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  • 1
    Electronic Resource
    Electronic Resource
    Fluorescence resonance energy transfer analysis of the structure of the four-way DNA junction (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 4846-4856 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00135a016
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  • 2
    Electronic Resource
    Electronic Resource
    The orphan receptor family RZR/ROR, melatonin and 5-lipoxygenase: An unexpected relationship (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of pineal research 18 (1995), S. 0 
    Details
    ISSN: 1600-079X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The orphan receptors RZRoα, RZRβ, RORod, RZRα2, RORα3, and RORγform a subfamily within the superfamily of nuclear hormone receptors. Recently, experimental evidence that the pineal gland hormone melatonin is the natural ligand for these nuclear receptors has come to light. This discovery is rather surprising, given that most people in the field believed melatonin acts exclusively through membrane receptors. However, these new findings establish a nuclear signalling pathway for melatonin, i.e., direct ligand-induced control of target gene transcription, which most probably mediates part of the physiological functions of the hormone. Interestingly, the very recently identified first RZR/melatonin responding gene, 5-Iipoxygenase, is not expressed in the brain and is not involved in circadian rhythmicity, but rather acts in the periphery, mainly in myeloid cells, as one of the key enzymes of allergic and inflammatory reactions. Thus, nuclear melatonin signalling opens up a new perspective in understanding the actions of the pineal gland hormone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-079X.1995.tb00157.x
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  • 3
    Electronic Resource
    Electronic Resource
    Two nuclear signalling pathways for vitamin D (1993)
    [s.l.] : Nature Publishing Group
    Nature 361 (1993), S. 657-660 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Recent evidence indicates that the retinoid/thyroid hor-mone/vitamin D subfamily of nuclear receptors might bind to their response elements only as heterodimers with RXR (refs 11-16). We wondered if both ligands, 1,25-dihydroxy-vitamin D3 (referred to as vitamin D) and 9-c/s-retinoic acid17'18, are ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/361657a0
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  • 4
    Electronic Resource
    Electronic Resource
    Vitamin D 3 -thyroid hormone receptor heterodimer polarity directs ligand sensitivity of transactivation (1994)
    [s.l.] : Nature Publishing Group
    Nature 370 (1994), S. 382-386 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] FIG. 1 Cooperativity of VDR-T3R heterodimers. a, Response elements. Comparison of the binding affinity of VDR-VDR, VDR-RXR, VDR-RAR and VDR-T3R complexes to all known natural VD response elements (VDRE) (ref. 17, and data not shown) showed that the VD response elements of rat calbindin-D9K (ref. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/370382a0
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  • 5
    Electronic Resource
    Electronic Resource
    Structural variants of the vitamin D analogue EB1089 reduce its ligand sensitivity and promoter selectivity (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 71 (1998), S. 340-350 
    Details
    ISSN: 0730-2312
    Keywords: vitamin D analogues ; vitamin D receptor ; ligand binding ; limited protease digestion ; ligand-dependent gel shift assay ; gene regulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The nuclear hormone 1α,25-dihydroxyvitamin D3 (VD) has important cell-regulatory functions but also a strong calcemic effect. Therefore, various VD analogues have been synthesized and screened for their biological profile. In order to gain more insight into the molecular basis of the high antiproliferative but low calcemic action of the VD analogue EB1089, we characterized this compound in comparison to five structurally related VD analogues. The activities of the six VD analogues in in vitro assays (limited protease digestion assays for determining interaction with monomeric vitamin D receptor (VDR), ligand-dependent gel shift assays for showing the increase of DNA binding of VDR-retinoid X receptor (RXR) heterodimers, and reporter gene assays on different types of VD response elements for demonstrating the efficacy in nuclear VD signalling) were found to represent their biological potency (antiproliferative effect on different malignant cell lines). In this series, EB1089 proved to be the most potent VD analogue; that is, every structural modification (20-epi configuration, cis-configuration at position C24, or changes at the ethyl groups at position C25) appeared to reduce the determined activities mediated through the VDR of these analogues. Moreover, the modifications of EB1089 resulted in a loss of VD response element selectivity, suggesting that this parameter is very critical for the biological profile of this VD analogue. J. Cell. Biochem. 71:340-350, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    1α,25-Dihydroxyvitamin D3 receptor as a mediator of transrepression of retinoid signaling (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 67 (1997), S. 287-296 
