Linked Life Data

17628004

Source:http://linkedlifedata.com/resource/pubmed/id/17628004

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2007-9-18
pubmed:abstractText
The type 2 deiodinase (D2) activates thyroid hormone and constitutes an important source of 3,5,3',-triiodothyronine in the brain. D2 is inactivated via WSB-1 mediated ubiquitination but can be rescued from proteasomal degradation by USP-33 mediated deubiquitination. Using an in silico analysis of published array data, we found a significant positive correlation between the relative mRNA expression levels of WSB-1 and USP-33 in a set of 56 mouse tissues (r = 0.08; P < 0.04). Subsequently, we used in situ hybridization combined with immunocytochemistry in rat brain to show that in addition to neurons, WSB-1 and USP-33 are differently expressed in astrocytes and tanycytes, the two main D2 expressing cell types in this tissue. Tanycytes, which are thought to participate in the feedback regulation of TRH neurons express both WSB-1 and USP-33, indicating the potential for D2 ubiquitination and deubiquitination in these cells. Notably, only WSB-1 is expressed in glial fibrillary acidic protein-positive astrocytes throughout the brain. Although developmental and environmental signals are known to regulate the expression of WSB-1 and USP-33 in other tissues, our real-time PCR studies indicate that changes in thyroid status do not affect the expression of these genes in several rat brain regions, whereas in the mediobasal hypothalamus, changes in gene expression were minimal. In conclusion, the correlation between the relative mRNA levels of WSB-1 and USP-33 in numerous tissues that do not express D2 suggests that these ubiquitin-related enzymes share additional substrates besides D2. Furthermore, the data indicate that changes in WSB-1 and USP-33 expression are not part of the brain homeostatic response to hypothyroidism or hyperthyroidism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4865-74
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed-meshheading:17628004-Animals, pubmed-meshheading:17628004-Astrocytes, pubmed-meshheading:17628004-Brain, pubmed-meshheading:17628004-Carrier Proteins, pubmed-meshheading:17628004-Computer Systems, pubmed-meshheading:17628004-Endopeptidases, pubmed-meshheading:17628004-Glial Fibrillary Acidic Protein, pubmed-meshheading:17628004-Hyperthyroidism, pubmed-meshheading:17628004-Hypothyroidism, pubmed-meshheading:17628004-Immunohistochemistry, pubmed-meshheading:17628004-In Situ Hybridization, pubmed-meshheading:17628004-Iodide Peroxidase, pubmed-meshheading:17628004-Male, pubmed-meshheading:17628004-Mice, pubmed-meshheading:17628004-Neurons, pubmed-meshheading:17628004-Polymerase Chain Reaction, pubmed-meshheading:17628004-Protein Processing, Post-Translational, pubmed-meshheading:17628004-RNA, Messenger, pubmed-meshheading:17628004-Rats, pubmed-meshheading:17628004-Rats, Wistar, pubmed-meshheading:17628004-Tissue Distribution
pubmed:year
2007
pubmed:articleTitle
Expression patterns of WSB-1 and USP-33 underlie cell-specific posttranslational control of type 2 deiodinase in the rat brain.
pubmed:affiliation
Institute of Experimental Medicine, Laboratory of Endocrine Neurobiology, Hungarian Academy of Sciences, Szigony u. 43, Budapest H-1083, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural