The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms
Abstract
Significance: Amyotrophic lateral sclerosis (ALS), an incurable motor neuron disease, is associated with mutation and misfolding of the Cu/Zn superoxide dismutase (SOD1) protein. Prior studies found that mutant misfolded SOD1 can convert wild-type (WT) SOD1 to a misfolded form inside living cells in a prion-like fashion. We now report that misfolded WT SOD1 can be transmitted from cell to cell, and that propagated protein misfolding can be perpetuated. Misfolded SOD1 transmission between cells can be mediated through release and uptake of protein aggregates or via small membrane-bounded transport vesicles called exosomes. These mechanisms may help explain why sporadic ALS, without a known genetic cause, can spread systematically from region to region in a progressive manner.
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In the citing paper
“Mutant SOD1 proteins misfold, filling MNs with toxic aggregates, which impinge on their survival5.”
From Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis (2020) · cites this paper as [5]
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“The overexpression of mutant SOD1 increases rates of cell death in MN-like NSC-34 cells5, and SOD1G93A affects Neuro2a cell survival63.”
From Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis (2020) · cites this paper as [5]
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Cites
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936
Self-citationA Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409
The changing scene of amyotrophic lateral sclerosis
Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
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Prion-like transmission of protein aggregates in neurodegenerative diseases
Brundin, P., Melki, R., & Kopito, R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2873 · Cited by 778
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Cited by
Sorted by citations
The biology , function , and biomedical applications of exosomes
Kalluri, R., & LeBleu, V. S. (2020) · Science · doi:10.1126/science.aau6977 · Cited by 10,770
The glymphatic system: a beginner's guide
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Spreading of pathology in neurodegenerative diseases: a focus on human studies
Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790
Extracellular vesicles round off communication in the nervous system
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“…the amyotrophic lateral sclerosis (ALS) disease based on studies demonstrating the efficient transfer of mutant and misfolded copper-zinc superoxide dismutase 1 (SOD1) to other cells, reason why exosomes are now suggested as targets to modulate ALS disease (Basso et al., 2013; Grad et al., 2014).”
Background
Metadata
- Authors
- Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O’Neill, M. A., Yanai, A., Silverman, J. M., Zeineddine, R., Corcoran, L., Kumita, J. R., Luheshi, L. M., Yousefi, M., Coleman, B. M., Hill, A. F., Plotkin, S. S., Mackenzie, I. R., & Cashman, N. R.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-02-18
- Volume
- 111
- Issue
- 9
- Pages
- 3620-3625
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 414
- References
- 5
- Language
- en
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- The paper
- Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O’Neill, M. A., Yanai, A., Silverman, J. M., Zeineddine, R., Corcoran, L., Kumita, J. R., Luheshi, L. M., Yousefi, M., Coleman, B. M., Hill, A. F., Plotkin, S. S., Mackenzie, I. R., & Cashman, N. R. (2014). Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1312245111
