Effects of dried natto diet on the transcript levels of the peroxisome proliferator‐activated receptor‐γ, coactivator‐1α and ‐1β, and nuclear receptor corepressor 1 genes in laying hens

2021 ◽  
Vol 92 (1) ◽  
Author(s):  
Yuta Seo ◽  
Takuya Kubota ◽  
Masami Sudo ◽  
Naomi Toda ◽  
Yasuki Ogawa ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Laying Hens ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Transcript Levels ◽  
Nuclear Receptor Corepressor

scholarly journals Identification of Nuclear Receptor Corepressor as a Peroxisome Proliferator-activated Receptor α Interacting Protein

1999 ◽  
Vol 274 (22) ◽  
pp. 15901-15907 ◽  
Author(s):  
Paul Dowell ◽  
Jane E. Ishmael ◽  
Dorina Avram ◽  
Valerie J. Peterson ◽  
Daniel J. Nevrivy ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Interacting Protein ◽  
Nuclear Receptor Corepressor

scholarly journals Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor δ-mediated transactivation

2002 ◽  
Vol 363 (1) ◽  
pp. 157 ◽  
Author(s):  
Anne-M. KROGSDAM ◽  
Curt A. F. NIELSEN ◽  
Søren NEVE ◽  
Dorte HOLST ◽  
Torben HELLEDIE ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Nuclear Receptor Corepressor

Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor δ-mediated transactivation

2002 ◽  
Vol 363 (1) ◽  
pp. 157-165 ◽  
Author(s):  
Anne-M. KROGSDAM ◽  
Curt A.F. NIELSEN ◽  
Søren NEVE ◽  
Dorte HOLST ◽  
Torben HELLEDIE ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptor ◽  
Hybrid System ◽  
Thyroid Hormone Receptor ◽  
Peroxisome Proliferator ◽  
Independent Manner ◽  
Peroxisome Proliferator Activated Receptor ◽  
Nuclear Receptor Corepressor ◽  
Two Hybrid

The nuclear receptor corepressor (NCoR) was isolated as a peroxisome-proliferator-activated receptor (PPAR) δ interacting protein using the yeast two-hybrid system. NCoR interacted strongly with the ligand-binding domain of PPARδ, whereas interactions with the ligand-binding domains of PPARγ and PPARα were significantly weaker. PPAR—NCoR interactions were antagonized by ligands in the two-hybrid system, but were ligand-insensitive in in vitro pull-down assays. Interaction between PPARδ and NCoR was unaffected by coexpression of retinoid X receptor (RXR) α. The PPARδ—RXRα heterodimer bound to an acyl-CoA oxidase (ACO)-type peroxisome-proliferator response element recruited a glutathione S-transferase—NCoR fusion protein in a ligand-independent manner. Contrasting with most other nuclear receptors, PPARδ was found to interact equally well with interaction domains I and II of NCoR. In transient transfection experiments, NCoR and the related silencing mediator for retinoid and thyroid hormone receptor (SMRT) were shown to exert a marked dose-dependent repression of ligand-induced PPARδ-mediated transactivation; in addition, transactivation induced by the cAMP-elevating agent forskolin was efficiently reduced to basal levels by NCoR as well as SMRT coexpression. Our results suggest that the transactivation potential of liganded PPARδ can be fine-tuned by interaction with NCoR and SMRT in a manner determined by the expression levels of corepressors and coactivators.

scholarly journals Peroxisome proliferator-activated receptor gamma (PPARγ) upregulation and dietary fat levels in laying hens

2021 ◽  
pp. 101049
Author(s):  
Shahram Barzegar ◽  
Robert A. Swick ◽  
Sarbast K. Kheravii ◽  
Mingan Choct ◽  
Shu-Biao Wu
Keyword(s):  
Dietary Fat ◽  
Laying Hens ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor

scholarly journals Inhibition of Cellular Proliferation through IκB Kinase-Independent and Peroxisome Proliferator-Activated Receptor γ-Dependent Repression of Cyclin D1

2001 ◽  
Vol 21 (9) ◽  
pp. 3057-3070 ◽  
Author(s):  
Chenguang Wang ◽  
Maofu Fu ◽  
Mark D'Amico ◽  
Chris Albanese ◽  
Jian-Nian Zhou ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
Nuclear Receptor ◽  
Cellular Proliferation ◽  
Biological Effects ◽  
S Phase ◽  
In Vivo Studies ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Iκb Kinase ◽  
Anti Inflammatory

ABSTRACT The nuclear receptor peroxisome proliferator-activated receptor γ (PPARγ) is a ligand-regulated nuclear receptor superfamily member. Liganded PPARγ exerts diverse biological effects, promoting adipocyte differentiation, inhibiting tumor cellular proliferation, and regulating monocyte/macrophage and anti-inflammatory activities in vitro. In vivo studies with PPARγ ligands showed enhancement of tumor growth, raising the possibility that reduced immune function and tumor surveillance may outweigh the direct inhibitory effects of PPARγ ligands on cellular proliferation. Recent findings that PPARγ ligands convey PPARγ-independent activities through IκB kinase (IKK) raises important questions about the specific mechanisms through which PPARγ ligands inhibit cellular proliferation. We investigated the mechanisms regulating the antiproliferative effect of PPARγ. Herein PPARγ, liganded by either natural (15d-PGJ2 and PGD2) or synthetic ligands (BRL49653 and troglitazone), selectively inhibited expression of the cyclin D1 gene. The inhibition of S-phase entry and activity of the cyclin D1-dependent serine-threonine kinase (Cdk) by 15d-PGJ2 was not observed in PPARγ-deficient cells. Cyclin D1 overexpression reversed the S-phase inhibition by 15d-PGJ2. Cyclin D1 repression was independent of IKK, as prostaglandins (PGs) which bound PPARγ but lacked the IKK interactive cyclopentone ring carbonyl group repressed cyclin D1. Cyclin D1 repression by PPARγ involved competition for limiting abundance of p300, directed through a c-Fos binding site of the cyclin D1 promoter. 15d-PGJ2 enhanced recruitment of p300 to PPARγ but reduced binding to c-Fos. The identification of distinct pathways through which eicosanoids regulate anti-inflammatory and antiproliferative effects may improve the utility of COX2 inhibitors.

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