Regulation Of In Vitro Fibril Formation Of Synuclein Mutant Proteins By Hsp104p

Author(s): Byungmoon Kong, Young Kee Chae, Kyunghee Lee.

Journal Name: Protein & Peptide Letters

Volume 10 , Issue 5 , 2003

Become EABM
Become Reviewer

Abstract:

Hsp104p, as an anti-oxidative protector of ROS generation, was examined to inquire if it prevents aggregation of synuclein mutants, A30P or A53T upon aging, in vitro. The role of Hsp104p was also addressed in dissociation of pre-formed aggregates of synuclein mutants. Significant protection in fibril formation was observed by wild-type Hsp104p regardless of ATP presence, not by mutant Hsp104p. To a lesser extent, the dissociation effect of wild-type Hsp104p was observed only in the presence of ATP. These results will be discussed in relation to the development of an antioxidant approach to prevent amyloid fibril formation in several neurodegenerative diseases.

Keywords: hsp104p, molecular chaperone, synuclein, aggregation

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 10
ISSUE: 5
Year: 2003
Page: [491 - 495]
Pages: 5
DOI: 10.2174/0929866033478717
Price: $58

Article Metrics

PDF: 1