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Vdr rxr ppar

Imourana Alassane-Kpembi, Juliana Rubira Gerez, Anne-Marie Cossalter, Manon Neves, Joëlle Laffitte, Claire Naylies, Yannick Lippi, Martine Kolf-Clauw, Ana Paula L Bracarense, Philippe Pinton, Isabelle P Oswald
The few data available on fusarenon-X (FX) do not support the derivation of health-based guidance values, although preliminary results suggest higher toxicity than other regulated trichothecenes. Using histo-morphological analysis and whole transcriptome profiling, this study was designed to obtain a global view of the intestinal alterations induced by FX. Deoxynivalenol (DON) served as a benchmark. FX induced more severe histological alterations than DON. Inflammation was the hallmark of the molecular toxicity of both mycotoxins...
August 8, 2017: Scientific Reports
Nirupama Chandel, Kamesh Ayasolla, Hongxiu Wen, Xiqian Lan, Shabirul Haque, Moin A Saleem, Ashwani Malhotra, Pravin C Singhal
Vitamin D receptor (VDR) deficient status has been shown to be associated with the activation of renin angiotensin system (RAS). We hypothesized that lack of VDR would enhance p53 expression in podocytes through down regulation of SIRT1; the former would enhance the transcription of angiotensinogen (Agt) and angiotensinogen II type 1 receptor (AT1R) leading to the activation of RAS. Renal tissues of VDR mutant (M) mice displayed increased expression of p53, Agt, renin, and AT1R. In vitro studies, VDR knockout podocytes not only displayed up regulation p53 but also displayed enhanced expression of Agt, renin and AT1R...
February 2017: Experimental and Molecular Pathology
Marta Dominguez, Susana Alvarez, Angel R de Lera
Retinoid X receptors (RXRs) are promiscuous partners of heterodimeric associations with other members of the Nuclear Receptor (NR) superfamily. Through these liaisons RXR ligands ("rexinoids") either transcriptionally activate on their own the "permissive" subclass of heterodimers (PPAR/RXR, LXR/RXR, FXR/RXR) or synergize with partner ligands in the "non-permissive" subclass of heterodimers (RAR/RXR, VDR/RXR and TR/RXR). The nature and extent of the interaction of the ligand-receptor complexes with co-regulators, which is cell and context-dependent, results ultimately in transcriptional modulation of cognate gene networks...
2017: Current Topics in Medicinal Chemistry
Carl E Wagner, Peter W Jurutka, Pamela A Marshall, Michael C Heck
Since the isolation and identification of the retinoid X receptor (RXR) as a member of the nuclear receptor (NR) superfamily in 1990, its analysis has ushered in a new understanding of physiological regulation by nuclear receptors, and novel methods to identify other unknown and orphan receptors. Expression of one or more of the three isoforms of RXR-α, β, and γ-can be found in every human cell type. Biologically, RXR plays a critical role through its ability to partner with other nuclear receptors. RXR is able to regulate nutrient metabolism by forming "permissive" heterodimers with peroxisome proliferator-activated receptor (PPAR), liver-X-receptor (LXR), farnesoid X receptor (FXR), pregnane X receptor (PXR) and constitutive androstane receptor (CAR), which function when ligands are bound to one or both of the heterodimer partners...
2017: Current Topics in Medicinal Chemistry
Kent Wehmeier, Luisa M Onstead-Haas, Norman C W Wong, Arshag D Mooradian, Michael J Haas
The vitamin D metabolite 24,25-dihydroxyvitamin D3 (24, 25[OH]2D3) was shown to induce nongenomic signaling pathways in resting zone chondrocytes and other cells involved in bone remodeling. Recently, our laboratory demonstrated that 24,25-[OH]2D3 but not 25-hydroxyvitamin D3, suppresses apolipoprotein A-I (apo A-I) gene expression and high-density lipoprotein (HDL) secretion in hepatocytes. Since 24,25-[OH]2D3 has low affinity for the vitamin D receptor (VDR) and little is known with regard to how 24,25-[OH]2D3 modulates nongenomic signaling in hepatocytes, we investigated the capacity of 24,25-[OH]2D3 to activate various signaling pathways relevant to apo A-I synthesis in HepG2 cells...
August 2016: Journal of Molecular Endocrinology
Kenji Moriyama, Hiroyuki Yamamoto, Kumi Futawaka, Asami Atake, Masato Kasahara, Tetsuya Tagami
Thyroid hormone exerts a pleiotropic effect on development, differentiation, and metabolism through thyroid hormone receptor (TR). A novel thyroid hormone receptor β isoform (TRβ4) was cloned using PCR from a human pituitary cDNA library as a template. We report here the characterization of TRβ4 from a molecular basis. Temporal expression of TRβ4 during the fetal period is abundant in the brain and kidney, comparable with the adult pattern. Western blot analysis revealed that TRs are ubiquitination labile proteins, while TRβ1 is potentially stable...
