Distribution of the 1,25 dihydroxy-vitamin D3 receptor in the bursa of Fabricius of chicken

1991 ◽  
Vol 47 (8) ◽  
pp. 838-841 ◽  
Author(s):  
M. Petrini ◽  
F. Bianchi ◽  
A. Dolfi ◽  
M. Lupetti
Keyword(s):  
Vitamin D3 ◽  
Bursa Of Fabricius ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
1,25 Dihydroxy Vitamin D3

scholarly journals Expression of 1,25-Dihydroxy Vitamin D3 Receptor in Breast Carcinoma

1998 ◽  
Vol 46 (11) ◽  
pp. 1335-1337 ◽  
Author(s):  
Michael Friedrich ◽  
Leyla Rafi ◽  
Werner Schmidt ◽  
Wolfgang Tilgen ◽  
Jörg Reichrath
Keyword(s):  
Breast Carcinoma ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
1,25 Dihydroxy Vitamin D3

scholarly journals Functions of 1,25-dihydroxy vitamin D3, vitamin D3 receptor and interleukin-22 involved in pathogenesis of gout arthritis through altering metabolic pattern and inflammatory responses

PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e12585
Author(s):  
Yuqi Chen ◽  
Huiya Ma ◽  
Youwei Du ◽  
Jianjian Dong ◽  
Chenkai Jin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Uric Acid ◽  
Vitamin D3 ◽  
Inflammatory Responses ◽  
Gouty Arthritis ◽  
Serum Levels ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
Interleukin 22 ◽  
1,25 Dihydroxy Vitamin D3

Background Gouty arthritis (GA) is a common type of inflammatory arthritis. Recent studies demonstrated that 1,25-dihydroxy vitamin D3 (1,25(OH) 2 VD3) and vitamin D3 receptor (VD-R) play a protective role in acute inflammation, but interleukin-22(IL-22) promotes inflammation, especially for arthritis. However, our understanding of the responses of 1,25(OH) 2VD3 and IL-22 to gout was still unclear. Presently, in-depth metabolomics, bioinformatics and clinical characteristics analyses were performed to elucidate the pathogenesis and valuable clinical indicators of gouty arthritis. Methods Peripheral venous blood was taken for investigation. The levels of IL-22 and 1,25(OH)2VD3 were determined in patient’s plasma via ELISA, and the mRNA levels of IL-22 and VD-R were measured via qRT-PCR. The interaction network of VD-R and IL22 were constructed by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING), and the biological function of the related proteins were analyzed by Clusterprofiler Metabolomics were performed to decipher the metabolic variations of GA. Results The levels of VD-R and 1,25(OH) 2 VD3 were identified to be low. What,s more, GA patients were reported to have high expression of IL-22. And IL-22 levels positively correlated with C-reactiveprotein (CRP) serum levels in the bivariate correlation analysis, whereas the level of 1,25(OH) 2VD3 negatively correlated with that of CRP. GO and KEGG analyses revealed that IL-22 and 1,25(OH) 2 VD3 were involved in stress immunity and inflammatory responses. These pathways are known to play a role in GA pathogenesis. Meanwhile, the metabolic profiles of GA serum showed that the increase in various amino acids and uric acid are involved in GA pathogenesis. Importantly, VD-R and IL22 closely correlated with the level of key metabolites uric acid, whose increase promoted the occurrence of GA. Conclusion GA patients have low levels of VD-R and 1,25(OH) 2 VD3, and high levels of IL-22 together with various amino acids and uric acid. The levels of IL-22 and 1,25(OH) 2VD3 were positively and negatively correlated with C-reactive protein (CRP) serum levels, respectively. Both IL-22 and 1,25(OH) 2 VD3 functioned in GA-related immune and inflammatory responses, and closely correlated with the level of GA-related uric acid. Overall, IL-22, VD-R and 1,25(OH) 2 VD3 play functionally important roles in inflammatory responses and are relevant to gout pathogenesis.

Presence of a 1,25-dihydroxy-vitamin D3 receptor in chick skeletal muscle myoblasts

1985 ◽  
Vol 128 (1) ◽  
pp. 305-311 ◽  
Author(s):  
Ricardo Boland ◽  
Anthony Norman ◽  
Eberhard Ritz ◽  
Wilhelm Hasselbach
Keyword(s):  
Skeletal Muscle ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
1,25 Dihydroxy Vitamin D3

Impact of the Vitamin D3 receptor on growth-regulatory pathways in mammary gland and breast cancer

2002 ◽  
Vol 83 (1-5) ◽  
pp. 85-92 ◽  
Author(s):  
JoEllen Welsh ◽  
Jennifer A. Wietzke ◽  
Glendon M. Zinser ◽  
Sarah Smyczek ◽  
Saara Romu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Regulatory Pathways ◽  
Vitamin D3 Receptor

Ligand modulates the conversion of DNA-bound vitamin D3 receptor (VDR) homodimers into VDR-retinoid X receptor heterodimers

1994 ◽  
Vol 14 (5) ◽  
pp. 3329-3338
Author(s):  
B Cheskis ◽  
L P Freedman
Keyword(s):  
Ligand Binding ◽  
Vitamin D3 ◽  
Hormone Receptors ◽  
Steroid Receptors ◽  
Dependent Manner ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
Binding Domains

Protein dimerization facilitates cooperative, high-affinity interactions with DNA. Nuclear hormone receptors, for example, bind either as homodimers or as heterodimers with retinoid X receptors (RXR) to half-site repeats that are stabilized by protein-protein interactions mediated by residues within both the DNA- and ligand-binding domains. In vivo, ligand binding among the subfamily of steroid receptors unmasks the nuclear localization and DNA-binding domains from a complex with auxiliary factors such as the heat shock proteins. However, the role of ligand is less clear among nuclear receptors, since they are constitutively localized to the nucleus and are presumably associated with DNA in the absence of ligand. In this study, we have begun to explore the role of the ligand in vitamin D3 receptor (VDR) function by examining its effect on receptor homodimer and heterodimer formation. Our results demonstrate that VDR is a monomer in solution; VDR binding to a specific DNA element leads to the formation of a homodimeric complex through a monomeric intermediate. We find that 1,25-dihydroxyvitamin D3, the ligand for VDR, decreases the amount of the DNA-bound VDR homodimer complex. It does so by significantly decreasing the rate of conversion of DNA-bound monomer to homodimer and at the same time enhancing the dissociation of the dimeric complex. This effectively stabilizes the bound monomeric species, which in turn serves to favor the formation of a VDR-RXR heterodimer. The ligand for RXR, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex. These results may explain how a nuclear receptor can bind DNA constitutively but still act to regulate transcription in a fully hormone-dependent manner.

Mechanisms of gene regulation by vitamin D3 receptor: a network of coactivator interactions

Gene ◽  
2000 ◽  
Vol 246 (1-2) ◽  
pp. 9-21 ◽  
Author(s):  
Christophe Rachez ◽  
Leonard P. Freedman
Keyword(s):  
Gene Regulation ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Vitamin D3 Receptor
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