| pubmed-article:19835916 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0007412 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0085262 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0285890 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0277785 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C1155342 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:19835916 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:19835916 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19835916 | pubmed:dateCreated | 2010-2-1 | lld:pubmed |
| pubmed-article:19835916 | pubmed:abstractText | Parkinson's disease (PD) is a neurodegenerative disorder characterized by the selective loss of dopaminergic neurons and the presence of Lewy bodies. alpha-Synuclein is a major component of Lewy bodies. Recently, many studies have focused on the interaction between alpha-synuclein and catecholamine in the pathogenesis of PD. However, no detailed relationship between cathecholamine and alpha-synuclein cytotoxicity has been elucidated. Therefore, this study established PC12 cell lines which overexpress human alpha-synuclein in a tetracycline-inducible manner. The overexpression of human alpha-synuclein increased the number of apoptotic cells in a long-term culture. Moreover, human alpha-synuclein expressing PC12 cells demonstrated an increased vulnerability to several stressors in a short culture period. Thapsigargin increased the SDS soluble oligomers of alpha-synuclein associated with catecholamine-quinone. The unfolded protein response (UPR) study showed that thapsigargin increased eIF2alpha phosphorylation and nuclear GADD153/CHOP induction under alpha-synuclein overexpressed conditions. The activities of the ATF6alpha and IRE1alpha pathways decreased. These findings suggest that an overexpression of alpha-synuclein partly inactivates the UPR. alpha-Methyltyrosine inhibited the dysfunction of the UPR caused by an overexpression of human alpha-synuclein. Therefore, these findings suggest that the coexistence of human alpha-synuclein with catecholamine enhances the endoplasmic reticulum stress-related toxicity in PD pathogenesis. | lld:pubmed |
| pubmed-article:19835916 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19835916 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19835916 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19835916 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19835916 | pubmed:issn | 1872-8111 | lld:pubmed |
| pubmed-article:19835916 | pubmed:author | pubmed-author:ItoSatoruS | lld:pubmed |
| pubmed-article:19835916 | pubmed:author | pubmed-author:TakeshimaTaka... | lld:pubmed |
| pubmed-article:19835916 | pubmed:author | pubmed-author:NakashimaKenj... | lld:pubmed |
| pubmed-article:19835916 | pubmed:author | pubmed-author:ImamuraKeikoK | lld:pubmed |
| pubmed-article:19835916 | pubmed:author | pubmed-author:NakasoKazuhir... | lld:pubmed |
| pubmed-article:19835916 | pubmed:copyrightInfo | Copyright 2009 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved. | lld:pubmed |
| pubmed-article:19835916 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19835916 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:19835916 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19835916 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19835916 | pubmed:pagination | 124-30 | lld:pubmed |
| pubmed-article:19835916 | pubmed:meshHeading | pubmed-meshheading:19835916... | lld:pubmed |
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| pubmed-article:19835916 | pubmed:meshHeading | pubmed-meshheading:19835916... | lld:pubmed |
| pubmed-article:19835916 | pubmed:meshHeading | pubmed-meshheading:19835916... | lld:pubmed |
| pubmed-article:19835916 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19835916 | pubmed:articleTitle | Endogenous catecholamine enhances the dysfunction of unfolded protein response and alpha-synuclein oligomerization in PC12 cells overexpressing human alpha-synuclein. | lld:pubmed |
| pubmed-article:19835916 | pubmed:affiliation | Department of Neurology, Institute of Neurological Sciences, Faculty of Medicine, Tottori University, Japan. s-itou@med.tottori-u.ac.jp | lld:pubmed |
| pubmed-article:19835916 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19835916 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19835916 | lld:pubmed |
