Vitamin D receptor and retinoid X receptor interactions in motion

Bársony, Julia; Prüfer, Kirsten

doi:10.1016/s0083-6729(02)65071-x

Cited by 61 publications

(37 citation statements)

References 213 publications

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“…92 In contrast, similar irradiation of rats leads to a 40-fold increase in vitamin D 3 . 92 This presumably relates to the presence of 7-DHC-D 7 -reductase, an enzyme capable of degrading 7-DHC, in the skin of cats. 145 Not surprisingly, a study in Australia demonstrated that, unlike other species, dogs did not show seasonal variation in serum 25-hydroxyvitamin D (25(OH)D) concentrations.…”

Section: Biology Of Vitamin D Activation Of Vitamin Dmentioning

confidence: 99%

Vitamin D Metabolism and Rickets in Domestic Animals

2010

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Rickets and osteomalacia are increasing in prevalence in people because of cultural practices, breast-feeding, decreased sun exposure, and increased sunscreen usage. Several hereditary forms of rickets owing to either renal phosphate wasting or defects in vitamin D metabolism are also reported in people. Rickets is well recognized in domestic animals, but published reports are not always supported by microscopic findings, and diagnoses based on clinical signs and radiology are unreliable. Most cases in domestic animals are caused by dietary deficiency of either vitamin D or phosphorus, but occasional inherited forms are reported in pigs, sheep, cats, and dogs. There is variation between species in susceptibility to dietary vitamin D and phosphorus deficiency and in the ability to manufacture vitamin D in their skin. A number of mouse models have been discovered or created to study human skeletal diseases and skeletal homeostasis. With the discovery that vitamin D is involved in not only calcium and phosphorus homeostasis but also in the immune system and cancer, there is great potential for new and existing animal models to generate valuable information about vitamin D and its many functions. This review presents an overview of vitamin D metabolism and rickets in domestic and laboratory animals and makes comparisons where appropriate with the disease in humans. Keywords bone, rickets, vitamin D, phosphorus, genetic diseasesRickets is a classic metabolic bone disease of humans and animals, first described in the first and second centuries. 158,165 With the discovery that vitamin D could prevent rickets, the prevalence of this disease in developed countries plummeted; however, it still occurs. In fact, the prevalence of rickets and vitamin D insufficiency is increasing in people of all ages in the developed world, due in part to decreased sunlight exposure and widespread sunscreen usage. 88 The disease is well recognized in animals, but published reports are uncommon and sometimes confusing.The pathogenesis of rickets involves impaired mineralization of physeal and epiphyseal cartilage during endochondral ossification and of newly formed osteoid. Most cases in domestic animals are caused by dietary deficiency of either vitamin D or phosphorus, but occasional inherited forms are reported. 109,200 Osteomalacia is caused by a failure of newly formed osteoid to mineralize, but it occurs in adults after closure of growth plates. 109In this article, we review vitamin D metabolism and rickets, with reference to the disease in domestic animals but presenting comparison with the disease in humans where appropriate. Biology of Vitamin D Activation of Vitamin DVitamin D is available from two sources: isomerization of 7-dehydrocholesterol (7-DHC) in the skin to vitamin D 3 following exposure to ultraviolet light or from ingestion of vitamin D 2 or D 3 in the diet. Only a few foods, including cod liver oil and fatty fish such as salmon and sardines, naturally contain high concentrations of vitamin D 3 .49 Vitamin D 2 i...

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Section: Biology Of Vitamin D Activation Of Vitamin Dmentioning

confidence: 99%

Vitamin D Metabolism and Rickets in Domestic Animals

2010

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“…This latter finding strongly suggests that the VDR requires a heterodimeric partner to bind effectively to this sequence of DNA. Indeed, incubation of the probe with 10 ng of purified VDR along with 10 ng of purified RXR , which has been shown to be a coregulator of VDR binding and transactivation (Barsony & Prufer 2002), resulted in the formation of a strong complex (lane 8). However, since it migrated slightly above that observed for the lower complex formed with nuclear extract (compare lane 8 with lane 9), it suggested to us that the lower nuclear complex is not composed of a VDR/RXR heterodimer, but rather as indicated by antibody experiments (Fig.…”

Section: Emsa With Purified Proteins Confirms Vdr and Sp1 Bindingmentioning

confidence: 99%

“…It is known that the RXRs (Barsony & Prufer 2002), and under some circumstances, the RARs (Pemrick et al 1998), can bind with the VDR to activate or repress corresponding DNA response elements. Since the purified VDR only formed a weakly detectable complex (Fig.…”

