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  1 / 131 MEDLINE  
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PMID:28636886
Autor:Sabir MS; Khan Z; Hu C; Galligan MA; Dussik CM; Mallick S; Stone AD; Batie SF; Jacobs ET; Whitfield GK; Haussler MR; Heck MC; Jurutka PW
Dirección:Arizona State University, School of Mathematical and Natural Sciences, 4701 W. Thunderbird Road Glendale, AZ 85306, USA. Electronic address: msabir@asu.edu.
Título:SIRT1 enzymatically potentiates 1,25-dihydroxyvitamin D signaling via vitamin D receptor deacetylation.
Fuente:J Steroid Biochem Mol Biol; 172:117-129, 2017 Sep.
ISSN:1879-1220
País de publicación:England
Idioma:eng
Resumen:The hormonal metabolite of vitamin D, 1,25-dihydroxyvitamin D (1,25D), binds to the vitamin D receptor (VDR) and promotes heterodimerization of VDR with a retinoid-X-receptor (RXR) to genomically regulate diverse cellular processes. Herein, it is revealed for the first time that VDR is post-translationally acetylated, and that VDR immunoprecipitated from human embryonic kidney (HEK293) cells displays a dramatic decrease in acetylated receptor in the presence of 1,25D-ligand, sirtuin-1 (SIRT1) deacetylase, or the resveratrol activator of SIRT1. To elucidate the functional significance of VDR deacetylation, vitamin-d-responsive-element (VDRE)-based transcriptional assays were performed to determine if deacetylase overexpression affects VDR/VDRE-driven transcription. In HEK293 kidney and TE85 bone cells, co-transfection of low amounts (1-5ng) of a SIRT1-expression vector elicits a reproducible and statistically significant enhancement (1.3- to 2.6-fold) in transcription mediated by VDREs from the CYP3A4 and cyp24a1 genes, where the magnitude of response to 1,25D-ligand is 6- to 30-fold. Inhibition of SIRT1 via EX-527, or utilization of a SIRT1 loss-of-function mutant (H363Y), resulted in abrogation of SIRT1-mediated VDR potentiation. Studies with a novel, non-acetylatable VDR mutant (K413R) showed that the mutant VDR possesses enhanced responsiveness to 1,25D, in conjunction with reduced, but still significant, sensitivity to exogenous SIRT1, indicating that acetylation of lysine 413 is relevant, but that other acetylated residues in VDR contribute to modulation of its activity. We conclude that the acetylation of VDR comprises a negative feedback loop that attenuates 1,25D-VDR signaling. This regulatory loop is reversed by SIRT1-catalyzed deacetylation of VDR to amplify VDR signaling and 1,25D actions.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide); 0 (Carbazoles); 0 (Receptors, Calcitriol); 0 (Retinoid X Receptors); 0 (VDR protein, human); EC 1.13.12.- (Luciferases); EC 1.14.13.67 (CYP3A4 protein, human); EC 1.14.14.1 (Cytochrome P-450 CYP3A); EC 3.5.1.- (SIRT1 protein, human); EC 3.5.1.- (Sirtuin 1); FXC9231JVH (Calcitriol)


  2 / 131 MEDLINE  
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PMID:28243735
Autor:Zeljic K; Supic G; Magic Z
Dirección:Faculty of Biology, University of Belgrade, Studentski trg 3, Belgrade, 11000, Serbia. katarina.zeljic@bio.bg.ac.rs.
Título:New insights into vitamin D anticancer properties: focus on miRNA modulation.
Fuente:Mol Genet Genomics; 292(3):511-524, 2017 Jun.
ISSN:1617-4623
País de publicación:Germany
Idioma:eng
Resumen:Vitamin D anticancer properties are well known and have been demonstrated in many in vitro and in vivo studies. Mechanistic insights have given an explanation on how vitamin D exerts antineoplastic functions, which are mainly conducted via the canonical vitamin D receptor (VDR)-vitamin D response elements (VDRE) pathway. Numerous findings indicate that dietary components, including vitamin D, could exert chemopreventive effects through alterations of microRNA (miRNA) expression. As miRNAs have important roles in regulating diverse and vital cellular processes, it has been speculated that vitamin D's non-classical effects, including anticancer effects, could be mediated through alterations of miRNA expression level. The current review focuses on up-to-date experimental data on modulation of miRNA expression by vitamin D treatment in cancer, obtained in a cell culture system, animal models and human cohorts. Reported findings in the review show that vitamin D modulates expression of numerous and diverse miRNAs specific for cancer types. Even in its early phases, with many questions remaining to be answered, dissecting the molecular pathways of vitamin D miRNA modulation is an emerging area of science. The complete unraveling of vitamin D molecular mechanisms will emphasize the vitamin D dietary component as a potential chemopreventive agent in cancer and personalized nutrition.
Tipo de publicación:JOURNAL ARTICLE; REVIEW
Nombre de substancia:0 (Antineoplastic Agents); 0 (MicroRNAs); 0 (Receptors, Calcitriol); 1406-16-2 (Vitamin D)


