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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-2-16
pubmed:abstractText
The thyroid gland is rich in selenium (Se) and expresses a variety of selenoproteins that are involved in antioxidative defense and metabolism of thyroid hormones (TH). Se deficiency impairs regular synthesis of selenoproteins and adequate TH metabolism. We recently generated mice that lack the plasma Se carrier, selenoprotein P (SePP). SePP-knockout mice display decreased serum Se levels and manifest growth defects and neurological abnormalities partly reminiscent of thyroid gland dysfunction or profound hypothyroidism. Thus, we probed the TH axis in developing and adult SePP-knockout mice. Surprisingly, expression of Se-dependent 5'-deiodinase type 1 was only slightly altered in liver, kidney, or thyroid at postnatal d 60, and 5'-deiodinase type 2 activity in brain was normal in SePP-knockout mice. Thyroid gland morphology, thyroid glutathione peroxidase activity, thyroid Se concentration, and serum levels of TSH, T4, or T3 were within normal range. Pituitary TSHbeta transcripts and hepatic 5'-deiodinase type 1 mRNA levels were unchanged, indicating regular T3 bioactivity in thyrotropes and hepatocytes. Cerebellar granule cell migration as a sensitive indicator of local T3 action during development was undisturbed. Collectively, these findings demonstrate that low levels of serum Se or SePP in the absence of other challenges do not necessarily interfere with regular functioning of the TH axis. 5'-deiodinase isozymes are preferentially supplied, and Se-dependent enzymes in the thyroid are even less-dependent on serum levels of Se or SePP than in brain. This indicates a top priority of the thyroid gland and its selenoenzymes with respect to the hierarchical Se supply within the organism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1306-13
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16322066-Animals, pubmed-meshheading:16322066-Blotting, Northern, pubmed-meshheading:16322066-Brain, pubmed-meshheading:16322066-Cell Movement, pubmed-meshheading:16322066-Cerebellum, pubmed-meshheading:16322066-Feedback, Physiological, pubmed-meshheading:16322066-Fluorometry, pubmed-meshheading:16322066-Gene Expression Regulation, pubmed-meshheading:16322066-Glutathione Peroxidase, pubmed-meshheading:16322066-Hepatocytes, pubmed-meshheading:16322066-Iodide Peroxidase, pubmed-meshheading:16322066-Mice, pubmed-meshheading:16322066-Mice, Knockout, pubmed-meshheading:16322066-Mice, Transgenic, pubmed-meshheading:16322066-Models, Biological, pubmed-meshheading:16322066-Pituitary Gland, pubmed-meshheading:16322066-RNA, Messenger, pubmed-meshheading:16322066-Selenium, pubmed-meshheading:16322066-Selenoprotein P, pubmed-meshheading:16322066-Thyroid Gland, pubmed-meshheading:16322066-Thyroid Hormones, pubmed-meshheading:16322066-Thyrotropin, pubmed-meshheading:16322066-Thyroxine, pubmed-meshheading:16322066-Tissue Distribution, pubmed-meshheading:16322066-Triiodothyronine
pubmed:year
2006
pubmed:articleTitle
Synthesis and metabolism of thyroid hormones is preferentially maintained in selenium-deficient transgenic mice.
pubmed:affiliation
Institut für Experimentelle Endokrinologie, Charité-Universitaetsmedizin Berlin, Schumannstrasse 20/21, D-10117 Berlin, Germany. lutz.schomburg@charite.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't