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DOI 10.1016/j.bbrc.2006.10.085
Title Small heat shock proteins protect against {alpha}-synuclein-induced toxicity and aggregation
Creator/Author Outeiro, Tiago Fleming [Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129 (United States)] ; Klucken, Jochen [Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129 (United States)] ; Strathearn, Katherine E. [Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907-2091 (United States)] ; Liu Fang [Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907-2091 (United States)] ; Nguyen, Paul [Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129 (United States)] ; Rochet, Jean-Christophe [Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907-2091 (United States)] ; Hyman, Bradley T. [Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129 (United States)] ; McLean, Pamela J. [Alzheimer's Research Unit, MassGeneral Institute for Neurodegenerative Disease, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129 (United States)]. E-mail: touteiro@partners.org
Publication Date2006 Dec 22
OSTI IdentifierOSTI ID: 20857925
Other Number(s)Journal ID: ISSN 0006-291X; BBRCA9; TRN: US07R0409030105
Resource TypeJournal Article
Resource RelationJournal: Biochemical and Biophysical Research Communications; Journal Volume: 351; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2006.10.085; PII: S0006-291X(06)02327-8; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Subject60 APPLIED LIFE SCIENCES; AGGLOMERATION; CELL CULTURES; HEAT-SHOCK PROTEINS; MESSENGER-RNA; NERVOUS SYSTEM DISEASES; POLYMERASE CHAIN REACTION; QUALITY CONTROL; TOXICITY
Description/Abstract 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 {alpha}B-crystallin, in LB diseases. We demonstrate, via quantitative PCR, that Hsp27 messenger RNA levels are {approx}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 {approx}80% in a culture model while {alpha}B-crystallin reduces toxicity by {approx}20%. In addition, intracellular inclusions were immunopositive for endogenous Hsp27, and overexpression of this protein reduced aSyn aggregation in a cell culture model.
Country of PublicationUnited States
LanguageEnglish
FormatSize: page(s) 631-638
System Entry Date2007 May 07

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