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Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation.

Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Research Abstract Details 

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  • Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Abstract Text:

    tiago fleming outeiroTiago Fleming Outeiro,jochen kluckenJochen Klucken,katherine e strathearnKatherine E Strathearn,fang liuFang Liu,paul nguyenPaul Nguyen,jean-christophe rochetJean-Christophe Rochet,bradley t hymanBradley T Hyman,pamela j mcleanPamela J McLean,tiago fleming outeiroTiago Fleming Outeiro,jochen kluckenJochen Klucken,katherine e strathearnKatherine E Strathearn,fang liuFang Liu,paul nguyenPaul Nguyen,jean-christophe rochetJean-Christophe Rochet,bradley t hymanBradley T Hyman,pamela j mcleanPamela J McLean,

    Protein misfolding and inclusion formation are common events in neurodegenerative diseases, such as Parkinson's disease (PD), Alzheimer's disease (AD) or Huntington's disease (HD). Alpha-synuclein (aSyn) is the main protein component of inclusions called Lewy bodies (LB) which are pathognomic of PD, Dementia with Lewy bodies (DLB), and other diseases collectively known as LB diseases. Heat shock proteins (HSPs) are one class of the cellular quality control system that mediate protein folding, remodeling, and even disaggregation. Here, we investigated the role of the small heat shock proteins Hsp27 and alphaB-crystallin, in LB diseases. We demonstrate, via quantitative PCR, that Hsp27 messenger RNA levels are approximately 2-3-fold higher in DLB cases compared to control. We also show a corresponding increase in Hsp27 protein levels. Furthermore, we found that Hsp27 reduces aSyn-induced toxicity by approximately 80% in a culture model while alphaB-crystallin reduces toxicity by approximately 20%. In addition, intracellular inclusions were immunopositive for endogenous Hsp27, and overexpression of this protein reduced aSyn aggregation in a cell culture model.

    Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Publishing Authors By Initials

    tf outeiroTF Outeiro,j kluckenJ Klucken,ke strathearnKE Strathearn,f liuF Liu,p nguyenP Nguyen,jc rochetJC Rochet,bt hymanBT Hyman,pj mcleanPJ McLean,tf outeiroTF Outeiro,j kluckenJ Klucken,ke strathearnKE Strathearn,f liuF Liu,p nguyenP Nguyen,jc rochetJC Rochet,bt hymanBT Hyman,pj mcleanPJ McLean,

    For similar proteins: nerve tissue proteins: synucleins: alpha-synuclein research abstracts see: proteins: nerve tissue proteins: synucleins: alpha-synuclein research

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    Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Biochemical and biophysical research communication

    VOLUME: 351

    Page Numbers: 631-8

    Journal Abbreviation: Biochem. Biophys. Res. Commun.

    ISSN: 0006-291X

    DAY: 26

    MONTH: 10

    YEAR: 2006

    Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 372516

    Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Keywords Mesh Terms:

    KEYWORDS: alpha-Synuclein

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Information

    Substance Name: alpha-Synuclein

    Registry Number: 0

    Grant and Affiliation Information for Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation.

    AFFILIATION: Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, Charlestown, MA 02129, USA. touteir@partners.org

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NINDS

    GRANT: R01-NS049221

    ACRONYM: NS

    MEDLINETA: Biochem Biophys Res Commun

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    Number Hits: 0

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