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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-2-3
pubmed:abstractText
In the present study we measured the levels of protein carbolnyls and the H and L subunits of ferritin in three hind limb muscles, [Extensor digitorum longus, Tibialis anterior and Soleus] of transgenic rats bearing the G93A hmSOD1 gene and of their non-transgenic littermates. All of the muscles from the transgenic animals showed significantly higher protein carbonyl levels, compared to the respective muscles from control non-transgenic animals. In two muscles (Tibialis anterior and Soleus) from transgenic rats, both L and H subunits of ferritin were upregulated. Moreover, we observed that the electrophoretic mobility of both ferritin subunits was retarded which indicates their post-translational modification. Ferritin immunoprecipitation experiments show an increased ubiquitination of both H and L ferritin in all muscles from the transgenic animals. Our data show for the first time that ferritin ubiquitination could be responsible for oxidative stress in muscles of rats bearing the G93A hmSOD1, consequently ferritin is not able to control the labile iron pool.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1873-2364
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-33
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Up-regulation of ferritin ubiquitination in skeletal muscle of transgenic rats bearing the G93A hmSOD1 gene mutation.
pubmed:affiliation
Department of Bioenergetics and Physiology of Exercise, Medical University of Gdansk, Poland.
pubmed:publicationType
Journal Article