Title: Exploiting the Diversity of the Heat-Shock Protein Family for Primary and Secondary Tauopathy Therapeutics
Volume: 9
Issue: 4
Author(s): Jose F. Abisambra, Umesh K. Jinwal, Jeffrey R. Jones, Laura J. Blair, John Koren III and Chad A. Dickey
Affiliation:
Keywords:
Heat shock proteins, chaperones, neurodegeneration, alzheimer, Hsp27, Tau, heat shock proteins (Hsps), 42-amino acid version, Alzheimer's disease
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 Alzheimers 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 Alzheimers disease. It will particularly focus on the pharmacological targeting of the Hsp70/90 system and the value of manipulating Hsp27 for treating Alzheimers disease.
