Exploiting the Diversity of the Heat-Shock Protein Family for Primary and Secondary Tauopathy Therapeutics

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.

Cite this article as:

F. Abisambra Jose, K. Jinwal Umesh, R. Jones Jeffrey, J. Blair Laura, Koren III John and A. Dickey Chad, Exploiting the Diversity of the Heat-Shock Protein Family for Primary and Secondary Tauopathy Therapeutics, Current Neuropharmacology 2011; 9 (4) . https://dx.doi.org/10.2174/157015911798376226