  3 / 131 MEDLINE  
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PMID:27154413
Autor:Zhou X; Zheng W; Nagana Gowda GA; Raftery D; Donkin SS; Bequette B; Teegarden D
Dirección:Interdepartmental Nutrition Program, Purdue University, West Lafayette, IN 47906, United States. Electronic address: zhou249@purdue.edu.
Título:1,25-Dihydroxyvitamin D inhibits glutamine metabolism in Harvey-ras transformed MCF10A human breast epithelial cell.
Fuente:J Steroid Biochem Mol Biol; 163:147-56, 2016 10.
ISSN:1879-1220
País de publicación:England
Idioma:eng
Resumen:Breast cancer is the second most common cancer among women in the US. The active form of vitamin D, 1,25-dihydroxyvitamin D (1,25(OH)2D), is proposed to inhibit cellular processes and to prevent breast cancer. The current studies investigated the effect of 1,25(OH)2D on glutamine metabolism during cancer progression employing Harvey-ras oncogene transformed MCF10A human breast epithelial cells (MCF10A-ras). Treatment with 1,25(OH)2D significantly reduced intracellular glutamine and glutamate levels measured by nuclear magnetic resonance (NMR) by 23±2% each. Further, 1,25(OH)2D treatment reduced glutamine and glutamate flux, determined by [U-(13)C5] glutamine tracer kinetics, into the TCA cycle by 31±0.2% and 17±0.4%, respectively. The relative levels of mRNA and protein abundance of the major glutamine transporter, solute linked carrier family 1 member A5 (SLC1A5), was significantly decreased by 1,25(OH)2D treatment in both MCF10A-ras cells and MCF10A which overexpress ErbB2 (HER-2/neu). Consistent with these results, glutamine uptake was reduced by 1,25(OH)2D treatment and the impact was eliminated with the SLC1A5 inhibitor L-γ-Glutamyl-p-nitroanilide (GPNA). A consensus sequence to the vitamin D responsive element (VDRE) was identified in silico in the SLC1A5 gene promoter, and site-directed mutagenesis analyses with reporter gene studies demonstrate a functional negative VDRE in the promoter of the SLC1A5 gene. siRNA-SLC1A5 transfection in MCF10A-ras cells significantly reduced SLC1A5 mRNA expression as well as decreased viable cell number similar to 1,25(OH)2D treatment. SLC1A5 knockdown also induced an increase in apoptotic cells in MCF10A-ras cells. These results suggest 1,25(OH)2D alters glutamine metabolism in MCF10A-ras cells by inhibiting glutamine uptake and utilization, in part through down-regulation of SLC1A5 transcript abundance. Thus, 1,25(OH)2D down-regulation of the glutamine transporter, SLC1A5, may facilitate vitamin D prevention of breast cancer.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Nombre de substancia:0 (Amino Acid Transport System ASC); 0 (Minor Histocompatibility Antigens); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (Receptors, Calcitriol); 0 (SLC1A5 protein, human); 0 (VDR protein, human); 0RH81L854J (Glutamine); 1406-16-2 (Vitamin D); 3KX376GY7L (Glutamic Acid); 66772-14-3 (1,25-dihydroxyvitamin D); 7300-59-6 (gamma-glutamine-4-nitroanilide); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.6.5.2 (Oncogene Protein p21(ras))


