Linked Life Data

12162447

Source:http://linkedlifedata.com/resource/pubmed/id/12162447

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-8-6
pubmed:abstractText
Almost all forms of reactive oxygen species (ROS) oxidize methionine residues of proteins to a mixture of the R- and S-isomers of methionine sulfoxide. Because organisms contain methionine sulfoxide reductases (Msr's) that can catalyze the thioredoxin-dependent reduction of the sulfoxides back to methionine, it was proposed that the cyclic oxidation/reduction of methionine residues might serve as antioxidants to scavenge ROS, and also to facilitate the regulation of critical enzyme activities. We summarize here results of studies showing that organisms possess two different forms of Msr--namely, MsrA that catalyzes reduction of the S-isomer and MsrB that catalyzes the reduction of the R-isomer. Deletion of the msrA gene in mice leads to increased sensitivity to oxidative stress and to a decrease (40%) in the maximum lifespan. This suggests that elimination of both Msr's would have more serious consequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:volume
234-235
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism.
pubmed:affiliation
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-8012, USA. erstadtman@nih.gov
pubmed:publicationType
Journal Article, Review