Cited by 589Prion Diseases and Protein MisfoldingEndoplasmic Reticulum Stress and DiseaseAlzheimer's disease research and treatments

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Oral Treatment Targeting the Unfolded Protein Response Prevents Neurodegeneration and Clinical Disease in Prion-Infected Mice

Moreno, Julie A., Halliday, Mark, Molloy, Colin, Radford, Helois, Verity, Nicholas, Axten, Jeffrey M., Ortori, Catharine A., Willis, Anne E., Fischer, Peter M., Barrett, David A., Mallucci, Giovanna R.·2013·Science Translational Medicine

DOI 10.1126/scitranslmed.3006767

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Abstract

During prion disease, an increase in misfolded prion protein (PrP) generated by prion replication leads to sustained overactivation of the branch of the unfolded protein response (UPR) that controls the initiation of protein synthesis. This results in persistent repression of translation, resulting in the loss of critical proteins that leads to synaptic failure and neuronal death. We have previously reported that localized genetic manipulation of this pathway rescues shutdown of translation and prevents neurodegeneration in a mouse model of prion disease, suggesting that pharmacological inhibition of this pathway might be of therapeutic benefit. We show that oral treatment with a specific inhibitor of the kinase PERK (protein kinase RNA-like endoplasmic reticulum kinase), a key mediator of this UPR pathway, prevented UPR-mediated translational repression and abrogated development of clinical prion disease in mice, with neuroprotection observed throughout the mouse brain. This was the case for animals treated both at the preclinical stage and also later in disease when behavioral signs had emerged. Critically, the compound acts downstream and independently of the primary pathogenic process of prion replication and is effective despite continuing accumulation of misfolded PrP. These data suggest that PERK, and other members of this pathway, may be new therapeutic targets for developing drugs against prion disease or other neurodegenerative diseases where the UPR has been implicated.

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RETRACTED: Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
Atkin, J. D., Farg, M. A., Walker, A. K., McLean, C., Tomas, D., & Horne, M. K. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.02.009 · Cited by 350
Retracted
Signal integration in the endoplasmic reticulum unfolded protein response
Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,431
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
Diabetes Mellitus and Exocrine Pancreatic Dysfunction in Perk−/− Mice Reveals a Role for Translational Control in Secretory Cell Survival
Harding, H. P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D. D., & Ron, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00264-7 · Cited by 1,217
Depleting Neuronal PrP in Prion Infection Prevents Disease and Reverses Spongiosis
Mallucci, G. R., Dickinson, A., Linehan, J. M., Klöhn, P., Brandner, S., & Collinge, J. (2003) · Science · doi:10.1126/science.1090187 · Cited by 783
Self-citation
Translational Regulation of Gene Expression during Conditions of Cell Stress
Spriggs, K. A., Bushell, M., & Willis, A. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.028 · Cited by 748
Self-citation
Discovery of 7-Methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1 H -indol-5-yl)-7 H -pyrrolo[2,3- d ]pyrimidin-4-amine (GSK2606414), a Potent and Selective First-in-Class Inhibitor of Protein Kinase R (PKR)-like Endoplasmic Reticulum Kinase (PERK)
Axten, J. M., Medina, J. R., Feng, Y., Shu, A. Y. L., Romeril, S. P., Grant, S. W., Li, W. H. H., Heerding, D. A., Minthorn, E. A., Mencken, T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300713s · Cited by 620
Self-citation
Sustained translational repression by eIF2α-P mediates prion neurodegeneration
Moreno, J. A., Radford, H. E., Peretti, D., Steinert, J. R., Verity, N., Martin, M. G., Halliday, M., Morgan, J., Dinsdale, D. D., Ortori, C. A., et al. (2012) · Nature · doi:10.1038/nature11058 · Cited by 616
Self-citation
The Unfolded Protein Response Is Activated in Pretangle Neurons in Alzheimer's Disease Hippocampus
Hoozemans, J. J. M., van Haastert, E. S., Nijholt, D. A. T., Rozemuller, A. J. M., Eikelenboom, P., & Scheper, W. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080814 · Cited by 600

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Authors: Moreno, J. A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J. M., Ortori, C. A., Willis, A. E., Fischer, P. M., Barrett, D. A., & Mallucci, G. R.
Affiliations: University of Leicester (GB)
GlaxoSmithKline (United States) (US)
University of Nottingham (GB)
Corresponding author: Mallucci, Giovanna R.
ORCID: Moreno, Julie A.
Molloy, Colin
Radford, Helois
Axten, Jeffrey M.
Willis, Anne E.
Fischer, Peter M.
Barrett, David A.
Mallucci, Giovanna R.
Venue: Science Translational Medicine
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2013-10-09
Volume: 5
Issue: 206
Pages: 206ra138-206ra138
ISSN: 1946-6234 (ISSN-L)
1946-6242
DOI: 10.1126/scitranslmed.3006767
OpenAlex: W2010375635
Cited by: 589
References: 29
Citations by year: 2026: 22 · 2025: 27 · 2024: 21 · 2023: 29 · 2022: 32 · 2021: 42 · 2020: 59 · 2019: 46 · 2018: 54 · 2017: 72 · 2016: 54 · 2015: 58 · 2014: 58 · 2013: 13
FWCI: 27.31
Type: journal article
Language: en
Open access: closed
Locations: Science Translational Medicine (publishedVersion)
PubMed (publishedVersion)
Leicester Research Archive (University of Leicester) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords: prion disease, unfolded protein response, protein synthesis inhibition, neurodegeneration, oral drug therapy, neuroprotection, prion replication, synaptic failure, neurodegenerative disease treatment
MeSH terms: Adenine, Administration, Oral, Animals, Blood-Brain Barrier, Brain, Indoles, Nerve Degeneration, Phosphorylation, Prions, Synapses, Protein Biosynthesis, Eukaryotic Initiation Factor-2, Prion Diseases, Neuroprotective Agents, eIF-2 Kinase, Mice, Unfolded Protein Response

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Oral Treatment Targeting the Unfolded Protein Response Prevents Neurodegeneration and Clinical Disease in Prion-Infected Mice

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