HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils.

ABSTRACT: Neurodegenerative diseases (NDs) are associated with accumulated misfolded proteins (MPs). MPs oligomerize and form multiple forms of amyloid fibril polymorphs that dictate fibril propagation and cellular dysfunction. Protein misfolding processes that impair protein homeostasis are implicated in onset and progression of NDs. A wide variety of molecular chaperones safeguard the cell from MP accumulation. A rather overlooked molecular chaperone is HSP10, known as a co-chaperone for HSP60. Due to the ubiquitous presence in human tissues and protein overabundance compared with HSP60, we studied how HSP10 alone influences fibril formation in vitro of Alzheimer's disease-associated Aβ1-42. At sub-stoichiometric concentrations, eukaryotic HSP10s (human and Drosophila) significantly

SUBMITTER: Larsson JNK 

PROVIDER: S-EPMC9234269 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature