Source:http://linkedlifedata.com/resource/pubmed/id/11714843
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2001-11-20
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| pubmed:abstractText |
Scavenger receptor class B type I (SR-BI) mediates the selective uptake of HDL cholesteryl esters (CEs) by the liver. LPL promotes this selective lipid uptake independent of lipolysis. In this study, the role of SR-BI in the mechanism of this LPL-mediated increase in selective CE uptake was explored. Baby hamster kidney (BHK) cells were transfected with the SR-BI cDNA, and significant SR-BI expression could be detected in immunoblots, whereas no SR-BI was visualized in control cells. Y1-BS1 murine adrenocortical cells were cultured without or with adrenocorticotropic hormone, and cells with no detectable or with SR-BI were obtained. These cells incubated without or with LPL in medium containing 125I/[3H]cholesteryl oleyl ether- labeled HDL3; tetrahydrolipstatin inhibited the catalytic activity of LPL. In BHK and in Y1-BS1 cells without or with SR-BI expression, apparent HDL3 selective CE uptake ([3H]CEt - 125I) was detectable. Cellular SR-BI expression promoted HDL3 selective CE uptake by approximately 250-1,900%. In BHK or Y1-BS1 cells, LPL mediated an increase in apparent selective CE uptake. Quantitatively, this stimulating LPL effect was very similar in control cells and in cells with SR-BI expression. The uptake of radiolabeled HDL3 was also investigated in human embryonal kidney 293 (HEK 293) cells that are an established SR-BI-deficient cell model. LPL stimulated [3H]cholesteryl oleyl ether uptake from labeled HDL3 by HEK 293 cells substantially, showing that LPL can induce selective CE uptake from HDL3 independent of SR-BI. To explore the role of cell surface proteoglycans on lipoprotein uptake, we induced proteoglycan deficiency by heparinase treatment. Proteoglycan deficiency decreased the LPL-mediated promotion of HDL3 selective CE uptake. In summary, evidence is presented that the stimulating effect of LPL on HDL3 selective CE uptake is independent of SR-BI and lipolysis. However, cell surface proteoglycans are required for the LPL action on selective CE uptake. It is suggested that pathways distinct from SR-BI mediate selective CE uptake from HDL.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD36,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lipoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Scavenger,
http://linkedlifedata.com/resource/pubmed/chemical/SCARB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Scarb1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Scavenger Receptors, Class B
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0022-2275
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
42
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1740-51
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11714843-Adrenal Cortex,
pubmed-meshheading:11714843-Animals,
pubmed-meshheading:11714843-Antigens, CD36,
pubmed-meshheading:11714843-Cell Line,
pubmed-meshheading:11714843-Cholesterol, HDL,
pubmed-meshheading:11714843-Cholesterol Esters,
pubmed-meshheading:11714843-Cloning, Molecular,
pubmed-meshheading:11714843-Cricetinae,
pubmed-meshheading:11714843-Embryo, Mammalian,
pubmed-meshheading:11714843-Humans,
pubmed-meshheading:11714843-Isotope Labeling,
pubmed-meshheading:11714843-Kidney,
pubmed-meshheading:11714843-Kinetics,
pubmed-meshheading:11714843-Lipoprotein Lipase,
pubmed-meshheading:11714843-Lipoproteins, HDL,
pubmed-meshheading:11714843-Membrane Proteins,
pubmed-meshheading:11714843-Receptors, Immunologic,
pubmed-meshheading:11714843-Receptors, Lipoprotein,
pubmed-meshheading:11714843-Receptors, Scavenger,
pubmed-meshheading:11714843-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11714843-Scavenger Receptors, Class B,
pubmed-meshheading:11714843-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
Lipoprotein lipase mediates an increase in selective uptake of HDL-associated cholesteryl esters by cells in culture independent of scavenger receptor BI.
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| pubmed:affiliation |
Universitaetsklinikum Hamburg-Eppendorf, Klinik und Poliklinik fuer Innere Medizin, Martinistrasse 52, 20246 Hamburg, Germany. Rinninger@uke.uni-hamburg.de
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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