Linked Life Data

17882015

Source:http://linkedlifedata.com/resource/pubmed/id/17882015

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2007-9-20
pubmed:abstractText
Degenerative diseases with abnormal protein aggregates are characterized by the accumulation of proteins with variable posttranslational modifications including phosphorylation, glycoxidation, oxidation, and nitration. Myofibrillar myopathies, including myotilinopathies and desminopathies, are characterized by the intracytoplasmic focal accumulation of proteins in insoluble aggregates in muscle cells. By using single immunohistochemistry, monodimensional gel electrophoresis and Western blotting, and bidimensional gel electrophoresis, in-gel digestion, and mass spectometry, desmin was demonstrated to be a major target of oxidation and nitration in both desminopathies and myotilinopathies. Because oxidized and nitrated proteins may have toxic effects and may impair ubiquitin-proteasomal function, modified desmin can be considered to be an additional element in the pathogenesis of myofibrillar myopathies. In addition to desmin, pyruvate kinase muscle splice form M1 is oxidized, thus supporting complemental mitochondrial damage, at least in some cases of myotilinopathy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-3069
pubmed:author
pubmed:issnType
Print
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
711-23
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Desmin is oxidized and nitrated in affected muscles in myotilinopathies and desminopathies.
pubmed:affiliation
Institut de Neuropatologia, Servei Anatomia Patològica, Institut d'Investigacio de Bellvitge-Hospital Universitari de Bellvitge, Hospitalet de Llobregat, Plataforma de Proteòmica, Barcelona Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't