Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2009-9-24
pubmed:abstractText
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease caused by the degeneration of motor neurons. Mutations in Cu/Zn superoxide dismutase (SOD1), including G93A, were reportedly linked to familial ALS. SOD1 is a key antioxidant enzyme, and is also one of the major targets for oxidative damage in the brains of patients suffering from Alzheimers disease (AD). Several lines of evidence suggest that intracellular amyloid beta (Abeta) is associated with the pathogenesis of AD. In this report we demonstrate that intracellular Abeta directly interacts with SOD1, and that this interaction decreases the enzymatic activity of the enzyme. We observed Abeta-SOD1 aggregates in the perinuclear region of H4 cells, and mapped the SOD1 binding region to Abeta amino acids 26-42. Interestingly, intracellular Ab binds to the SOD1 G93A mutant with greater affinity than to wild-type SOD1. This resulted in considerably less mutant enzymatic activity. Our study implicates a potential role for Abeta in the development of ALS by interacting with the SOD1 G93A mutant.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-10486579, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-10623648, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-10809401, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-11861655, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-12427831, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-12864925, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-15036614, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-15485483, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-15548589, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-15592359, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-15952898, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-16626394, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-16781128, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-16968707, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-18059133, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-18368143, http://linkedlifedata.com/resource/pubmed/commentcorrection/19478559-9108116
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1226-3613
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
611-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Intracellular amyloid beta interacts with SOD1 and impairs the enzymatic activity of SOD1: implications for the pathogenesis of amyotrophic lateral sclerosis.
pubmed:affiliation
School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't