    Details
    ISSN: 0730-2312
    Keywords: vitamin D3 receptor ; regulation of transcription ; retinoid signaling transrepression ; tumor necrosis factor-α receptor type I ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The receptors for retinoic acid (RA) and for 1α,25-dihydroxyvitamin D3 (VD), RAR, RXR, and VDR are ligand-inducible members of the nuclear receptor superfamily. These receptors mediate their regulatory effects by binding as dimeric complexes to response elements located in regulatory regions of hormone target genes. Sequence scanning of the tumor necrosis factor-α type I receptor (TNFαRI) gene identified a 3′ enhancer region composed of two directly repeated hexameric core motifs spaced by 2 nucleotides (DR2). On this novel DR2-type sequence, but not on a DR5-type RA response element, VD was shown to act through its receptor, the vitamin D receptor (VDR), as a repressor of retinoid signalling. The repression appears to be mediated by competitive protein-protein interactions between VDR, RAR, RXR, and possibly their cofactors. This VDR-mediated transrepression of retinoid signaling suggests a novel mechanism for the complex regulatory interaction between retinoids and VD. J. Cell. Biochem. 67:287-296, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    High-affinity nuclear receptor binding of 20-epi analogues of 1,25-dihydroxyvitamin D3 correlates well with gene activation (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 62 (1996), S. 325-333 
    Details
    ISSN: 0730-2312
    Keywords: regulation of transcription ; vitamin D3 analogues ; vitamin D3 receptor ; receptor binding ; limited protease digestion assay ; structure-activity relationships ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The hormone 1,25-dihydroxyvitamin D3 (VD) has the potential for clinical use in several diseases, such as cancer, osteoporosis, and psoriasis. The action of VD is mediated by primary responding genes that contain in their promoter region a binding site for the transcription factor VDR. Most of the known VD response elements are formed by a direct repeat of two hexameric core binding motifs spaced by three nucleotides (DR3) bound by a heterodimer of VDR and the retinoid X receptor (RXR). Various VD analogues have been developed in order to optimize the therapeutic profile of VD. This report presents a novel experimental system that may help in the understanding of the structural basis for the high potency of a VD analogue like KH1060, which is a 20-epi-22-oxa-derivative of VD. In human breast cancer cells, MCF-7, the half-maximal gene activation values for KH1060 and seven of its structural precursors were determined on a DR3-type VD response element. These eight analogues cover conservative structural changes from 20-epi-VD (MC1288) to KH1060. With a modified version of the limited protease digestion assay the functional affinity of the analogues to VDR was measured. The functional receptor affinity of the eight analogues was found to be directly proportional to their potency in VDR-RXR-mediated gene activity. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Potent gene regulatory and antiproliferative activities of 20-methyl analogues of 1,25 dihydroxyvitamin D3 (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 63 (1996), S. 199-206 
    Details
    ISSN: 0730-2312
    Keywords: regulation of transcription ; control of proliferation ; vitamin D3 analogues ; vitamin D3 receptor ; limited protease digestion assay ; lymphocytes ; breast cancer cells ; promoter selectivity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biological active form of vitamin D3, 1,25-dihydroxyvitamin D3 (VD), regulates cellular growth and differentiation. This provides the hormone with an interesting therapeutic potential. However, hypercalcemia is a side effect, which is caused by VD's classical action, the regulation of calcium homeostasis. This made the need for VD analogues with selectively increased cell regulatory properties. Studies with 20-epi analogues pointed out the importance of the carbon-20 position and led to the development of 20-methyl derivatives of VD. In this report the biological properties of the compounds ZK161422 and ZK157202, which are 20-methyl- and 20-methyl-23-eneanalogues, respectively, have been analyzed in comparison with VD. Both compounds show about 2-fold lower affinity to the VD receptor (VDR) than VD. However, compared to VD, their antiproliferative effect is up to 30-fold higher on human peripheral blood mononuclear cells