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Lackie RE, Maciejewski A, Ostapchenko VG, et al. The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases. Front Neurosci. 2017;11:254doi: 10.3389/fnins.2017.00254.
Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W. Y., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017). The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases. Frontiers in neuroscience, 11254. https://doi.org/10.3389/fnins.2017.00254
Lackie, Rachel E, et al. "The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases." Frontiers in neuroscience vol. 11 (2017): 254. doi: https://doi.org/10.3389/fnins.2017.00254
Lackie RE, Maciejewski A, Ostapchenko VG, Marques-Lopes J, Choy WY, Duennwald ML, Prado VF, Prado MAM. The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases. Front Neurosci. 2017 May 16;11:254. doi: 10.3389/fnins.2017.00254. eCollection 2017. PMID: 28559789; PMCID: PMC5433227.
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Front Neurosci. 2017 May 16;11:254. doi: 10.3389/fnins.2017.00254. eCollection 2017.

The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases.

Frontiers in neuroscience

Rachel E Lackie, Andrzej Maciejewski, Valeriy G Ostapchenko, Jose Marques-Lopes, Wing-Yiu Choy, Martin L Duennwald, Vania F Prado, Marco A M Prado

Affiliations

  1. Molecular Medicine, Robarts Research Institute, University of Western OntarioLondon, ON, Canada.
  2. Program in Neuroscience, University of Western OntarioLondon, ON, Canada.
  3. Department of Biochemistry, University of Western OntarioLondon, ON, Canada.
  4. Department of Pathology and Laboratory Medicine, University of Western OntarioLondon, ON, Canada.
  5. Department of Physiology and Pharmacology, University of Western OntarioLondon, ON, Canada.
  6. Department of Anatomy and Cell Biology, Schulich School of Medicine and Dentistry, University of Western OntarioLondon, ON, Canada.

PMID: 28559789 PMCID: PMC5433227 DOI: 10.3389/fnins.2017.00254

Abstract

The accumulation of misfolded proteins in the human brain is one of the critical features of many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta-amyloid (Aβ) peptide-either soluble (oligomers) or insoluble (plaques) and of tau protein, which form neurofibrillary tangles, are the major hallmarks of AD. Chaperones and co-chaperones regulate protein folding and client maturation, but they also target misfolded or aggregated proteins for refolding or for degradation, mostly by the proteasome. They form an important line of defense against misfolded proteins and are part of the cellular quality control system. The heat shock protein (Hsp) family, particularly Hsp70 and Hsp90, plays a major part in this process and it is well-known to regulate protein misfolding in a variety of diseases, including tau levels and toxicity in AD. However, the role of Hsp90 in regulating protein misfolding is not yet fully understood. For example, knockdown of Hsp90 and its co-chaperones in a

Keywords: ALS; Alzheimer's disease; HOP; Huntington's disease; Parkinson's disease; STIP1; TDP-43; tau

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