Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2014 Jan;386(1-2):45-61.
doi: 10.1007/s11010-013-1844-y. Epub 2013 Oct 5.

Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door?

Subhankar Paul  1 , Sailendra Mahanta
Affiliations
Review

Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door?

Subhankar Paul et al. Mol Cell Biochem. 2014 Jan.

Abstract

A number of acute and chronic neurodegenerative disorders are caused due to misfolding and aggregation of many intra- and extracellular proteins. Protein misfolding and aggregation processes in cells are strongly regulated by cellular molecular chaperones known as heat-shock proteins (Hsps) that include Hsp60, Hsp70, Hsp40, and Hsp90. Recent studies have shown the evidences that Hsps are colocalized in protein aggregates in Alzheimer's disease (AD), Parkinson's disease (PD), Polyglutamine disease (PGD), Prion disease, and other neurodegenerative disorders. This fact indicates that Hsps might have attempted to prevent aggregate formation in cells and thus to suppress disease conditions. Experimental findings have already established in many cases that selective overexpression of Hsps like Hsp70 and Hsp40 prevented the disease progression in various animal models and cellular models. However, recently, various Hsp modulators like geldanamycin, 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin, and celastrol have shown to up-regulate the expression level of Hsp70 and Hsp40, which in turn triggers the solubilization of diseased protein aggregates. Hsps are, therefore, if appropriately selected, an attractive choice for therapeutic targeting in various kinds of neurodegeneration and hence are expected to have strong potential as therapeutic agents in suppressing or curing AD, PD, PGD, and other devastative neurodegenerative disorders. In the present review, we report the experimental findings that describe the implication of Hsps in the development of neurodegeneration and explore the possibility of how Hsps can be used directly or as a target by other agents to prevent various neurodegeneration through preventing aggregation process and thus reducing the toxicity of the oligomers based on the previous reports.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Neuropathol Appl Neurobiol. 2000 Aug;26(4):304-12 - PubMed
    1. Biochemistry. 2012 Jan 31;51(4):888-98 - PubMed
    1. Proc Natl Acad Sci U S A. 2008 May 20;105(20):7206-11 - PubMed
    1. Cell. 1998 Feb 6;92(3):351-66 - PubMed
    1. Biochem Biophys Res Commun. 2008 Nov 28;376(4):637-41 - PubMed

Substances

LinkOut - more resources