Proteomic analysis of glutamate-induced toxicity in HT22 cells

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dc.contributor.authorYou Ra Lee-
dc.contributor.authorH W Park-
dc.contributor.authorSung Goo Park-
dc.contributor.authorS Cho-
dc.contributor.authorP K Myung-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorDo Hee Lee-
dc.date.accessioned2017-04-19T09:06:31Z-
dc.date.available2017-04-19T09:06:31Z-
dc.date.issued2007-
dc.identifier.issn1615-9853-
dc.identifier.uri10.1002/pmic.200600644ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7769-
dc.description.abstractIn the present study, we have investigated the proteome changes associated with glutamate-induced HT22 cell death, a model system to study oxidative stress-mediated toxicity. Among a number of HT22 proteins exhibiting altered expression, several molecular chaperones demon-strated substantial changes. For example, the levels of Hsp90 and Hsp70 decreased as cell death progressed whereas that of Hsp60 increased dramatically. Interestingly, cytosolic Hsp60 increased more prominently than mitochondrial Hsp60. Concomitantly, the accumulation of poly-ubiquitylated proteins and differential regulation of the peptidase activities and the subunits of 26S proteasomes were observed in glutamate-treated HT22 cells. Our findings that the molecular chaperones and the ubiquitin-proteasome system undergo changes during glutamate-induced HT22 cell death may suggest the importance of a protein quality control system in oxidative damage-mediated toxicity.-
dc.publisherWiley-
dc.titleProteomic analysis of glutamate-induced toxicity in HT22 cells-
dc.title.alternativeProteomic analysis of glutamate-induced toxicity in HT22 cells-
dc.typeArticle-
dc.citation.titleProteomics-
dc.citation.number2-
dc.citation.endPage193-
dc.citation.startPage185-
dc.citation.volume7-
dc.contributor.affiliatedAuthorYou Ra Lee-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorDo Hee Lee-
dc.contributor.alternativeName이유라-
dc.contributor.alternativeName박혜원-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName명평근-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName이도희-
dc.identifier.bibliographicCitationProteomics, vol. 7, no. 2, pp. 185-193-
dc.identifier.doi10.1002/pmic.200600644-
dc.subject.keywordglutamate-
dc.subject.keywordHT22-
dc.subject.keywordmolecular chaperones-
dc.subject.keywordoxidative stress-
dc.subject.keywordubiquitin-proteasome system-
dc.subject.localGlutamate-
dc.subject.localglutamate-
dc.subject.localHT22-
dc.subject.localmolecular chaperone-
dc.subject.localMolecular chaperones-
dc.subject.localmolecular chaperones-
dc.subject.localMolecular chaperone-
dc.subject.localOxidative stre-
dc.subject.localOxidative stress-
dc.subject.localOXIDATIVE STRESS-
dc.subject.localOxidative Stress-
dc.subject.localoxidative stress-
dc.subject.localubiquitin-proteasome system-
dc.subject.localUbiquitin-proteasome system-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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