| pubmed-article:9699885 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9699885 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9699885 | lifeskim:mentions | umls-concept:C0044707 | lld:lifeskim |
| pubmed-article:9699885 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:9699885 | lifeskim:mentions | umls-concept:C0301818 | lld:lifeskim |
| pubmed-article:9699885 | pubmed:issue | 1-6 | lld:pubmed |
| pubmed-article:9699885 | pubmed:dateCreated | 1998-8-27 | lld:pubmed |
| pubmed-article:9699885 | pubmed:abstractText | 11Beta-hydroxysteroid dehydrogenase (11beta-HSD) is thought to confer aldosterone specificity to mineralocorticoid target cells by protecting the mineralocorticoid receptor (MR) from occupancy by endogenous glucocorticoids. In aldosterone target cells the type 2 11beta-HSD is present, which, in contrast to the type 1 11beta-HSD, has very high affinity for its substrate, is unidirectional and prefers NAD as cofactor. cDNAs encoding 11beta-HSD2 have been recently cloned from different species, and the cell-specific expression of its mRNA and protein were determined. 11Beta-HSD2 is expressed in every aldosterone target tissue. Northern analysis revealed that the rabbit 11beta-HSD2 is expressed at high levels in the renal collecting duct and at much lower levels in the colon. RT-PCR experiments demonstrated that 11beta-HSD2 mRNA is present only in aldosterone target cells within the kidney. We determined the subcellular localization of the rabbit 11beta-HSD2 using a chimera encoding 11beta-HSD2 and the green fluorescent protein (GFP). This construct was stably transfected into CHO and MDCK cells. The expressed 11beta-HSD2/GFP protein retained high enzymatic activity, and its characteristics were undistinguishable from those of the native enzyme. The intracellular localization of this protein was determined by fluorescence microscopy. 11Beta-HSD2-associated fluorescence was observed as a reticular network over the cytoplasm whereas the plasma membrane and the nucleus were negative, suggesting endoplasmic reticulum (ER) localization. Co-staining with markers for ER proteins, the Golgi membrane, mitochondria and nucleus confirmed that 11beta-HSD2 is localized exclusively to the ER. To determine what structural motifs are responsible for the ER localization, we generated deletion mutants missing the C-terminal 42 and 118 amino acids, and fused them to GFP. Similarly as with the intact 11beta-HSD2, these mutants localized exclusively to the ER. Both C-terminal deletion mutants completely lost dehydrogenase activity, independently whether activity was determined in intact cells or homogenates. These results indicate that 11beta-HSD2 has a novel ER retrieval signal which is not localized to the C-terminal region. In addition, the C-terminal 118 amino acids are essential for NAD-dependent 11beta-HSD activity. | lld:pubmed |
| pubmed-article:9699885 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9699885 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9699885 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9699885 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9699885 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9699885 | pubmed:issn | 0960-0760 | lld:pubmed |
| pubmed-article:9699885 | pubmed:author | pubmed-author:Fejes-TóthGG | lld:pubmed |
| pubmed-article:9699885 | pubmed:author | pubmed-author:Náray-Fejes-T... | lld:pubmed |
| pubmed-article:9699885 | pubmed:author | pubmed-author:ColombowalaI... | lld:pubmed |
| pubmed-article:9699885 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9699885 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:9699885 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9699885 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9699885 | pubmed:pagination | 311-6 | lld:pubmed |
| pubmed-article:9699885 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:meshHeading | pubmed-meshheading:9699885-... | lld:pubmed |
| pubmed-article:9699885 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9699885 | pubmed:articleTitle | The role of 11beta-hydroxysteroid dehydrogenase in steroid hormone specificity. | lld:pubmed |
| pubmed-article:9699885 | pubmed:affiliation | Department of Physiology, Dartmouth Medical School, Lebanon, NH 03756, USA. | lld:pubmed |
| pubmed-article:9699885 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9699885 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9699885 | pubmed:publicationType | Review | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9699885 | lld:pubmed |
