Stressing Out Hsp90 in Neurotoxic Proteinopathies

Author(s): Carmen Inda, Alexander Bolaender, Tai Wang, Srinivasa R. Gandu, John Koren III.

Journal Name: Current Topics in Medicinal Chemistry

Volume 16 , Issue 25 , 2016

Become EABM
Become Reviewer

Graphical Abstract:


A toxic accumulation of proteins is the hallmark pathology of several neurodegenerative disorders. Protein accumulation is regularly prevented by the network of molecular chaperone proteins, including and especially Hsp90. For reasons not yet elucidated, Hsp90 and the molecular chaperones interact with, but do not degrade, these toxic proteins resulting in the pathogenic accumulation of proteins such as tau, in Alzheimer’s Disease, and α-synuclein, in Parkinson’s Disease. In this review, we describe the associations between Hsp90 and the pathogenic and driver proteins of several neurodegenerative disorders. We additionally describe how the inhibition of Hsp90 promotes the degradation of both mutant and pathogenic protein species in models of neurodegenerative diseases. We also examine the current state of Hsp90 inhibitors capable of crossing the blood-brain barrier; compounds which may be capable of slowing, preventing, and possible reversing neurodegenerative diseases.

Keywords: HsP90, Neurodegenerative disease, α-Synuclein, DNA.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2016
Page: [2829 - 2838]
Pages: 10
DOI: 10.2174/1568026616666160413141350
Price: $58

Article Metrics

PDF: 34
PRC: 1