| pubmed-article:12899521 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12899521 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:12899521 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:12899521 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12899521 | pubmed:dateCreated | 2003-8-5 | lld:pubmed |
| pubmed-article:12899521 | pubmed:abstractText | The 25-hydroxyvitamin D-1alpha-OHase (1alpha-OHase) is responsible for producing the active form of vitamin D, 1alpha,25-dihydroxyvitamin D. The enzyme not only is expressed in kidneys, but also is expressed in many nonrenal tissues, including skin. In this study, we compared the regulation of the 1alpha-OHase expression in kidney cells and keratinocytes. Using transfected luciferase reporter gene constructs, we compared the activity and regulatory features of the human 1alpha-OHase gene promoter in C-21 human kidney cells (PTH/PTHrP receptor positive) and cultured human keratinocytes (NHKs). We found that two regions, -1,100 bp and -396 bp from the ATG, were highly sensitive to parathyroid hormone (PTH) in C-21 cells but not in NHK. Furthermore, three CRE-like sequences (CLS) were identified within this PTH-sensitive area of the 1alpha-OHase promoter and when deleted they reduced induction of PTH by 50%-95% in C-21 cells. To further investigate the differential regulation profile, we examined the protein products of 1alpha-OHase in kidney and skin. Western blot analysis of whole cell extracts from these tissues with a 1alpha-OHase-specific antibody revealed the predicted 1alpha-OHase protein product of 56 kDa in kidney and a larger protein product of 59 kDa in skin. Using RT-PCR for the 1alpha-OHase in skin and kidney, we detected an insertion between exons 2 and 3 in skin but not in kidney. These results suggest that the regulation of renal and skin 1alpha-OHase gene expression may be tissue specific and possibly produce different splice variants, and that this specificity is likely conferred by differential expression of CRE-binding proteins in different cell types. In conclusion, the differential tissue expression of 1alpha-OHase gene variants and the tissue-specific regulation profile open up a new paradigm in the understanding of the role of 25-hydroxyvitamin D3 1alpha-hydroxylase gene in the regulation of vitamin D physiology. | lld:pubmed |
| pubmed-article:12899521 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:keyword | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12899521 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12899521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12899521 | pubmed:issn | 0080-0015 | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:HolickMichael... | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:ReichrathJörg... | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:TangprichaVin... | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:ChenTai CTC | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:FlanaganJohn... | lld:pubmed |
| pubmed-article:12899521 | pubmed:author | pubmed-author:WangLilinL | lld:pubmed |
| pubmed-article:12899521 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12899521 | pubmed:volume | 164 | lld:pubmed |
| pubmed-article:12899521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12899521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12899521 | pubmed:pagination | 157-67 | lld:pubmed |
| pubmed-article:12899521 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:12899521 | pubmed:meshHeading | pubmed-meshheading:12899521... | lld:pubmed |
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| pubmed-article:12899521 | pubmed:meshHeading | pubmed-meshheading:12899521... | lld:pubmed |
| pubmed-article:12899521 | pubmed:meshHeading | pubmed-meshheading:12899521... | lld:pubmed |
| pubmed-article:12899521 | pubmed:meshHeading | pubmed-meshheading:12899521... | lld:pubmed |
| pubmed-article:12899521 | pubmed:meshHeading | pubmed-meshheading:12899521... | lld:pubmed |
| pubmed-article:12899521 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12899521 | pubmed:articleTitle | Regulation of the 25-hydroxyvitamin D-1alpha-hydroxylase gene and its splice variant. | lld:pubmed |
| pubmed-article:12899521 | pubmed:affiliation | Department of Medicine, Endocrine Section, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA. | lld:pubmed |
| pubmed-article:12899521 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12899521 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
