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Abisambra JF, Jinwal UK, Jones JR, et al. Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics. Curr Neuropharmacol. 2011;9(4):623-31doi: 10.2174/157015911798376226.
Abisambra, J. F., Jinwal, U. K., Jones, J. R., Blair, L. J., Koren, J., & Dickey, C. A. (2011). Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics. Current neuropharmacology, 9(4), 623-31. https://doi.org/10.2174/157015911798376226
Abisambra, Jose F, et al. "Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics." Current neuropharmacology vol. 9,4 (2011): 623-31. doi: https://doi.org/10.2174/157015911798376226
Abisambra JF, Jinwal UK, Jones JR, Blair LJ, Koren J, Dickey CA. Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics. Curr Neuropharmacol. 2011 Dec;9(4):623-31. doi: 10.2174/157015911798376226. PMID: 22654720; PMCID: PMC3263456.
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Curr Neuropharmacol. 2011 Dec;9(4):623-31. doi: 10.2174/157015911798376226.

Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics.

Current neuropharmacology

Jose F Abisambra, Umesh K Jinwal, Jeffrey R Jones, Laura J Blair, John Koren, Chad A Dickey

Affiliations

  1. Department of Molecular Medicine, USF Health Byrd Alzheimer's Institute, Tampa, FL 33613, USA.

PMID: 22654720 PMCID: PMC3263456 DOI: 10.2174/157015911798376226

Abstract

The heat shock protein (Hsp) family is an evolutionarily conserved system that is charged with preventing unfolded or misfolded proteins in the cell from aggregating. In Alzheimer's disease, extracellular accumulation of the amyloid β peptide (Aβ) and intracellular aggregation of the microtubule associated protein tau may result from mechanisms involving chaperone proteins like the Hsps. Due to the ability of Hsps to regulate aberrantly accumulating proteins like Aβ and tau, therapeutic strategies are emerging that target this family of chaperones to modulate their pathobiology. This article focuses on the use of Hsp-based therapeutics for treating primary and secondary tauopathies like Alzheimer's disease. It will particularly focus on the pharmacological targeting of the Hsp70/90 system and the value of manipulating Hsp27 for treating Alzheimer's disease.

Keywords: Heat shock proteins; Hsp27; Tau.; alzheimer; chaperones; neurodegeneration

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