Linked Life Data

16954605

Source:http://linkedlifedata.com/resource/pubmed/id/16954605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-9-6
pubmed:abstractText
University of Oldenburg, Department of Biology, Molecular Neurobiology, D-26111 Oldenburg, Germany Ubiquitinated tau-positive inclusion bodies in oligodendrocytes are consistent features in a variety of neurodegenerative disorders, and their formation points to an underlying incapacity of the protein quality control system that normally prevents the accumulation of misfolded proteins. To study the consequences of proteasomal impairment, we have used an oligodendroglial cell line, namely OLN-t40 cells, genetically engineered to express the longest human tau isoform. Treatment of OLN-t40 cells with the proteasomal inhibitor MG-132 (0.5 microM, 18 h) caused the formation of large, nonfibrillary tau-positive aggregates containing the small HSP alphaB-crystallin and ubiquitin in the vicinity of the microtubule organizing center (MTOC). The sequestration of misfolded proteins into specialized regions, called aggresomes, in response to stress stimuli has been reported to be associated with a redistribution of intermediate filaments (IFs). In oligodendroglial cells, which do not contain a cytoplasmic IF system, aggresomelike inclusions were instead surrounded by bundles of MTs and contained clusters of mitochondria. Aggresome formation was prevented by both MT-stabilizing and -destabilizing drugs, indicating not only that an intact cytoskeleton but also the dynamic instability of the MT network is required. Furthermore, the binding of stress-induced alphaBcrystallin to the MTs points to a possible protective role during disease progression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0895-8696
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-68
pubmed:meshHeading
pubmed-meshheading:16954605-Alternative Splicing, pubmed-meshheading:16954605-Cell Line, pubmed-meshheading:16954605-Crystallins, pubmed-meshheading:16954605-Cysteine Proteinase Inhibitors, pubmed-meshheading:16954605-Heat-Shock Proteins, pubmed-meshheading:16954605-Humans, pubmed-meshheading:16954605-Inclusion Bodies, pubmed-meshheading:16954605-Leupeptins, pubmed-meshheading:16954605-Microtubule-Organizing Center, pubmed-meshheading:16954605-Microtubules, pubmed-meshheading:16954605-Mitochondria, pubmed-meshheading:16954605-Nocodazole, pubmed-meshheading:16954605-Oligodendroglia, pubmed-meshheading:16954605-Oxidative Stress, pubmed-meshheading:16954605-Paclitaxel, pubmed-meshheading:16954605-Protein Isoforms, pubmed-meshheading:16954605-Tubulin Modulators, pubmed-meshheading:16954605-Ubiquitin, pubmed-meshheading:16954605-tau Proteins
pubmed:year
2006
pubmed:articleTitle
The dynamic instability of microtubules is required for aggresome formation in oligodendroglial cells after proteolytic stress.
pubmed:affiliation
University of Oldenburg, Department of Biology, Molecular Neurobiology, D-26111 Oldenburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't