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

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.

journal_name

Curr Neuropharmacol

authors

Abisambra JF,Jinwal UK,Jones JR,Blair LJ,Koren J 3rd,Dickey CA

doi

10.2174/157015911798376226

subject

Has Abstract

pub_date

2011-12-01 00:00:00

pages

623-31

issue

4

eissn

1570-159X

issn

1875-6190

pii

CN-9-623

journal_volume

9

pub_type

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