Linked Life Data

12205033

Source:http://linkedlifedata.com/resource/pubmed/id/12205033

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2002-9-2
pubmed:abstractText
The CAG/polyglutamine (polyGln)-related diseases include nine different members that together form the most common class of inherited neurodegenerative disorders; neurodegeneration is linked to the same type of mutation, found in unrelated genes, consisting of an abnormal expansion of a polyGln tract normally present in the wild-type proteins. Nuclear, cytoplasmic, or neuropil aggregates are detectable in CAG/polyGln-related diseases, but their role is still debated. Alteration of the androgen receptor (AR), one of these proteins, has been linked to spinal and bulbar muscular atrophy, an X-linked recessive disease characterized by motoneuronal death. By using immortalized motoneuronal cells (the neuroblastoma-spinal cord cell line NSC34), we analyzed neuropil aggregate formation and toxicity: green fluorescent protein-tagged wild-type or mutated ARs were cotransfected into NSC34 cells with a blue fluorescent protein tagged to mitochondria. Altered mitochondrial distribution was observed in neuronal processes containing aggregates; occasionally, neuropil aggregates and mitochondrial concentration corresponded to axonal swelling. Neuropil aggregates also impaired the distribution of the motor protein kinesin. These data suggest that neuropil aggregates may physically alter neurite transport and thus deprive neuronal processes of factors or components that are important for axonal and dendritic functions. The soma may then be affected, leading to neuronal dysfunctions and possibly to cell death.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1530-6860
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1418-20
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes.
pubmed:affiliation
Institute of Endocrinology, Centre of Excellence for the Study and Treatment of Neurodegenerative Diseases, University of Milan, Milano, Italy.
pubmed:publicationType
Journal Article