21 results match your criteria Nuclear Receptor [Journal]

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The integration of lipid-sensing and anti-inflammatory effects: how the PPARs play a role in metabolic balance.

Nucl Recept 2007 May 25;5(1). Epub 2007 May 25.

Molecular Imaging Group, Medical Research Council Clinical Sciences Centre, Imperial College, Hammersmith Campus, London W12 0HS, UK.

The peroxisomal proliferating-activated receptors (PPARs) are lipid-sensing transcription factors that have a role in embryonic development, but are primarily known for modulating energy metabolism, lipid storage, and transport, as well as inflammation and wound healing. Currently, there is no consensus as to the overall combined function of PPARs and why they evolved. We hypothesize that the PPARs had to evolve to integrate lipid storage and burning with the ability to reduce oxidative stress, as energy storage is essential for survival and resistance to injury/infection, but the latter increases oxidative stress and may reduce median survival (functional longevity). Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-5-1DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899481PMC
May 2007
4 Reads

Association of common variation in the PPARA gene with incident myocardial infarction in individuals with type 2 diabetes: a Go-DARTS study.

Nucl Recept 2005 Nov 25;3. Epub 2005 Nov 25.

The Institute of Cardiovascular Research, Ninewells Hospital and Medical School, Dundee, DD1 9SY, Scotland, UK.

Background: Common variants of the PPARA gene have been found to associate with ischaemic heart disease in non diabetic men. The L162V variant was found to be protective while the C2528G variant increased risk. L162V has also been associated with altered lipid measures. Read More

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http://dx.doi.org/10.1186/1478-1336-3-4DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1318486PMC
November 2005
38 Reads

Gene expression profiling of potential peroxisome proliferator-activated receptor (PPAR) target genes in human hepatoblastoma cell lines inducibly expressing different PPAR isoforms.

Nucl Recept 2005 Oct 3;3. Epub 2005 Oct 3.

Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.

Background: Peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors and commonly play an important role in the regulation of lipid homeostasis. To identify human PPARs-responsive genes, we established tetracycline-regulated human hepatoblastoma cell lines that can be induced to express each human PPAR and investigated the gene expression profiles of these cells.

Results: The expression of each introduced PPAR gene was investigated using the various concentrations of doxycycline in the culture media. Read More

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http://dx.doi.org/10.1186/1478-1336-3-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1262764PMC
October 2005
10 Reads

Evolutionary selection across the nuclear hormone receptor superfamily with a focus on the NR1I subfamily (vitamin D, pregnane X, and constitutive androstane receptors).

Nucl Recept 2005 Sep 30;3. Epub 2005 Sep 30.

Department of Pathology, Children's Hospital of Pittsburgh, University of Pittsburgh, Pittsburgh, PA 15213, USA.

Background: The nuclear hormone receptor (NR) superfamily complement in humans is composed of 48 genes with diverse roles in metabolic homeostasis, development, and detoxification. In general, NRs are strongly conserved between vertebrate species, and few examples of molecular adaptation (positive selection) within this superfamily have been demonstrated. Previous studies utilizing two-species comparisons reveal strong purifying (negative) selection of most NR genes, with two possible exceptions being the ligand-binding domains (LBDs) of the pregnane X receptor (PXR, NR1I2) and the constitutive androstane receptor (CAR, NR1I3), two proteins involved in the regulation of toxic compound metabolism and elimination. Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-3-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1262763PMC
September 2005
6 Reads

Thyroid hormone receptor binding to DNA and T3-dependent transcriptional activation are inhibited by uremic toxins.

Nucl Recept 2005 Apr 4;3(1). Epub 2005 Apr 4.

Molecular Pharmacology Laboratory, Department of Pharmaceutical Sciences, School of Health Sciences, University of Brasilia, Brazil.

BACKGROUND: There is a substantial clinical overlap between chronic renal failure (CRF) and hypothyroidism, suggesting the presence of hypothyroidism in uremic patients. Although CRF patients have low T3 and T4 levels with normal thyroid-stimulating hormone (TSH), they show a higher prevalence of goiter and evidence for blunted tissue responsiveness to T3 action. However, there are no studies examining whether thyroid hormone receptors (TRs) play a role in thyroid hormone dysfunction in CRF patients. Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-3-1DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1087878PMC
April 2005
7 Reads

The evolution of drug-activated nuclear receptors: one ancestral gene diverged into two xenosensor genes in mammals.

Nucl Recept 2004 Oct 12;2(1). Epub 2004 Oct 12.

BACKGROUND: Drugs and other xenobiotics alter gene expression of cytochromes P450 (CYP) by activating the pregnane X receptor (PXR) and constitutive androstane receptor (CAR) in mammals. In non-mammalian species, only one xenosensor gene has been found. Using chicken as a model organism, the aim of our study was to elucidate whether non-mammalian species only have one or two xenosensors like mammals. Read More

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http://dx.doi.org/10.1186/1478-1336-2-7DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC524364PMC
October 2004
12 Reads
14 Citations

Diurnal difference in CAR mRNA expression.

Nucl Recept 2004 Aug 28;2(1). Epub 2004 Aug 28.

Faculty of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.

BACKGROUND: The constitutive androstane receptor (CAR, NR1I3) plays a key role in the transcriptional activation of genes that encode xenobiotic/steroid and drug metabolizing enzymes. RESULTS: The expression of CAR mRNA throughout the circadian rhythm is reported for the first time in phase with the clock gene Bmal1 and in antiphase with the clock-controlled gene Rev-erbalpha mRNAs, with a peak at Zeitgeber time (ZT) 20 and a trough at ZT8, and a peak/trough ratio of 2.0. Read More

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http://dx.doi.org/10.1186/1478-1336-2-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC517509PMC
August 2004
6 Reads

Binding of estrogen receptor with estrogen conjugated to bovine serum albumin (BSA).

Nucl Recept 2004 Aug 19;2(1). Epub 2004 Aug 19.

Geriatrics, University of Arkansas for Medical Sciences, 4301 West Markham Street, Little Rock, AR 72205, USA.

BACKGROUND: The classic model of estrogen action requires that the estrogen receptor (ER) activates gene expression by binding directly or indirectly to DNA. Recent studies, however, strongly suggest that ER can act through nongenomic signal transduction pathways and may be mediated by a membrane bound form of the ER. Estradiol covalently linked to membrane impermeable BSA (E2-BSA) has been widely used as an agent to study these novel membrane-associated ER events. Read More

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http://dx.doi.org/10.1186/1478-1336-2-5DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC516042PMC
August 2004
6 Reads

Endotoxin leads to rapid subcellular re-localization of hepatic RXRalpha: A novel mechanism for reduced hepatic gene expression in inflammation.

Nucl Recept 2004 Aug 16;2(1). Epub 2004 Aug 16.

Texas Children's Liver Center, Department of Pediatrics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

BACKGROUND: Lipopolysaccharide (LPS) treatment of animals down-regulates the expression of hepatic genes involved in a broad variety of physiological processes, collectively known as the negative hepatic acute phase response (APR). Retinoid X receptor alpha (RXRalpha), the most highly expressed RXR isoform in liver, plays a central role in regulating bile acid, cholesterol, fatty acid, steroid and xenobiotic metabolism and homeostasis. Many of the genes regulated by RXRalpha are repressed during the negative hepatic APR, although the underlying mechanism is not known. Read More

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http://dx.doi.org/10.1186/1478-1336-2-4DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC514570PMC
August 2004
6 Reads

Estrogen receptor-dependent activation of AP-1 via non-genomic signalling.

Nucl Recept 2004 Jun 14;2(1). Epub 2004 Jun 14.

Dept, of Cell and Molecular Biology, Karolinska Institutet, SE-171 77 Stockholm, Sweden.

BACKGROUND: Ligand-bound estrogen receptor alpha (ERalpha) and estrogen receptor beta (ERbeta) modulate AP-1-dependent transcription via protein-protein interactions on DNA, in a manner that depends on the type of cells and the subtype of ER. We present here evidence for an additional mechanism by which ERs modulate the transcriptional activity of AP-1. RESULTS: We show that ERs located in the cytoplasm efficiently activate transcription at AP-1 sites in response to 17beta-estradiol, while ERs present in the nucleus repress transcription under the same conditions. Read More

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http://dx.doi.org/10.1186/1478-1336-2-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC434532PMC
June 2004
2 Reads

A conserved lysine in the estrogen receptor DNA binding domain regulates ligand activation profiles at AP-1 sites, possibly by controlling interactions with a modulating repressor.

Nucl Recept 2004 05 7;2(1). Epub 2004 May 7.

Departments of Pathology, & Biochemistry and Molecular Genetics University of Virginia, School of Medicine, MR5 Rm, 3123, 415 Lane Rd, Charlottesville, VA 22908-0904, USA.

