Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-11-17
pubmed:abstractText
Peroxisome proliferators and thyroid hormones have a number of common metabolic effects. The possibility that the signal transduction pathways of both groups of effectors converge at the receptor level was investigated. It was shown that T3, specifically bound to the rat thyroid beta-receptor, was not displaced to a significant extent by ciprofibrate or bezafibrate. No specific binding of T3 to the mouse peroxisome proliferator activated receptor could be demonstrated. In transactivation experiments peroxisome proliferators were unable to activate the thyroid receptor and T3 did not activate a chimeric receptor containing the ligand binding domain of the peroxisome proliferator activated receptor. It is concluded that peroxisome proliferators and thyroid hormone do not cross-react at the level of their nuclear receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
332
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Peroxisome proliferators and T3 operate by way of distinct receptors.
pubmed:affiliation
Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Catholic University of Leuven, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't