  4 / 131 MEDLINE  
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PMID:27003919
Autor:Toderici M; de la Morena-Barrio ME; Padilla J; Miñano A; Antón AI; Iniesta JA; Herranz MT; Fernández N; Vicente V; Corral J
Dirección:Servicio de Hematología y Oncología Médica, Hospital Universitario Morales Meseguer, Centro Regional de Hemodonación, Universidad de Murcia, IMIB-Arrixaca, Murcia, Spain.
Título:Identification of Regulatory Mutations in SERPINC1 Affecting Vitamin D Response Elements Associated with Antithrombin Deficiency.
Fuente:PLoS One; 11(3):e0152159, 2016.
ISSN:1932-6203
País de publicación:United States
Idioma:eng
Resumen:Antithrombin is a crucial anticoagulant serpin whose even moderate deficiency significantly increases the risk of thrombosis. Most cases with antithrombin deficiency carried genetic defects affecting exons or flanking regions of SERPINC1.We aimed to identify regulatory mutations inSERPINC1 through sequencing the promoter, intron 1 and 2 of this gene in 23 patients with antithrombin deficiency but without known genetic defects. Three cases with moderate antithrombin deficiency (63-78%) carried potential regulatory mutations. One located 200 bp before the initiation ATG and two in intron 1. These mutations disrupted two out of five potential vitamin D receptor elements (VDRE) identified in SERPINC1 with different software. One genetic defect, c.42-1060_-1057dupTTGA, was a new low prevalent polymorphism (MAF: 0.01) with functional consequences on plasma antithrombin levels. The relevance of the vitamin D pathway on the regulation of SERPINC1 was confirmed in a cell model. Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium. This study shows further evidence of the transcriptional regulation of SERPINC1 by vitamin D and first describes the functional and pathological relevance of mutations affecting VDRE of this gene. Our study opens new perspectives in the search of new genetic defects involved in antithrombin deficiency and the risk of thrombosis as well as in the design of new antithrombotic treatments.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (SERPINC1 protein, human); 9000-94-6 (Antithrombin III)


  5 / 131 MEDLINE  
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PMID:26488808
Autor:Ji L; Gupta M; Feldman BJ
Dirección:Department of Pediatrics, Division of Pediatric Endocrinology, Stanford University School of Medicine, Stanford, California 94305-5457.
Título:Vitamin D Regulates Fatty Acid Composition in Subcutaneous Adipose Tissue Through Elovl3.
Fuente:Endocrinology; 157(1):91-7, 2016 Jan.
ISSN:1945-7170
País de publicación:United States
Idioma:eng
Resumen:Fatty acids (FAs) are a major energy source in the body. White adipose tissue (WAT) is a primary site where FAs are stored as triacylglycerols. Brown adipose tissue also stores and recruits FAs as a carbon source for uncoupled ß-oxidation during thermogenesis. The deletion of the vitamin D nuclear hormone receptor (VDR) gene in mice (VDRKO) results in a lean WAT phenotype with increased levels of expression of the brown adipose tissue marker Ucp1 in the WAT. However, the impact of vitamin D/VDR on FA composition in WAT has not been explored in detail. To address this question, we examined the FA composition of sc and visceral white adipose depots of VDRKO mice. We found that the levels of a subset of saturated and monounsaturated FAs of C18-C24 are specifically increased in the sc adipose depot in VDRKO mice. We revealed that a specific elongase enzyme (Elovl3), which has an important role in brown fat biology, is directly regulated by VDR and likely contributes to the altered FA composition in VDRKO mice. We also demonstrate that Elovl3 is regulated by vitamin D in vivo and tissue specifically in the sc WAT depot. We discovered that regulation of Elovl3 expression is mediated by ligand-dependent VDR occupancy of a negative-response element in the promoter proximal region of the Elovl3 gene. These data suggest that vitamin D/VDR tissue specifically modulates FA composition in sc WAT through direct regulation of Elovl3 expression.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Fatty Acids); 0 (Isoenzymes); 0 (Ligands); 0 (Receptors, Calcitriol); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (fatty acid elongases); FXC9231JVH (Calcitriol)


