Linked Life Data

20089131

Source:http://linkedlifedata.com/resource/pubmed/id/20089131

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-7-26
pubmed:abstractText
Small heat shock proteins (sHsps) are characteristically observed in glial cell inclusion bodies in a variety of neurodegenerative diseases. The small Hsp27 (HspB1) is stress inducible and participates in the defence against misfolded proteins. Under normal conditions, it forms oligomeric structures with molecular masses ranging from 50 to 800 kDa. These structures are highly dynamic and their dynamic organization is regulated by phosphorylation, which has been suggested to be a crucial factor in modulating the activity of the protein. To investigate the responses of Hsp27 to stress induced by proteasomal inhibition, and its state of phosphorylation and oligomerization during aggregate formation, three oligodendroglial cell lines stably expressing Hsp27 were established: OLN27 wild type, OLN27DDD expressing triple mutant Hsp27 in its phosphorylation mimicking form, and OLN27AAA, expressing non-phosphorylatable Hsp27. Our data show that the proteasomal inhibitor MG-132 promotes Hsp27 phosphorylation by activation of p38 mitogen activated protein kinase and leads to the formation of small oligomers. However, Hsp27 is recruited to aggresomes independently of its state of phosphorylation. After 24 h of treatment, all three cell lines had formed protein accumulations in the vicinity of the centrosome, but in cells over-expressing Hsp27, aggresome formation was delayed in comparison with OLN-93 oligodendroglial cells not expressing Hsp27.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1471-4159
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
960-71
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Effect of proteasome inhibition by MG-132 on HSP27 oligomerization, phosphorylation, and aggresome formation in the OLN-93 oligodendroglia cell line.
pubmed:affiliation
University of Oldenburg, Department of Biology, Molecular Neurobiology, Oldenburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't