The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease
Open accessAbstract
Histone deacetylases (HDACs) are currently being discussed as promising therapeutic targets to treat neurodegenerative diseases. However, the role of specific HDACs in cognition and neurodegeneration remains poorly understood. Here, we investigate the function of HDAC6, a class II member of the HDAC superfamily, in the adult mouse brain. We report that mice lacking HDAC6 are cognitively normal but reducing endogenous HDAC6 levels restores learning and memory and α‐tubulin acetylation in a mouse model for Alzheimer's disease (AD). Our data suggest that this therapeutic effect is, at least in part, linked to the observation that loss of HDAC6 renders neurons resistant to amyloid‐β‐mediated impairment of mitochondrial trafficking. Thus, our study suggests that targeting HDAC6 could be a suitable strategy to ameliorate cognitive decline observed in AD.
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Cites
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · cited 4×
“…play an important role during AD pathogenesis (Stokin et al, 2005), and that one of the best-described roles of HDAC6 is deacetylation of a -tubulin K40ac (Haggarty et al, 2003; Hubbert et al, 2002), we decided to analyze tubulin acetylation in APPPS1-21 and APPPS1-21-Hdac6 (cid:1) / (cid:1) mice.”
InfluentialDendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
HDAC2 negatively regulates memory formation and synaptic plasticity
Guan, J.-S., Haggarty, S. J., Giacometti, E., Dannenberg, J.-H., Joseph, N., Gao, J., Nieland, T. J. F., Zhou, Y., Wang, X., Mazitschek, R., et al. (2009) · Nature · doi:10.1038/nature07925 · Cited by 1,644
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456
HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.
Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224
Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease
Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066
Cited by
Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?
Simões-Pires, C., Zwick, V., Nurisso, A., Schenker, E., Carrupt, P.-A., & Cuendet, M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-7 · Cited by 341
Cook, C., Carlomagno, Y., Gendron, T. F., Dunmore, J., Scheffel, K., Stetler, C., Davis, M., Dickson, D., Jarpe, M., DeTure, M., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 309
Shukla, S., & Tekwani, B. L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00537 · Cited by 314
Metadata
- Authors
- Govindarajan, N., Rao, P., Burkhardt, S., Sananbenesi, F., Schlüter, O. M., Bradke, F., Lu, J., & Fischer, A.
- Venue
- EMBO Molecular Medicine
- Published
- 2012-11-26
- Volume
- 5
- Issue
- 1
- Pages
- 52-63
- ISSN
- 1757-4676 (ISSN-L)
- 1757-4684
- OpenAlex
- W1846838131
- Cited by
- 342
- References
- 54
- FWCI
- 16.98
- Type
- journal article
- Language
- en
- Open access
- gold
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- Govindarajan, N., Rao, P., Burkhardt, S., Sananbenesi, F., Schlüter, O. M., Bradke, F., Lu, J., & Fischer, A. (2013). Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease. EMBO Molecular Medicine. https://doi.org/10.1002/emmm.201201923
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