BACKGROUND: Estrogen receptors alpha and beta (ERalpha and ERbeta) differentially activate genes with AP-1 elements. ERalpha activates AP-1 targets via activation functions with estrogens (the AF-dependent pathway), whereas ERbeta, and a short version of ERalpha (ERalpha DBD-LBD) activate only with anti-estrogens (AF-independent pathway). The DNA binding domain (DBD) plays an important role in both pathways, even though neither pathway requires ERE recognition. Read More

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http://dx.doi.org/10.1186/1478-1336-2-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC446215PMC
May 2004
11 Reads

Alternative splicing affects the function and tissue-specific expression of the human constitutive androstane receptor.

Nucl Recept 2004 Mar 25;2(1). Epub 2004 Mar 25.

Dr, Margarete Fischer-Bosch Institute of Clinical Pharmacology, Auerbachstrasse 112, D-70376 Stuttgart, Germany.

BACKGROUND: The constitutive androstane receptor (CAR) plays a key role in the control of drug metabolism and transport by mediating the phenobarbital-type induction of many phase I and II drug metabolizing enzymes and drug transporters. RESULTS: We identified transcripts generated by four different alternative splicing events in the human CAR gene. Two of the corresponding ligand binding domain isoforms demonstrated novel functional properties: First, CAR(SV3), which is encoded by a transcript containing an lengthened exon 7, differentially transactivated target gene promoters. Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-2-1DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC406421PMC
March 2004
4 Reads

The peroxisome proliferator activated receptor δ is required for the differentiation of THP-1 monocytic cells by phorbol ester.

Nucl Recept 2003 11;1. Epub 2003 Dec 11.

Biomedical Research Centre, University of Dundee, Ninewells Hospital and Medical School, Dundee. DD1 9SY, UK.

Background: PPARδ (NR1C2) promotes lipid accumulation in human macrophages and has been implicated in the response of macrophages to vLDL. We have investigated the role of PPARδ in PMA-stimulated macrophage differentiation. The THP-1 monocytic cell line which displays macrophage like differentiation in response to phorbol esters was used as a model system. Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-1-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC317379PMC
December 2003
8 Reads

SF-1 a key player in the development and differentiation of steroidogenic tissues.

Nucl Recept 2003 Sep 18;1(1). Epub 2003 Sep 18.

UMR CNRS 6547, Physiologie Comparée et Endocrinologie Moléculaire, Université Blaise Pascal, Clermont II, Complexe Universitaire des Cézeaux, 24 avenue des Landais, 63177 Aubiere Cedex, France.

Since its discovery in the early 1990s, the orphan nuclear receptor SF-1 has been attributed a central role in the development and differentiation of steroidogenic tissues. SF-1 controls the expression of all the steroidogenic enzymes and cholesterol transporters required for steroidogenesis as well as the expression of steroidogenesis-stimulating hormones and their cognate receptors. SF-1 is also an essential regulator of genes involved in the sex determination cascade. Read More

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http://dx.doi.org/10.1186/1478-1336-1-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC240021PMC
September 2003
2 Reads

A neuronal-specific differentiation protein that directly modulates retinoid receptor transcriptional activation.

Nucl Recept 2003 Sep 10;1(1). Epub 2003 Sep 10.

Department of Molecular and Cellular Biochemistry, University of Kentucky, 800 Rose Street, Lexington, KY 40536, USA.

BACKGROUND: The specificity of a nuclear receptor's ability to modulate gene expression resides in its ability to bind a specific lipophilic ligand, associate with specific dimerization partners and bind specific DNA sequences in the promoter regions of genes. This sequence of events appears to be the basis for targeting an additional regulatory complex composed of a variety of protein and RNA components that deliver signals for facilitation or inhibition of the RNA polymerase complex. Characterization of the tissue and cell-specific components of these coregulatory complexes appear to be integral to our understanding of nuclear receptor regulation of transcription. Read More

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http://nuclear-receptor.biomedcentral.com/articles/10.1186/1
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http://dx.doi.org/10.1186/1478-1336-1-7DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC222963PMC
September 2003
6 Reads

PLZF is a negative regulator of retinoic acid receptor transcriptional activity.

Nucl Recept 2003 Sep 6;1(1). Epub 2003 Sep 6.

INSERM U 459 and Ligue Nationale Contre le Cancer, Faculté de Médecine Henri Warembourg, 1 place de Verdun, 59045 Lille cedex, France.

