Van Der Putten, P. Herman and Lotz, Gregor (2013) Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases. Neurotherapeutics, 10 (3). pp. 416-428.

Abstract

A common pathological hallmark of protein-conformational brain diseases is the formation of disease-specific protein aggregates. In Alzheimer’s disease (AD), these are comprised of Amyloid-β (Aβ) and Tau as opposed to α-synuclein in Parkinson`s disease (PD) and N-terminal fragments of mutant huntingtin (mHTT) in Huntington’s disease (HD). Most aggregates also sequester molecular chaperones, a protein family that assist in folding, re-folding, stabilization and processing of client proteins including misfolded proteins in brain diseases. Molecular chaperone modulation has achieved remarkable therapeutic effects in some cellular and preclinical animal models of protein-conformational diseases. This has raised hope for chaperone-based strategies to combat these diseases. Here, we briefly review the functional diversity and medical significance of molecular chaperones, their therapeutic potential and common and specific challenges towards clinical application.

Item Type:	Article
Date Deposited:	26 Apr 2016 23:46
Last Modified:	26 Apr 2016 23:46
URI:	https://oak.novartis.com/id/eprint/9204