Document Detail


Binding of lipoprotein lipase to the cell surface is essential for the transmembrane transport of chylomicron cholesteryl ester.
MedLine Citation:
PMID:  7115744     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Four cell types, F1 rat heart cells, rat preadipocytes, human skin fibroblasts and bovine endothelial cells, were used to investigate whether surface binding of lipoprotein lipase was essential in the transmembrane transport of chylomicron cholesteryl ester. Exposure of F1 heart cells to colchicine resulted in decrease in endogenous surface-bound lipoprotein lipase and a concomitant fall in the uptake of chylomicron cholesteryl linoleyl ether, a nondegradable analog of cholesteryl ester. Uptake of chylomicron cholesteryl linoleyl ether was enhanced by addition of milk lipoprotein lipase and this enhancement also persisted in the presence of colchicine. The drug did not reduce surface binding to the enzyme. Milk lipoprotein lipase was bound to the cell surface of the different cell types and its fate during chase in enzyme-free medium was determined. The t 1/2 of surface-bound enzyme in endothelial cells and in F1 heart cells was about 2 h; it was 4 h in skin fibroblasts. The decrease in surface-bound lipoprotein lipase was accompanied by a parallel fall in the binding and uptake of chylomicron cholesteryl linoleyl ether by the various cell types examined. This decrease in the uptake of cholesteryl linoleyl ether occurred even though lipoprotein lipase activity in the medium was present, as evidenced by the hydrolysis of [14C]triacylglycerol. Release of surface-bound endogenous or exogenous lipoprotein lipase by heparin was accompanied by almost complete elimination of uptake of cholesteryl linoleyl ether in presence of complete hydrolysis of [14C]triacylglycerol. The present results indicate that the transmembrane transport of cholesteryl ester is catalyzed by lipoprotein lipase only when the enzyme is bound to the cell membrane.
Authors:
T Chajek-Shaul; G Friedman; O Stein; T Olivecrona; Y Stein
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  712     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1982 Jul 
Date Detail:
Created Date:  1982-12-02     Completed Date:  1982-12-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  200-10     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adipose Tissue / metabolism
Animals
Aorta / metabolism
Cattle
Cell Membrane / metabolism*
Cells, Cultured
Cholesterol Esters / metabolism*
Chylomicrons / metabolism*
Endothelium / metabolism
Fibroblasts / metabolism
Humans
Lipoprotein Lipase / metabolism*
Lymph / metabolism
Male
Muscle, Smooth, Vascular
Myocardium / metabolism
Rats
Skin / metabolism
Chemical
Reg. No./Substance:
0/Cholesterol Esters; 0/Chylomicrons; EC 3.1.1.34/Lipoprotein Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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