The calciferol receptor (VDR) is a protein that is activated by vitamin D. It is interested in maintaining the mineral harmony in the body and causing growth and hair expansion. It also interacts with adipose structure.
VDRs will be expressed in the parathyroid glands, intestines, epithelial virtual data room comparison cells, and many immune system cell types. They are thought to regulate the intestinal ingestion of calcium supplements, and to mediate some of the effects of vitamin D on bone routine service. They are also thought to enjoy an important position in metabolism.
VDR can be found in a variety of areas, including epithelial cells, macrophages, neutrophils, and skin keratinocytes. However , they are most widely expressed in the kidneys and bone.
The VDR is phosphorylated in serine elements by several protein kinases. These kinases include PKA and PKC. The effect of the kinases on VDR is ligand centered. Specifically, the phosphorylation of Ser51 by PKC reduced 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, specifically in oligodendrocytes in white matter. Although VDR immunoreactivity has been recognized in a number of glial cell lines, no data has been shown that the presence of VDR in glia is a cause for increased risk of tumorigenesis.
Additionally , VDR seems to be present in a subset of neurons. In fact , nuclear discoloration has been revealed in man cortex and glial cell-lines.
A large 220-kDa protein is found in human principal glioblastoma skin cells. In contrast, a small recombinant VDR-like protein was produced.