BACKGROUND: Retinoic acid receptors (RARs) are ligand-regulated transcription factors controlling cellular proliferation and differentiation. Receptor-interacting proteins such as corepressors and coactivators play a crucial role in specifying the overall transcriptional activity of the receptor in response to ligand treatment. Little is known however on how receptor activity is controlled by intermediary factors which interact with RARs in a ligand-independent manner. Read More

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http://dx.doi.org/10.1186/1478-1336-1-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC212040PMC
September 2003
11 Reads

Expression and localization of P1 promoter-driven hepatocyte nuclear factor-4α (HNF4α) isoforms in human and rats.

Nucl Recept 2003 8;1. Epub 2003 Aug 8.

Department of Cellular Function, Division of Cellular and Molecular Pathology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.

Background: Hepatocyte nuclear factor-4α (HNF4α; NR2A1) is an orphan member of the nuclear receptor superfamily involved in various processes that could influence endoderm development, glucose and lipid metabolism. A loss-of-function mutation in human HNF4α causes one form of diabetes mellitus called maturity-onset diabetes of the young type 1 (MODY1) which is characterized in part by a diminished insulin secretory response to glucose. The expression of HNF4α in a variety of tissues has been examined predominantly at the mRNA level, and there is little information regarding the cellular localization of the endogenous HNF4α protein, due, in part, to the limited availability of human HNF4α-specific antibodies. Read More

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http://dx.doi.org/10.1186/1478-1336-1-5DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC194242PMC
August 2003
15 Reads

Establishment of a monoclonal antibody for human LXRalpha: Detection of LXRalpha protein expression in human macrophages.

Nucl Recept 2003 May 9;1(1). Epub 2003 May 9.

Department of Life Sciences, The University of Tokyo Research Center for Advanced Science and Technology (RCAST), Tokyo, Japan.

Liver X activated receptor alpha (LXRalpha) forms a functional dimeric nuclear receptor with RXR that regulates the metabolism of several important lipids, including cholesterol and bile acids. As compared with RXR, the LXRalpha protein level in the cell is low and the LXRalpha protein itself is very hard to detect. We have previously reported that the mRNA for LXRalpha is highly expressed in human cultured macrophages. Read More

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http://dx.doi.org/10.1186/1478-1336-1-1DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC166117PMC
May 2003
9 Reads

Complex effects of rexinoids on ligand dependent activation or inhibition of the xenobiotic receptor, CAR.

Nucl Recept 2003 Jun 6;1(1). Epub 2003 Jun 6.

Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

BACKGROUND: CAR/RXR heterodimers bind a variety of hormone response elements and activate transcription in the absence of added ligands. This constitutive activity of murine CAR can be inhibited by the inverse agonist ligand androstanol or increased by the agonist TCPOBOP. RXR agonists activate some RXR heterodimer complexes, which are termed permissive, while other non-permissive complexes are not responsive to such ligands. Read More

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http://dx.doi.org/10.1186/1478-1336-1-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179875PMC
June 2003
2 Reads

Stat3 enhances transactivation of steroid hormone receptors.

Nucl Recept 2003 Jun 13;1(1). Epub 2003 Jun 13.

Department of Medicine and Pharmacology & Therapeutics, Roswell Park Cancer Institute, Buffalo, NY 14263, USA.

BACKGROUND: Steroid hormone receptors (SHRs) are members of the superfamily of ligand-activated transcription factors that regulate many biological processes. Co-regulators act as bridging molecules between the SHR and general transcription factors to enhance transactivation of target genes. Previous studies demonstrated that Stat3 is constitutively activated in prostate cancer and can enhance prostate specific antigen (PSA) expression and promote androgen independent growth. Read More

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http://dx.doi.org/10.1186/1478-1336-1-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179876PMC
June 2003
6 Reads

ERbeta Binds N-CoR in the Presence of Estrogens via an LXXLL-like Motif in the N-CoR C-terminus.

Nucl Recept 2003 Jun 28;1(1). Epub 2003 Jun 28.

Metabolic Research Unit and Diabetes Center, University of California, San Francisco, CA 94143, USA.

Nuclear receptors (NRs) usually bind the corepressors N-CoR and SMRT in the absence of ligand or in the presence of antagonists. Agonist binding leads to corepressor release and recruitment of coactivators. Here, we report that estrogen receptor beta (ERbeta) binds N-CoR and SMRT in the presence of agonists, but not antagonists, in vitro and in vivo. Read More

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http://dx.doi.org/10.1186/1478-1336-1-4DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179877PMC
June 2003
8 Reads
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