Linked Life Data

17584300

Source:http://linkedlifedata.com/resource/pubmed/id/17584300

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2007-6-22
pubmed:abstractText
Abnormal protein aggregates are commonly observed in affected neurons in many neurodegenerative disorders. We have reported that valosin-containing protein (VCP) co-localizes with protein aggregates in patients' neurons and in cultured cells expressing diseased proteins. However, the significance of such co-localization remains elucidated. Here we report the involvement of VCP in the re-solubilization process of abnormal protein aggregates. VCP recognized and accumulated onto pre-formed protein aggregates created by proteasome inhibition. VCP knockdown or the expression of dominant-negative VCP both significantly delayed the elimination of ubiquitin-positive aggregates. VCP was involved in the clearance of pre-formed polyglutamine aggregates as well. Paradoxically, VCP knockdown also diminished polyglutamine aggregate formation. Furthermore, its ATPase activity was required for the re-solubilization and re-activation of heat-denatured proteins, such as luciferase, from insoluble aggregates. We thus propose that VCP functions as a mediator for both aggregate formation and clearance depending upon the concentration of soluble aggregate-prone proteins, indicating dual VCP functions as an aggregate formase and an unfoldase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1356-9597
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
889-901
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Involvement of valosin-containing protein (VCP)/p97 in the formation and clearance of abnormal protein aggregates.
pubmed:affiliation
Laboratory of Functional Biology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't