PMID- 8647322
OWN - NLM
STAT- MEDLINE
DCOM- 19960725
LR  - 20191210
IS  - 0303-7207 (Print)
IS  - 0303-7207 (Linking)
VI  - 116
IP  - 2
DP  - 1996 Feb 5
TI  - Crosstalk between the thyroid hormone and peroxisome proliferator-activated 
      receptors in regulating peroxisome proliferator-responsive genes.
PG  - 213-21
AB  - Peroxisome proliferators and thyroid hormones have overlapping metabolic effects 
      and regulate a similar subset of genes involved in maintaining lipid homeostasis. 
      Transcriptional activation by peroxisome proliferators is mediated by peroxisome 
      proliferator-activated receptors (PPARs) that bind to specific peroxisome 
      proliferator-response elements (PPREs) through heterodimerization with retinoid X 
      receptors (RXRs). We examined the effect of thyroid hormone receptor alpha (TR 
      alpha) on DNA binding in vitro and transcriptional activation in vivo by rat 
      PPAR. Gel mobility shift assays using in vitro translated receptors demonstrated 
      that TR alpha was capable of binding on its own and cooperatively with RXR alpha 
      to the rat acyl-CoA oxidase PPRE and of inhibiting the binding of rat PPAR/RXR 
      alpha heterodimers to this element. This inhibition was the result of competition 
      between TR alpha and PPAR for limiting amounts of the heterodimerization partner 
      RXR alpha and for binding to the PPRE. Interestingly, cotransfection of a TR 
      alpha expression plasmid into mammalian cells resulted in potentiation of the 
      peroxisome proliferator- and PPAR/RXR alpha-dependent transcriptional induction 
      of a reporter gene containing the acyl-CoA oxidase PPRE. TR alpha therefore 
      appears to cooperate with RXR and PPAR to positively modulate peroxisome 
      proliferator-dependent transactivation in vivo. Our findings suggest that there 
      is crosstalk between the thyroid hormone and peroxisome proliferator signaling 
      pathways in the regulation of peroxisome proliferator-responsive genes.
FAU - Hunter, J
AU  - Hunter J
AD  - Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
FAU - Kassam, A
AU  - Kassam A
FAU - Winrow, C J
AU  - Winrow CJ
FAU - Rachubinski, R A
AU  - Rachubinski RA
FAU - Capone, J P
AU  - Capone JP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Ireland
TA  - Mol Cell Endocrinol
JT  - Molecular and cellular endocrinology
JID - 7500844
RN  - 0 (Macromolecular Substances)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Receptors, Thyroid Hormone)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Thyroid Hormones)
RN  - 0 (Transcription Factors)
RN  - 9007-49-2 (DNA)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.3.3.6 (Acyl-CoA Oxidase)
SB  - IM
MH  - Acyl-CoA Oxidase
MH  - Animals
MH  - Base Sequence
MH  - Binding, Competitive
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - DNA/*metabolism
MH  - Gene Expression
MH  - Kidney
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - Oxidoreductases/genetics
MH  - Rats
MH  - Receptors, Cytoplasmic and Nuclear/drug effects/*physiology
MH  - Receptors, Retinoic Acid/metabolism
MH  - Receptors, Thyroid Hormone/genetics/physiology
MH  - Retinoid X Receptors
MH  - Signal Transduction
MH  - Thyroid Hormones/*pharmacology
MH  - Transcription Factors/drug effects/metabolism/*physiology
MH  - Transfection
EDAT- 1996/02/05 00:00
MHDA- 1996/02/05 00:01
CRDT- 1996/02/05 00:00
PHST- 1996/02/05 00:00 [pubmed]
PHST- 1996/02/05 00:01 [medline]
PHST- 1996/02/05 00:00 [entrez]
AID - 0303720795037179 [pii]
AID - 10.1016/0303-7207(95)03717-9 [doi]
PST - ppublish
SO  - Mol Cell Endocrinol. 1996 Feb 5;116(2):213-21. doi: 10.1016/0303-7207(95)03717-9.