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The vitamin D receptor (VDR) is a protein that is turned on by vitamin D. It is involved in maintaining the mineral equilibrium in the body and adding to growth and hair production. It also treats adipose muscle.

VDRs are expressed in the parathyroid glands, intestines, epithelial cellular material, and many immune system cell types. They are believed to regulate the intestinal absorption of calcium supplement, and to mediate some of the associated with vitamin D in bone maintenance. Fortunately they are thought to enjoy an important position in metabolic rate.

VDR is found in a variety of damaged tissues, including epithelial cells, macrophages, neutrophils, and skin keratinocytes. However , they can be most widely stated in the kidneys and bone tissues.

The VDR is phosphorylated upon serine elements by a lot of protein kinases. These kinases include PKA and PKC. The effect of such kinases about VDR is certainly ligand based. Specifically, the phosphorylation of Ser51 simply by PKC decreased VDR nuclear localization. Likewise, phosphorylation of Ser182 by PKA reduced RXR heterodimerization.

Research have shown that VDRs are present in a subset of glial cells, particularly in oligodendrocytes in white matter. Although VDR immunoreactivity has been found in a number of glial cell lines, no facts has been provided that the existence of VDR in glia is a cause of increased likelihood of tumorigenesis.

In addition , VDR appears to be present in a subset of neurons. Actually nuclear discoloration has been showed in man cortex and glial cell-lines.

A large 220-kDa protein can be found in human most important glioblastoma cells. In contrast, a small recombinant VDR-like protein was produced.

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