NDLI: ALS-linked mutant superoxide dismutase 1 (SOD1) alters mitochondrial protein composition and decreases protein import

Content Provider	PubMed Central
Author	Li, Quan Velde, Christine Vande Israelson, Adrian Xie, Jing Bailey, Aaron O. Dong, Meng-qui Chun, Seung-joo Roy, Tamal Winer, Leah Yates, John R. Capaldi, Roderick A. Cleveland, Don W. Miller, Timothy M.
Abstract	Mutations in superoxide dismutase 1 (SOD1) cause familial ALS. Mutant SOD1 preferentially associates with the cytoplasmic face of mitochondria from spinal cords of rats and mice expressing SOD1 mutations. Two-dimensional gels and multidimensional liquid chromatography, in combination with tandem mass spectrometry, revealed 33 proteins that were increased and 21 proteins that were decreased in SOD1G93A rat spinal cord mitochondria compared with SOD1WT spinal cord mitochondria. Analysis of this group of proteins revealed a higher-than-expected proportion involved in complex I and protein import pathways. Direct import assays revealed a 30% decrease in protein import only in spinal cord mitochondria, despite an increase in the mitochondrial import components TOM20, TOM22, and TOM40. Recombinant SOD1G93A or SOD1G85R, but not SOD1WT or a Parkinson's disease-causing, misfolded α-synucleinE46K mutant, decreased protein import by >50% in nontransgenic mitochondria from spinal cord, but not from liver. Thus, altered mitochondrial protein content accompanied by selective decreases in protein import into spinal cord mitochondria comprises part of the mitochondrial damage arising from mutant SOD1.
Related Links	http://dx.doi.org/10.1073/pnas.1014862107
Ending Page	21151
Page Count	6
Starting Page	21146
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	49
Volume Number	107
Language	English
Publisher	National Academy of Sciences
Publisher Date	2010-12-07
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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