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Characterization and Hsp104-induced artificial clearance of familial ALS-related SOD1 aggregates

Authors
Kim, YongminPark, Ju-HwangJang, Ja-YoungRhim, HyangshukKang, Seongman
Issue Date
10-5월-2013
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Mutant SOD1; Amyotrophic lateral sclerosis; Hsp104; SOD1 aggregate; FLIP
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.434, no.3, pp.521 - 526
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
434
Number
3
Start Page
521
End Page
526
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103237
DOI
10.1016/j.bbrc.2013.03.107
ISSN
0006-291X
Abstract
Hsp104, a molecular chaperone protein, originates from Saccharomyces cerevisiae and shows potential for development as a therapeutic disaggregase for the treatment of neurodegenerative disorders. This study shows that aggregates of mutant superoxide dismutase 1 (SOD1), which cause amyotrophic lateral sclerosis (ALS), are disaggregated by Hsp104 in an ATP-dependent manner. Mutant SOD1 aggregates were first characterized using fluorescence loss in photobleaching experiments based on the reduced mobility of aggregated proteins. Hsp104 restored the mobility of mutant SOD1 proteins to a level comparable with that of the wild-type. However, ATPase-deficient Hsp104 mutants did not restore mobility, suggesting that, rather than preventing aggregation, Hsp104 disaggregates mutant SOD1 after it has aggregated. Despite the restored mobility, however, mutant SOD1 proteins existed as trimers or other higher-order structures, rather than as naturally occurring dimers. This study sheds further light on the mechanisms underlying the disaggregation of SOD1 mutant aggregates in ALS. (C) 2013 Elsevier Inc. All rights reserved.
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