DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ha, Yong-Hwang | ko |
dc.contributor.author | Liew, Hyun-Jeong | ko |
dc.contributor.author | Park, Hyun-Young | ko |
dc.contributor.author | Kim, Ki-Bong | ko |
dc.contributor.author | Suh, Yoo-Hun | ko |
dc.contributor.author | Churchill, David G | ko |
dc.date.accessioned | 2013-03-11T04:38:02Z | - |
dc.date.available | 2013-03-11T04:38:02Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2011-10 | - |
dc.identifier.citation | NEUROSCIENCE RESEARCH, v.71, no.2, pp.168 - 177 | - |
dc.identifier.issn | 0168-0102 | - |
dc.identifier.uri | http://hdl.handle.net/10203/98267 | - |
dc.description.abstract | In this study, alpha-synuclein was treated in vitro with salicylaldehyde (SA), lysine (lys) and Mn+ (Cu2+ or Zn2+) in various ratios. SA induced aggregation of alpha-syn in the ratio of 1:500 (alpha-syn:SA) after incubation (pH 7.4, PBS buffer, 16-24 h). Free lys can thus scavenge SA, inhibiting the aggregation of alpha-syn up to similar to 63% (alpha-syn:SA:lys = 1:1000:5000). When Cu2+ and Zn2+ are added to SA and alpha-syn, protein aggregation is induced. In the case of Zn2+, the aggregation of alpha-syn increased to 74% (ratio = 1:1000:50). Fluorescence studies support the production of protein-bound Zn2+-salicylaldimine species. For Cu2+, aggregation of alpha-syn was shown (138%). Thus, possible protective or inducing effects of lys, Cu2+ and Zn2+ may exist with alpha-syn. alpha-Syn, SA and Cu2+ can undergo complexation (fluorescence. CD and MALDI data). Cellular toxicity of SA (700 mu M). Zn2+ (700 mu M) and Cu2+ (700 mu M) on SH-SY5Y (1 x 10(5) cells) showed 9.8%, 38.0% and 14.4% compared to control values. Combinations showed more severe toxicities: 71.9% and 93.1% for SA (70 mu M) + Cu2+ (700 mu M) and SA (70 mu M) + Zn2+ (700 mu M), respectively, suggesting complexation itself may be toxic. (C) 2011 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved. | - |
dc.language | English | - |
dc.publisher | ELSEVIER IRELAND LTD | - |
dc.subject | TOXIC DOPAMINE METABOLITE | - |
dc.subject | N-TERMINAL FRAGMENTS | - |
dc.subject | BLOOD-BRAIN-BARRIER | - |
dc.subject | PARKINSONS-DISEASE | - |
dc.subject | OXIDATIVE STRESS | - |
dc.subject | ELEVATED LEVELS | - |
dc.subject | LEWY BODIES | - |
dc.subject | 3,4-DIHYDROXYPHENYLACETALDEHYDE | - |
dc.subject | ALDEHYDE | - |
dc.subject | PRODUCTS | - |
dc.title | Interplay of salicylaldehyde, lysine, and M(2+) ions on alpha-synuclein aggregation: Cancellation of aggregation effects and determination of salicylaldehyde neurotoxicity | - |
dc.type | Article | - |
dc.identifier.wosid | 000295556600009 | - |
dc.identifier.scopusid | 2-s2.0-80052385533 | - |
dc.type.rims | ART | - |
dc.citation.volume | 71 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 168 | - |
dc.citation.endingpage | 177 | - |
dc.citation.publicationname | NEUROSCIENCE RESEARCH | - |
dc.contributor.localauthor | Churchill, David G | - |
dc.contributor.nonIdAuthor | Liew, Hyun-Jeong | - |
dc.contributor.nonIdAuthor | Suh, Yoo-Hun | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | alpha-Synuclein | - |
dc.subject.keywordAuthor | Salicylaldehyde | - |
dc.subject.keywordAuthor | L-Lysine | - |
dc.subject.keywordAuthor | Zinc(II) | - |
dc.subject.keywordAuthor | Copper(II) | - |
dc.subject.keywordAuthor | Protein aggregation | - |
dc.subject.keywordPlus | TOXIC DOPAMINE METABOLITE | - |
dc.subject.keywordPlus | N-TERMINAL FRAGMENTS | - |
dc.subject.keywordPlus | BLOOD-BRAIN-BARRIER | - |
dc.subject.keywordPlus | PARKINSONS-DISEASE | - |
dc.subject.keywordPlus | OXIDATIVE STRESS | - |
dc.subject.keywordPlus | ELEVATED LEVELS | - |
dc.subject.keywordPlus | LEWY BODIES | - |
dc.subject.keywordPlus | 3,4-DIHYDROXYPHENYLACETALDEHYDE | - |
dc.subject.keywordPlus | ALDEHYDE | - |
dc.subject.keywordPlus | PRODUCTS | - |
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