2016: Endocrine Research
Kirtimaan Syal, Anand Srinivasan, Dibyajyoti Banerjee
Diabetes and tuberculosis are world's most deadly epidemics. People suffering from diabetes are susceptible to tuberculosis. Molecular link between the two is largely unknown. It is known that Vitamin A receptor (RXR) heterodimerizes with Vitamin D receptor (VDR) and Peroxisome proliferator-activator receptor-γ (PPARγ) to regulate Tryptophan-aspartate containing coat protein (TACO) expression and fatty acid metabolism respectively, so it would be interesting to check the expression of these genes in diabetes mellitus (DM) patients which might explain the susceptibility of diabetics to tuberculosis...
July 2015: Indian Journal of Clinical Biochemistry: IJCB
Eva Morales, Manuel Sanchez-Solis, Luis Garcia-Marcos
Asthma and allergy are complex diseases influenced by poorly understood environmental and genetic factors. The innate and adaptive immune systems play an important role in the pathogenesis of these diseases. Many genes involved in inflammation and immunoregulation pathways have been related to asthma and allergy susceptibility. Among the diverse extra-skeletal actions of vitamin D, growing evidence indicates that vitamin D is an important modulator of the immune system response and may influence the development of asthma and allergy susceptibility through different mechanisms...
2015: Mini Reviews in Medicinal Chemistry
Nina Ditsch, Doris Mayr, Miriam Lenhard, Carolin Strauss, Andrea Vodermaier, Julia Gallwas, Doris Stoeckl, Monika Graeser, Tobias Weissenbacher, Klaus Friese, Udo Jeschke
Non-steroidal nuclear receptors play a major role in breast cancer development. A correlation among, and possible prognostic function of, the members of the nuclear receptor superfamily has been discussed controversially over the years. Hence, we conducted a quantification of the different expression levels of the thyroid receptor (TR), retinoid X receptor (RXR), peroxisome proliferator-activated receptor (PPAR) and vitamin D receptor (VDR) in malignant breast tumour tissue samples. Patients diagnosed and treated for breast cancer between 1990 and 2000 were included...
October 2012: Oncology Letters
A Pestka, J S Fitzgerald, B Toth, U R Markert, U Jeschke
BACKGROUND: Nuclear Hormone Receptors (NHR) are, as the name implies, receptors located in the cell nucleus that have transcription modulating characteristics. Activated non-steroidal lipophilic ligands bind these receptors resulting in dimerisation of the ligands, DNA-binding and transcriptional regulation of target proteins that influence especially cell differentiation, metabolic homeostasis and embryogenesis. METHODS: This review is based on publications derived from PubMed based pursuit of scientific literature in conjunction with the authors' experience...
August 2013: Current Molecular Medicine
Hitoshi Kotani, Hiroki Tanabe, Hajime Mizukami, Sakae Amagaya, Makoto Inoue
We investigated the properties of honokiol, a natural rexinoid, as a regulator of retinoid X receptor (RXR) heterodimers with various partner nuclear receptors (NRs), in comparison with those of the synthetic rexinoid bexarotene. Honokiol alone was hardly capable of activating peroxisome proliferator-activated receptor (PPAR) γ/RXR, RXR/liver X receptor (LXR), and RXR/vitamin D receptor (VDR) heterodimers, whereas it effectively potentiated their activation by agonists for the partner NRs of the RXR heterodimers...
2012: Biological & Pharmaceutical Bulletin
Efrén Pérez, William Bourguet, Hinrich Gronemeyer, Angel R de Lera
As the promiscuous partner of heterodimeric associations, retinoid X receptors (RXRs) play a key role within the Nuclear Receptor (NR) superfamily. Some of the heterodimers (PPAR/RXR, LXR/RXR, FXR/RXR) are "permissive" as they become transcriptionally active in the sole presence of either an RXR-selective ligand ("rexinoid") or a NR partner ligand. In contrast, "non-permissive" heterodimers (including RAR/RXR, VDR/RXR and TR/RXR) are unresponsive to rexinoids alone but these agonists superactivate transcription by synergizing with partner agonists...
January 2012: Biochimica et Biophysica Acta
Natacha Rochel, Fabrice Ciesielski, Julien Godet, Edelmiro Moman, Manfred Roessle, Carole Peluso-Iltis, Martine Moulin, Michael Haertlein, Phil Callow, Yves Mély, Dmitri I Svergun, Dino Moras
Nuclear hormone receptors (NHRs) control numerous physiological processes through the regulation of gene expression. The present study provides a structural basis for understanding the role of DNA in the spatial organization of NHR heterodimers in complexes with coactivators such as Med1 and SRC-1. We have used SAXS, SANS and FRET to determine the solution structures of three heterodimer NHR complexes (RXR-RAR, PPAR-RXR and RXR-VDR) coupled with the NHR interacting domains of coactivators bound to their cognate direct repeat elements...
