Linked Life Data

12730456

Source:http://linkedlifedata.com/resource/pubmed/id/12730456

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5 Suppl 1
pubmed:dateCreated
2003-5-5
pubmed:abstractText
Biological functions of selenium are exerted by selenoproteins that contain selenocysteine in their primary structure. Selenocysteine is synthesized and inserted into proteins cotranslationally by a complex process. Families of selenoproteins include the glutathione peroxidases, the iodothyronine deiodinases and the thioredoxin reductases. These are redox enzymes that take advantage of the chemical properties of selenium to catalyze, respectively, removal of hydroperoxides by glutathione, deiodination of thyroid hormones and support of cellular processes requiring reduction of disulfides. Approximately 10 additional selenoproteins have been identified. One of them, selenoprotein P, is an extracellular protein that contains most of the selenium in plasma. It associates with endothelial cells, probably through its heparin-binding properties. Selenoprotein P has been postulated to protect against oxidative injury and to transport selenium from the liver to peripheral tissues. Selenium-dependent protection against diquat-induced liver necrosis and lipid peroxidation in the rat correlates with the presence of selenoprotein P. Recent results support a transport function. When (75)SeO(3)(2-) was administered intravenously to rats, liver tissue took up (75)Se within minutes, associated with a rapid decline in plasma (75)Se. Brain tissue did not begin accumulating (75)Se until (75)Se-labeled selenoprotein P had begun appearing in the plasma after 30 min. These results suggest that tissues like liver can take up small-molecule forms of selenium whereas presence of the element in selenoprotein P facilitates uptake by tissues like brain. Thus, there is evidence for both antioxidant and selenium transport functions of selenoprotein P.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3166
pubmed:author
pubmed:issnType
Print
pubmed:volume
133
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1517S-20S
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Selenoprotein metabolism and function: evidence for more than one function for selenoprotein P.
pubmed:affiliation
Division of Gastroenterology, Department of Medicine and Clinical Nutrition Research Unit, Vanderbilt University School of Medicine, Nashville, TN 37232-2279, USA. raymond.burk@vanderbilt.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review