and even up to 300-fold higher on human breast cancer MCF-7 cells. Whereas the hypercalcemic effect for ZK157202 is also increased 10-fold, ZK161422 has the same calcium-mobilizing potency as VD. Moreover, ZK161422, but not ZK157202, showed preference for gene activation from a promoter carrying a VD response element with a palindromic arrangement of two hexameric receptor binding sites spaced by 9 nucleotides (IP9) rather than for activation from a response element formed by a direct repeat spaced by 3 nucleotides (DR3). This observation supports a model, in which promoter selectivity reflects the selectively increased antiproliferative effect of VD analogues. © 1996 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Sensitive induction of apoptosis in breast cancer cells by a novel 1,25-dihydroxyvitamin D3 analogue shows relation to promoter selectivity (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 552-562 
    Details
    ISSN: 0730-2312
    Keywords: apoptosis ; tumor regression ; control of proliferation ; vitamin D3 analogues ; breast cancer ; vitamin D3 receptor ; regulation of transcription ; promoter selectivity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biologically active form of vitamin D3, the nuclear hormone 1α,25-dihydroxyvitamin D3 (VD), is an important regulator of cellular growth, differentiation, and death. The hormone mediates its action through the activation of the transcription factor VDR, which is a member of the superfamily of nuclear receptors. In most cases the ligand-activated VDR is found in complex with the retinoid X receptor (RXR) and stimulates gene transcription mainly from VD response elements (VDREs) that are formed by two hexameric core binding motifs and are arranged either as a direct repeat spaced by three nucleotides (DR3) or as an inverted palindrome spaced by nine nucleotides (IP9). The two VD analogues CB1093 and EB1089 are both very potent inhibitors of the proliferation of MCF-7 cultured breast cancer cells displaying approximately 100-fold lower IC50 values (0.1 nM) than the natural hormone. In addition, CB1093 is even more potent in vivo than EB1089 in producing regression of experimental mammary tumors. Moreover, both VD analogues induce apoptosis in MCF-7 cells, but CB1093 is effective at concentrations approximately 10-fold lower than EB1089. In accordance, the reduction of Bcl-2 protein expression showed CB1093 to be more potent than EB1089. This suggests that the antiproliferative effect of CB1093 may be related mainly to its apoptosis inducing effect, whereas EB1089 may preferentially have effects on growth arrest. EB1089 is known to result in a selectivity for the activation of IP9-type VDREs, whereas CB1093 shows a preference for the activation of DR3-type VDREs. This promoter selectivity suggests that the effects of VD and its analogues on growth arrest and the induction of apoptosis may be mediated by different primary VD responding genes. In conclusion, CB1093 was found to be a potent inhibitor of rat mammary tumor growth in vivo. CB1093 also displayed a high potency in vitro in the induction of apoptosis, a process that may be linked to a promoter selectivity for DR3-type VDREs. J. Cell. Biochem. 66: 552-562, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of a vitamin D3 response element in the fibronectin gene that is bound by a vitamin D3 receptor homodimer (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 60 (1996), S. 322-333 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; VDR ; homodimer ; vitamin D regulation ; transcription ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin (FN) is an important adhesive noncollagenous glycoprotein involved in maintenance of the extracellular matrix and cell adhesiveness, loss of which has been implicated in the metastatic potential of cells. Regulation of FN occurs at the transcriptional level by the active metabolite of vitamin D3, 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3). Transient transfection of homologous and heterologous promoter reporter constructs into ROS 17/2,8 (rat osteosarcoma), NIH 3T3 (mouse fibroblast), and MCF-7 (human mammary carcinoma) cell lines showed a consistent two- to threefold induction of transcription when stimulated with 1,25-(OH)2D3. These heterologous promoter transfection studies with gel shift analysis locate a third, natural DR6-type vitamin D responsive element (VDRE) at nucleotide positions -171 to -154 in the murine FN promoter. Interestingly, this VDRE is also present in rat and human FN promoters. This study shows that 1,25-(OH)2D3 induces FN transcription from an existing elevated basal transcriptional activity by acting through two putative hexameric core binding motifs which bind VDR homodimers. Furthermore, the FN VDRE is the first homodimer-type VDRE that is not overlaid by a DR3-type structure. © 1996 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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