Linked Life Data

10191285

Source:http://linkedlifedata.com/resource/pubmed/id/10191285

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-5-3
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
610-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10191285-Acetyl-CoA C-Acyltransferase, pubmed-meshheading:10191285-Animals, pubmed-meshheading:10191285-Blotting, Northern, pubmed-meshheading:10191285-Blotting, Western, pubmed-meshheading:10191285-Carrier Proteins, pubmed-meshheading:10191285-Cell Line, pubmed-meshheading:10191285-Cholesterol, pubmed-meshheading:10191285-Cholesterol Esters, pubmed-meshheading:10191285-Esterification, pubmed-meshheading:10191285-Fibroblasts, pubmed-meshheading:10191285-Fluorescent Antibody Technique, pubmed-meshheading:10191285-Gene Expression, pubmed-meshheading:10191285-Kinetics, pubmed-meshheading:10191285-Mice, pubmed-meshheading:10191285-Microbodies, pubmed-meshheading:10191285-Molecular Weight, pubmed-meshheading:10191285-Oleic Acid, pubmed-meshheading:10191285-Plant Proteins, pubmed-meshheading:10191285-Transfection, pubmed-meshheading:10191285-Tritium
pubmed:year
1999
pubmed:articleTitle
Expression and intracellular processing of the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts.
pubmed:affiliation
Department of Physiology and Pharmacology, Texas A&M University, TVMC, College Station, TX 77843-4466, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.