodegenerative dementia caused by protein aggregation within the endoplasmic reticulum (ER) and associated ER stress (Roussel et al., 2013).”
Background
Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 306 · see citing works
The Association Between Obstructive Sleep Apnea and Alzheimer’s Disease: A Meta-Analysis Perspective
Emamian, F., Khazaie, H., Tahmasian, M., Leschziner, G. D., Morrell, M. J., Hsiung, G.-Y. R., Rosenzweig, I., & Sepehry, A. A. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00078 · Cited by 258 · see citing works
ER stress and UPR in Alzheimer’s disease: mechanisms, pathogenesis, treatments
Ajoolabady, A., Lindholm, D., Ren, J., & Pratico, D. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05153-5 · Cited by 261 · see citing works
Axonal Endoplasmic Reticulum Ca2+ Content Controls Release Probability in CNS Nerve Terminals
de Juan‐Sanz, J., Holt, G. T., Schreiter, E. R., de Juan, F., Kim, D. S., & Ryan, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.010 · Cited by 257 · see citing works
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Authors: Roussel, B. D., Kruppa, A. J., Miranda, E., Crowther, D. C., Lomas, D. A., & Marciniak, S. J.
Affiliations: Inserm (FR)
University of Cambridge (GB)
Istituto Pasteur (IT)
Corresponding author: Marciniak, Stefan J
ORCID: Roussel, Benoit D
Kruppa, Antonina J
Miranda, Elena
Crowther, Damian C
Lomas, David A
Marciniak, Stefan J
Venue: The Lancet Neurology
Publisher: Elsevier BV
Published: 2013-01
Volume: 12
Issue: 1
Pages: 105-118
ISSN: 1474-4422 (ISSN-L)
DOI: 10.1016/s1474-4422(12)70238-7
OpenAlex: W2051661723
Cited by: 441
References: 137
Citations by year: 2026: 9 · 2025: 16 · 2024: 25 · 2023: 19 · 2022: 28 · 2021: 25 · 2020: 31 · 2019: 35 · 2018: 32 · 2017: 34 · 2016: 54 · 2015: 41 · 2014: 54 · 2013: 38
FWCI: 3.92
Type: journal article
Language: en
Open access: green
inserm.hal.science
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: The Lancet Neurology (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, cc-by)
HAL (submittedVersion)
UCL Discovery (University College London) (submittedVersion)
IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
Apollo
Funders: Wellcome Trust (G1002610, 089703/Z/09/Z, 100140, 089703, 100140/Z/12/Z)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: endoplasmic reticulum dysfunction, endoplasmic reticulum stress, unfolded protein response, neurodegenerative diseases, cerebral ischemia, stroke, sleep apnea, Alzheimer's disease, amyloid-beta, neuroserpin, multiple sclerosis, amyotrophic lateral sclerosis, prion disease, Parkinson's disease, Huntington's disease, protein misfolding
MeSH terms: Animals, Endoplasmic Reticulum, Humans, Nervous System Diseases, Signal Transduction, Amyloid beta-Peptides, Protein Folding, Unfolded Protein Response

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Endoplasmic reticulum dysfunction in neurological disease

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