| pubmed-article:10191285 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0001019 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C1434133 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:10191285 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:10191285 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10191285 | pubmed:dateCreated | 1999-5-3 | lld:pubmed |
| pubmed-article:10191285 | pubmed:abstractText | Although the sterol carrier protein 2 (SCP-2) gene encodes for two proteins, almost nothing is known of the function and potential processing of the larger transcript corresponding to the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase (SCP-x), in intact cells. L-cell fibroblasts transfected with cDNA encoding for the 58 kDa SCP-x protein had a 4.5-fold increase in SCP-x mRNA transcript levels. Western blot analysis showed SCP-x protein expression reached 0.011% of total protein, representing a 4.1-fold increase over basal levels. Surprisingly, the 13.2 kDa SCP-2 protein also increased 2-fold in the transfected cells. This was consistent with part of the 58 kDa SCP-x being proteolytically processed to 13.2 kDa SCP-2 as there was no evidence of an mRNA transcript corresponding to a 13.2/15.2 kDa gene product in the transfected L-cell clones. Confocal immunofluorescence microscopy of transfected L-cells showed that SCP-x/SCP-2 co-localized in highest concentration with catalase in peroxisomes, but significant amounts appeared extra-peroxisomal. Overexpression of SCP-x significantly altered cholesterol uptake and metabolism. Uptake of exogenous [3H]cholesterol and total cholesterol mass were increased 1.9- and 1.4-fold, respectively, in SCP-x expressors. Although cholesterol ester mass was unaltered, incorporation of exogenous [3H]cholesterol and [3H]oleic acid into cholesteryl esters increased 2.3- and 2.5-fold, respectively. These results from intact cells suggest the 13.2 kDa SCP-2 can arise from the larger SCP-2 gene product and indicate a role for the 58 kDa SCP-x protein in cholesterol uptake and intracellular cycling. | lld:pubmed |
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| pubmed-article:10191285 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10191285 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10191285 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10191285 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10191285 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10191285 | pubmed:issn | 0022-2275 | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:PetrescuA DAD | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:KierA BAB | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:SchroederFF | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:RothsJ BJB | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:AtshavesB PBP | lld:pubmed |
| pubmed-article:10191285 | pubmed:author | pubmed-author:StarodubOO | lld:pubmed |
| pubmed-article:10191285 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10191285 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:10191285 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10191285 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10191285 | pubmed:pagination | 610-22 | lld:pubmed |
| pubmed-article:10191285 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10191285 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10191285 | pubmed:articleTitle | Expression and intracellular processing of the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts. | lld:pubmed |
| pubmed-article:10191285 | pubmed:affiliation | Department of Physiology and Pharmacology, Texas A&M University, TVMC, College Station, TX 77843-4466, USA. | lld:pubmed |
| pubmed-article:10191285 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10191285 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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