May 2011: Nature Structural & Molecular Biology
Lajos Széles, Szilárd Póliska, Gergely Nagy, Istvan Szatmari, Attila Szanto, Attila Pap, Malin Lindstedt, Saskia J A M Santegoets, Ralph Rühl, Balázs Dezsö, László Nagy
Retinoid X receptors (RXRs) are heterodimerization partners for many nuclear receptors and also act as homodimers. Heterodimers formed by RXR and a nonpermissive partner, e.g. retinoic acid receptor (RAR) and vitamin D receptor (VDR), can be activated only by the agonist of the partner receptor. In contrast, heterodimers that contain permissive partners, e.g. liver X receptor (LXR) and peroxisome proliferator-activated receptor (PPAR), can be activated by agonists for either the partner receptor or RXR, raising the possibility of pleiotropic RXR signaling...
November 2010: Molecular Endocrinology
Samir Satih, Hélène Savinel, Nadège Rabiau, Luc Fontana, Yves-Jean Bignon, Dominique J Bernard-Gallon
BACKGROUND: Most of breast cancers are considered sporadic and modulation of the two major genes BRCA1 and BRCA2 expressions caused by tissue-specific somatic mutations lead to this pathology. The nutritional intake of phytoestrogens seems to reduce the risk of breast cancer and investigation of their potential as anticancer agents has increased. However, the possible mechanisms and signalling pathways of phytoestrogen action in breast cancer prevention remains unknown. RESULTS: Using Taqman Low Density Array technology, we investigated the BRCA2 loss of function role in sporadic breast cancers and the links existing with soy isoflavones on a panel of nuclear receptor expression...
2009: Journal of Molecular Signaling
Magdalena Kopij, Andrzej Rapak
The nuclear receptors form a group of structurally homologous proteins which act as ligand-dependent transcription factors and regulate a variety of intracellular processes. The nuclear receptors act as monomomers, homodimers, or heterodimers together with retinoid X receptor (RXR). They bind in the nucleus to a specific nucleotide sequence in the promoter region called the response element (RE). Certain nuclear receptors (e.g. Nur77, GR, RXR, RAR, VDR, PPAR) can influence apoptosis through the induction of pro- and/or anti-apoptotic proteins or affect other transcription factors...
October 17, 2008: Postȩpy Higieny i Medycyny Doświadczalnej
Richard J Wood
The focus of the current review is to highlight some new insights into the molecular mechanism by which vitamin D, a potentially nutritionally modulated factor, influences adipogenesis. Recent studies, predominantly using the mouse 3T3-L1 pre-adipocyte cell culture model, have shown that the role of vitamin D in inhibiting adipogenesis is mediated at the molecular level through a vitamin D receptor (VDR)-dependent inhibition of CCAAT enhancer binding protein-alpha (C/EBP alpha) and peroxisome proliferator-activated receptor-gamma (PPAR gamma) expression and a decrease in PPAR gamma transactivating activity in the pre-adipocyte...
January 2008: Nutrition Reviews
Deborah K Stafslien, Kevin L Vedvik, Therese De Rosier, Mary Szatkowski Ozers
Because RXR plays a significant role in nuclear receptor signaling as a common heterodimeric partner for TR, PPAR, RAR, VDR, LXR and others, the ability of RXRbeta ligand binding domain (LBD) to interact with coregulator peptides bearing LXXLL or other interaction motifs was investigated using time-resolved fluorescence resonance energy transfer (TR-FRET). The random phage display peptide D22 and peptides derived from PGC1alpha, SRC1-4, SRC2-3, PRIP/RAP250 and RIP140 yielded the highest TR-FRET signal with RXRbeta LBD in the presence of saturating 9-cis retinoic acid (9-cisRA)...
January 29, 2007: Molecular and Cellular Endocrinology
Yuichi Hashimoto, Hiroyuki Miyachi
Here we review our studies on the molecular design of nuclear receptor antagonists, including retinoic acid receptor (RAR) antagonists, retinoid X receptor (RXR) antagonists, androgen receptor (AR) antagonists, and vitamin D receptor (VDR) antagonists, based on inhibition of folding of helix 12, which contains a co-activator binding site. Recent progress in structural development studies of peroxisome proliferator-activated receptor (PPAR) ligands is also reviewed.
September 1, 2005: Bioorganic & Medicinal Chemistry
Thomas W Dunlop, Sami Väisänen, Christian Frank, Ferdinand Molnár, Lasse Sinkkonen, Carsten Carlberg
Peroxisome proliferator-activated receptor (PPAR) delta is the most widely expressed member of the PPAR family of nuclear receptor fatty acid sensors. Real-time PCR analysis of breast and prostate cancer cell lines demonstrated that PPARdelta expression was increased 1.5 to 3.2-fold after three hours stimulation with the natural vitamin D receptor (VDR) agonist, 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3). In silico analysis of the 20 kb of the human PPARdelta promoter revealed a DR3-type 1alpha,25(OH)2D3 response element approximately 350 bp upstream of the transcription start site, which was able to bind VDR-retinoid X receptor (RXR) heterodimers and mediate a 1alpha,25(OH)2D3-dependent upregulation of reporter gene activity...
June 3, 2005: Journal of Molecular Biology
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