Section: Characterization Of a Vdre In The Egfr Promoter · Kenneth Rmentioning

confidence: 99%

Identification and characterization of a response element in the EGFR promoter that mediates transcriptional repression by 1,25-dihydroxyvitamin D3 in breast cancer cells

McGaffin

Chrysogelos²

2005

Journal of Molecular Endocrinology

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Reduction of epidermal growth factor receptor (EGFR) mRNA and protein by 1,25-dihydroxyvitamin D3 has been documented in MCF7, T47D, and BT549 breast cancer cells. In the present report, functional mapping of the EGFR promoter in BT549 cells has revealed a sequence of DNA between nucleotide positions −536 and −478 that resembles a consensus vitamin D response element (VDRE) and confers a vitamin D response upon both the homologous and a minimal heterologous promoter. In vitro footprinting and gel shift assays demonstrate the presence of an unidentified nuclear factor that is required for strong binding of the vitamin D receptor (VDR) to this putative VDRE. An Sp1 binding site was also identified in close proximity and shown to bind Sp1 from nuclear extract. Mutational analysis and functional studies using a minimal heterologous promoter provide evidence that the VDR in concert with an unknown nuclear partner mediates basal EGFR repression through displacement of Sp1 which is augmented in the presence of a ligand.

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“…In some cases, receptors have been shown to accumulate in distinct nuclear foci in the presence of ligand (van Steensel et al, 1995). Intracellular trafficking and subcellular or subnuclear compartmentalization may be a general phenomenon of type II nuclear hormone receptors and could be differentially influenced by ligand interaction, association with cofactors and/or through heterodimerization with RXR (Baumann et al, 2001b;Mackem et al, 2001;Akiyama et al, 2002;Barsony and Prufer, 2002;.…”

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confidence: 99%

Activity and subcellular compartmentalization of peroxisome proliferator-activated receptor α are altered by the centrosome-associated protein CAP350

Patel

Truant

Rachubinski

et al. 2005

Journal of Cell Science

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Peroxisome proliferator-activated nuclear hormone receptors (PPAR) are ligand-activated transcription factors that play pivotal roles in governing metabolic homeostasis and cell growth. PPARs are primarily in the nucleus but, under certain circumstances, can be found in the cytoplasm. We show here that PPARα interacts with the centrosome-associated protein CAP350. CAP350 also interacts with PPARδ, PPARγ and liver-X-receptor α, but not with the 9-cis retinoic acid receptor, RXRα. Immunofluorescence analysis indicated that PPARα is diffusely distributed in the nucleus and excluded from the cytoplasm. However, in the presence of coexpressed CAP350, PPARα colocalizes with CAP350 to discrete nuclear foci and to the centrosome, perinuclear region and intermediate filaments. In contrast, the subcellular distribution of RXRα or of thyroid hormone receptor α was not altered by coexpression of CAP350. An amino-terminal fragment of CAP350 was localized exclusively to nuclear foci and was sufficient to recruit PPARα to these sites. Mutation of the single putative nuclear hormone receptor interacting signature motif LXXLL present in this fragment had no effect on its subnuclear localization but abrogated recruitment of PPARα to nuclear foci. Surprisingly, mutation of the LXXLL motif in this CAP350 subfragment did not prevent its binding to PPARα in vitro, suggesting that this motif serves some function other than PPARα binding in recruiting PPARα to nuclear spots. CAP350 inhibited PPARα-mediated transactivation in an LXXLL-dependent manner, suggesting that CAP350 represses PPARα function. Our findings implicate CAP350 in a dynamic process that recruits PPARα to discrete nuclear and cytoplasmic compartments and suggest that altered intracellular compartmentalization represents a regulatory process that modulates PPAR function.

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Vitamin D receptor and retinoid X receptor interactions in motion

Cited by 61 publications

References 213 publications

Vitamin D Metabolism and Rickets in Domestic Animals

Vitamin D Metabolism and Rickets in Domestic Animals

Identification and characterization of a response element in the EGFR promoter that mediates transcriptional repression by 1,25-dihydroxyvitamin D3 in breast cancer cells

Activity and subcellular compartmentalization of peroxisome proliferator-activated receptor α are altered by the centrosome-associated protein CAP350

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