The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
Open accessAbstract
The accumulation of insoluble protein aggregates in intra and perinuclear inclusions is a hallmark of Huntington's disease (HD) and related glutamine-repeat disorders. A central question is whether protein aggregation plays a direct role in the pathogenesis of these neurodegenerative diseases. Here we show by using a filter retardation assay that the mAb 1C2, which specifically recognizes the elongated polyglutamine (polyQ) stretch in huntingtin, and the chemical compounds Congo red, thioflavine S, chrysamine G, and Direct fast yellow inhibit HD exon 1 protein aggregation in a dose-dependent manner. On the other hand, potential inhibitors of amyloid-β formation such as thioflavine T, gossypol, melatonin, and rifampicin had little or no inhibitory effect on huntingtin aggregation in vitro . The results obtained by the filtration assay were confirmed by electron microscopy, SDS/PAGE, and MS. Furthermore, cell culture studies revealed that the Congo red dye at micromolar concentrations reduced the extent of HD exon 1 aggregation in transiently transfected COS cells. Together, these findings contribute to a better understanding of the mechanism of huntingtin fibrillogenesis in vitro and provide the basis for the development of new huntingtin aggregation inhibitors that may be effective in treating HD.
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Cites
Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291
Self-citationSittler, A., Devys, D., Weber, C., & Mandel, J.-L. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.1.95 · Cited by 198
Cited by
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115
“…which greatly compromises membrane integrity, and lead to neuronal degeneration via the creation of significant alterations in the equilibrium of ions and small metabolites between the cytoplasm and the extracellular space (Heiser et al., 2000; Volles et al., 2001; Volles and Lansbury, 2003).”
BackgroundInfluentialMolecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lueder, G., Lehrach, H., & Wanker, E. E. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1393 · Cited by 631
Self-citationPivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
Sánchez, I., Mahlke, C., & Yuan, J. (2003) · Nature · doi:10.1038/nature01301 · Cited by 503
Metadata
- Authors
- Heiser, V., Scherzinger, E., Boeddrich, A., Nordhoff, E., Lurz, R., Schugardt, N., Lehrach, H., & Wanker, E. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-05-30
- Volume
- 97
- Issue
- 12
- Pages
- 6739-6744
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2041993377
- Cited by
- 262
- References
- 2
- FWCI
- 6.99
- Type
- journal article
- Language
- en
- Open access
- green
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- Heiser, V., Scherzinger, E., Boeddrich, A., Nordhoff, E., Lurz, R., Schugardt, N., Lehrach, H., & Wanker, E. E. (2000). Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.110138997
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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