Source:http://linkedlifedata.com/resource/pubmed/id/11961126
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
2002-4-18
|
pubmed:abstractText |
Thyroid hormone [triiodothyronine (T3)] positively regulates NADPH cytochrome P450 reductase (P450R) mRNA expression in rat liver, with P450R transcription initiation being a key regulated step. T3 is presently shown to have significant post-transcriptional effects on P450R expression. T3 increased the size of cytoplasmic P450R mRNA by approximately 105 nucleotides 12 h after T3 treatment, followed by a return to basal levels at 24 h. Primer extension analysis and Northern hybridization with 5'-untranslated region probes revealed no change in P450R mRNA 5' structure with T3 treatment. By contrast, RNase H analysis revealed a transient, T3-induced increase in P450R mRNA poly(A) tail, from approximately 100 to approximately 205 A. This increase in P450R polyadenylation, detectable in the nucleus 8 h after T3 treatment and in the cytoplasm at 12 h, was transient and was reversed by 16 h, when the T3-induced accumulation of cytoplasmic P450R mRNA was near maximal. Actinomycin D blocked the increase in P450R poly(A) tail and the induction of P450R mRNA, indicating a requirement for ongoing gene transcription for both T3 responses. T3 treatment destabilized P450R mRNA in rat liver in vivo, as shown by the T3-dependent 6-fold decrease in cytoplasmic P450R mRNA half-life, from a basal value of >or=16 h in uninduced liver to approximately 2.5 h, measured 24 h after T3 administration. These findings demonstrate that T3 increases nuclear polyadenylation of P450R RNA as a transient, early regulatory response and that this response is temporally dissociated from the subsequent decrease in cytoplasmic P450R mRNA stability.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3' Untranslated Regions,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH-Ferrihemoprotein Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease H,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Triiodothyronine
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0026-895X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
61
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1089-96
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11961126-3' Untranslated Regions,
pubmed-meshheading:11961126-Animals,
pubmed-meshheading:11961126-Cell Nucleus,
pubmed-meshheading:11961126-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11961126-Half-Life,
pubmed-meshheading:11961126-Male,
pubmed-meshheading:11961126-NADPH-Ferrihemoprotein Reductase,
pubmed-meshheading:11961126-Poly A,
pubmed-meshheading:11961126-Polyadenylation,
pubmed-meshheading:11961126-RNA, Messenger,
pubmed-meshheading:11961126-RNA Stability,
pubmed-meshheading:11961126-Rats,
pubmed-meshheading:11961126-Rats, Inbred F344,
pubmed-meshheading:11961126-Ribonuclease H,
pubmed-meshheading:11961126-Thyroid Hormones,
pubmed-meshheading:11961126-Transcription, Genetic,
pubmed-meshheading:11961126-Triiodothyronine
|
pubmed:year |
2002
|
pubmed:articleTitle |
Post-transcriptional regulation of hepatic NADPH-cytochrome P450 reductase by thyroid hormone: independent effects on poly(A) tail length and mRNA stability.
|
pubmed:affiliation |
Division of Cell and Molecular Biology, Department of Biology, Boston University, Boston, Massachusetts, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|