  6 / 131 MEDLINE  
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PMID:26369615
Autor:Dimitrov V; White JH
Dirección:Departments of Physiology and Medicine, McGill University, Montreal, Quebec, Canada.
Título:Species-specific regulation of innate immunity by vitamin D signaling.
Fuente:J Steroid Biochem Mol Biol; 164:246-253, 2016 Nov.
ISSN:1879-1220
País de publicación:England
Idioma:eng
Resumen:While many global mechanisms of innate immune responses to pathogen threat are conserved over a vast range of species, the details of those responses and their regulation appear to be highly species-specific. An array of studies over recent years has revealed that hormonal vitamin D is an important regulator of innate immunity. In humans, the hormone-bound VDR directly induces the transcription of genes encoding antimicrobial peptides (AMPs), pattern recognition receptors and key cytokines implicated in innate immune responses. We find that the vitamin D response elements (VDREs) in a number of these human genes are highly conserved in a range of primates, but not present in rodent genes. Consistent with this, VDR target genes encoding AMPs human beta-defensin 2 (HBD2) and cathelicidin (CAMP) and the pattern recognition receptor NOD2 are induced by 1,25(OH) D in human cells of epithelial or myeloid origin but not similarly regulated in mouse cells. In addition, while conditioned media from human epithelial cells treated with 1,25(OH) D produced antimicrobial activity against E. coli and the lung pathogen Pseudomonas aeruginosa, no such activity was detected in conditioned media from comparable 1,25(OH) D-treated mouse epithelial cells. Given that other work has provided evidence that 1,25(OH) D does control innate immune responses in mouse models of disease, we discuss the species-specific similarities and differences in 1,25(OH) D-regulated innate immunity.
Tipo de publicación:JOURNAL ARTICLE; REVIEW
Nombre de substancia:0 (Cathelicidins); 0 (Culture Media, Conditioned); 0 (DEFB4A protein, human); 0 (NOD2 protein, human); 0 (Nod2 Signaling Adaptor Protein); 0 (beta-Defensins); 0 (cathelicidin antimicrobial peptide); 1406-16-2 (Vitamin D); EC 1.14.15.16 (CYP24A1 protein, human); EC 1.14.15.16 (Vitamin D3 24-Hydroxylase)


  7 / 131 MEDLINE  
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PMID:26314252
Autor:González-Duarte RJ; Cázares-Ordoñez V; Díaz L; Ortíz V; Larrea F; Avila E
Dirección:Department of Reproductive Biology, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Vasco de Quiroga # 15, Col. Sección XVI, 14080, Mexico, D.F., Mexico.
Título:The expression of RNA helicase DDX5 is transcriptionally upregulated by calcitriol through a vitamin D response element in the proximal promoter in SiHa cervical cells.
Fuente:Mol Cell Biochem; 410(1-2):65-73, 2015 Dec.
ISSN:1573-4919
País de publicación:Netherlands
Idioma:eng
Resumen:The DEAD box RNA helicase DDX5 is a multifunctional protein involved in the regulatory events of gene expression. Herein, we presented evidence indicating that DDX5 is transcriptionally upregulated by calcitriol, the hormonal form of vitamin D3. In silico analysis revealed the presence of two putative vitamin D response elements (VDREs) in the DDX5 promoter region. Using luciferase reporter assays, we demonstrated that the DDX5 promoter containing these putative VDREs significantly increased the luciferase activity in vitamin D receptor (VDR)-positive SiHa cells upon calcitriol treatment. Electrophoretic mobility shift assays showed the ability of VDR and retinoid X receptor to interact only with the most proximal VDRE, while chromatin immunoprecipitation analysis confirmed the occupancy of this VDRE by the VDR. Finally, we demonstrated that calcitriol significantly increased both DDX5 mRNA and protein in SiHa cells. In summary, this study shows that DDX5 gene is transcriptionally upregulated by calcitriol through a VDRE located in its proximal promoter. Given the importance of DDX5 as a master regulator of differentiation programs, our study suggests that the pro-differentiating properties of calcitriol may be related with the induction of DDX5.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Receptors, Calcitriol); 0 (Retinoid X Receptors); 0 (VDR protein, human); EC 3.6.1.- (Ddx5 protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases); FXC9231JVH (Calcitriol)


  8 / 131 MEDLINE  
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PMID:26112182
Autor:Wijenayaka AR; Yang D; Prideaux M; Ito N; Kogawa M; Anderson PH; Morris HA; Solomon LB; Loots GG; Findlay DM; Atkins GJ
Dirección:Centre for Orthopaedic and Trauma Research, University of Adelaide, Adelaide, South Australia 5005, Australia.
Título:1α,25-dihydroxyvitamin D3 stimulates human SOST gene expression and sclerostin secretion.
Fuente:Mol Cell Endocrinol; 413:157-67, 2015 Sep 15.
ISSN:1872-8057
País de publicación:Ireland
Idioma:eng
Resumen:Sclerostin, the SOST gene product, is a negative regulator of bone formation and a positive regulator of bone resorption. In this study, treatment of human primary osteoblasts, including cells differentiated to an osteocyte-like stage, with 1α,25-dihydroxyvitaminD3 (1,25D) resulted in the dose-dependent increased expression of SOST mRNA. A similar effect was observed in human trabecular bone samples cultured ex vivo, and in osteocyte-like cultures of differentiated SAOS2 cells. Treatment of SAOS2 cells with 1,25D resulted in the production and secretion of sclerostin protein. In silico analysis of the human SOST gene revealed a single putative DR3-type vitamin D response element (VDRE) at position -6216 bp upstream of the transcription start site (TSS). This sequence was confirmed to have strong VDRE activity by luciferase reporter assays and electrophoretic mobility shift analysis (EMSA). Sequence substitution in the VDR/RXR half-sites abolished VDRE reporter activity and binding of nuclear proteins. A 6.3 kb fragment of the human proximal SOST promoter demonstrated responsiveness to 1,25D. The addition of the evolutionary conserved region 5 (ECR5), a known bone specific enhancer region, ahead of the 6.3 kb fragment increased basal promoter activity but did not increase 1,25D responsiveness. Site-specific mutagenesis abolished the responsiveness of the 6.3 kb promoter to 1,25D. We conclude that 1,25D is a direct regulator of human SOST gene and sclerostin protein expression, extending the pathways of control of sclerostin expression. At least some of this responsiveness is mediated by the identified classical VDRE however the nature of the transcriptional regulation by 1,25D warrants further investigation.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nombre de substancia:0 (Bone Morphogenetic Proteins); 0 (Genetic Markers); 0 (SOST protein, human); FXC9231JVH (Calcitriol)


