Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease
DC Field | Value | Language |
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dc.contributor.author | Kang, Hyo Jung | - |
dc.contributor.author | Yoon, Won Joo | - |
dc.contributor.author | Moon, Gyeong Joon | - |
dc.contributor.author | Kim, Doo Yeon | - |
dc.contributor.author | Sohn, Seonghyang | - |
dc.contributor.author | Kwon, Hyuk Jae | - |
dc.contributor.author | Gwag, Byoung Joo | - |
dc.date.available | 2019-09-30T02:09:00Z | - |
dc.date.issued | 2005-04 | - |
dc.identifier.issn | 0969-9961 | - |
dc.identifier.issn | 1095-953X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/36700 | - |
dc.description.abstract | Excitotoxicity, oxidative stress, and apoptosis have been recognized as routes to neuronal death in various neurological diseases. We examined the possibility that PHF-1 tau, a substrate for various proteases, would be selectively cleaved depending upon routes of neuronal death. Cleavage form of PHF-1 tau was not observed in cortical cell cultures exposed to excitotoxins or oxidative stress that cause neuronal cell necrosis. PHF-1 tau was cleaved within 8 h following exposure of cortical cell cultures to apoptosis-inducing agents. This cleavage was blocked by inclusion of zDEVD-fmk, an inhibitor of caspase-3, and accompanied by activation of caspase-3. Levels and cleavage of PHF-1 tau were markedly increased in AD brain compared with control. Moreover, PHF-1 tau and active caspase-3 were colocalized mostly in tangle-bearing neurons. The current findings suggest that PHF-1 tau is cleaved by caspase-3 during apoptosis and neurodegenerative process in AD. (c) 2005 Elsevier Inc. All rights reserved. | - |
dc.format.extent | 9 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Caspase-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.nbd.2004.12.004 | - |
dc.identifier.bibliographicCitation | NEUROBIOLOGY OF DISEASE, v.18, no.3, pp 450 - 458 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000227820500004 | - |
dc.identifier.scopusid | 2-s2.0-14744300176 | - |
dc.citation.endPage | 458 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 450 | - |
dc.citation.title | NEUROBIOLOGY OF DISEASE | - |
dc.citation.volume | 18 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | Alzheimer's disease | - |
dc.subject.keywordAuthor | neurofibrillary tangles | - |
dc.subject.keywordAuthor | caspase-3 | - |
dc.subject.keywordAuthor | apoptosis | - |
dc.subject.keywordAuthor | tau | - |
dc.subject.keywordAuthor | glutamate | - |
dc.subject.keywordPlus | CULTURED CORTICAL-NEURONS | - |
dc.subject.keywordPlus | NEUROFIBRILLARY PATHOLOGY | - |
dc.subject.keywordPlus | GLUTAMATE TRANSPORT | - |
dc.subject.keywordPlus | TRANSGENIC MICE | - |
dc.subject.keywordPlus | CELL-DEATH | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | NECROSIS | - |
dc.subject.keywordPlus | NEURODEGENERATION | - |
dc.relation.journalResearchArea | Neurosciences & Neurology | - |
dc.relation.journalWebOfScienceCategory | Neurosciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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