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Adherent Monomer-Misfolded SOD1 英文参考文献
AdherentMonomer-MisfoldedSOD1
YasuhiroWatanabe*,EriMorita,YasuyoFukada,KojiDoi,KenichiYasui,MichioKitayama,Toshiya
Nakano,KenjiNakashima
DepartmentofNeurology,InstituteofNeurologicalSciences,FacultyofMedicine,TottoriUniversity,Yonago,Japan
Abstract
Background:Multiplecellularfunctionsarecompromisedinamyotrophiclateralsclerosis(ALS).InfamilialALS(FALS)with
Cu/Znsuperoxidedismutase(SOD1)mutations,themechanismsbywhichthemutationinSOD1leadstosuchawiderange
ofabnormalitiesremainselusive.
Methodology/PrincipalFindings:ToinvestigateunderlyingcellularconditionscausedbytheSOD1mutation,weexplored
mutant SOD1-interacting proteins in the spinal cord of symptomatic transgenic mice expressing a mutant SOD1,
SOD1Leu126delTT withaFLAGsequence(DFmice).Thisgeneproductisstructurallyunabletoformafunctionalhomodimer.
Tissues were obtained from both DF mice and disease-free mice expressing wild-type with FLAG SOD1 (WF mice). Both
FLAG-taggedSOD1andcross-linkingproteinswereenrichedandsubjectedtoashotgunproteomicanalysis.Weidentified
34 proteins (or protein subunits) in DF preparations, while in WF preparations, interactions were detected with only 4
proteins.
Conclusions/Significance: These results indicate that disease-causing mutant SOD1 likely leads to inadequate protein-
proteininteractions.ThiscouldbeanearlyandcrucialprocessinthepathogenesisofFALS.
Citation: Watanabe Y, Morita E, Fukada Y, Doi K, Yasui K, et al. (2008) Adherent Monomer-Misfolded SOD1. PLoS ONE 3(10): e3497. doi:10.1371/
journal.pone.0003497
Editor:UlrichMueller,UniversityofGiessen,Germany
ReceivedAugust14,2008;AcceptedSeptember22,2008;PublishedOctober23,2008
Copyright: ? 2008 Watanabe et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits
unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited.
Funding:AGrant-in-AidforScientificResearchfromtheMinistryofEducation,Culture,Sports,ScienceandTechnologyofJa
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