  9 / 131 MEDLINE  
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PMID:25966099
Autor:Lu L; Li SM; Zhang L; Liu XQ; Li DY; Zhao XL; Liu YP
Dirección:Farm Animal Genetic Resources Exploration and Innovation Key Laboratory of Sichuan Province, Sichuan Agricultural University, Ya'an, China.
Título:Expression of ß-defensins in intestines of chickens injected with vitamin D3 and lipopolysaccharide.
Fuente:Genet Mol Res; 14(2):3330-7, 2015 Apr 13.
ISSN:1676-5680
País de publicación:Brazil
Idioma:eng
Resumen:The objective of this study was to evaluate the effect of vitamin D3 (VD3) on the regulation of chicken intestinal ß-defensin genes under normal and lipopolysaccharides (LPS) conditions. Four treatment groups were used, including a negative control group, VD3-injection group, LPS-injection group, and both VD3-injection and LPS-injection group. At 4, 24, and 48 h post-injection, intestines were collected and RNA was isolated to measure the chicken ß-defensin genes with putative vitamin D responsive elements using quantitative polymerase chain reaction. Expressions of all 7 chicken ß-defensin genes was detectable in the intestines. Significant increases in GAL-6, -7 and -9 were found following LPS injection treatment at 4, 24, and 48 h post-injection, respectively, whereas VD3 injection did not affect the expression of any investigated genes under normal conditions. However, the expression of GAL-4, -5, -6, and -10 were synergistically upregulated by VD3 in combination with LPS. These results suggest that VD3 enhances the immune immunity during LPS challenge by inducing the expression of chicken ß-defensin genes when birds are exposed to immune stressors.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Avian Proteins); 0 (Lipopolysaccharides); 0 (beta-Defensins); 1C6V77QF41 (Cholecalciferol)


  10 / 131 MEDLINE  
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PMID:25548222
Autor:Thangamani S; Kim M; Son Y; Huang X; Kim H; Lee JH; Cho J; Ulrich B; Broxmeyer HE; Kim CH
Dirección:Laboratory of Immunology and Hematopoiesis, Department of Comparative Pathobiology, College of Veterinary Medicine, Purdue University, West Lafayette, IN 47907;
Título:Cutting edge: progesterone directly upregulates vitamin d receptor gene expression for efficient regulation of T cells by calcitriol.
Fuente:J Immunol; 194(3):883-6, 2015 Feb 01.
ISSN:1550-6606
País de publicación:United States
Idioma:eng
Resumen:The two nuclear hormone receptor ligands progesterone and vitamin D (vit.D) play important roles in regulating T cells. The mechanism that connects these two hormones in regulating T cells has not been established. In this study, we report that progesterone is a novel inducer of vit.D receptor (VDR) in T cells and makes T cells highly sensitive to calcitriol. At the molecular level, the induction by progesterone is mediated by two progesterone receptor-binding elements in the intron region after the first noncoding exon of the human VDR gene. Increased expression of VDR by progesterone allows highly sensitive regulation of T cells by vit.D even when vit.D levels are suboptimal. This novel regulatory pathway allows enhanced induction of regulatory T cells but suppression of Th1 and Th17 cells by the two nuclear hormones. The results have significant ramifications in effective regulation of T cells to prevent adverse immune responses during pregnancy.
Tipo de publicación:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Nombre de substancia:0 (Receptors, Calcitriol); 4G7DS2Q64Y (Progesterone); FXC9231JVH (Calcitriol)



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