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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-2-22
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pubmed:abstractText |
The liver is the major organ responsible for the uptake of oxidized low density lipoproteins (Ox-LDL) from the blood circulation with Kupffer cells as major cellular uptake site. Candidate binding proteins for Ox-LDL on membranes from Kupffer and endothelial liver cells were identified with ligand blots. Under nonreducing conditions, a major binding protein with an estimated molecular mass of 95 kDa and a minor stained protein of 220 kDa were detected on Kupffer cell membranes, while endothelial cell membranes expressed only a 220-kDa binding protein. Both the 95-kDa protein of Kupffer cell membranes and the 220-kDa protein of endothelial membranes displayed saturable binding of 125I-Ox-LDL with a Kd of 15 and 5 micrograms/ml, respectively. LDL was a weak competitor for the binding of 125I-Ox-LDL to the 95-kDa protein, while the degree of competition appeared to be dependent on the oxidation grade of LDL with a complete competition with LDL oxidized for 20 h with 10 microM Cu2+. We conclude that the 95-kDa binding protein, highly concentrated on rat Kupffer cells, forms the most likely candidate for mediating the in vivo uptake of Ox-LDL from the blood circulation.
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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/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
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, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Scavenger Receptors, Class B,
http://linkedlifedata.com/resource/pubmed/chemical/acetyl-LDL
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
824-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8288634-Animals,
pubmed-meshheading:8288634-Endothelium, Vascular,
pubmed-meshheading:8288634-Kupffer Cells,
pubmed-meshheading:8288634-Lipoproteins, LDL,
pubmed-meshheading:8288634-Male,
pubmed-meshheading:8288634-Membrane Proteins,
pubmed-meshheading:8288634-Molecular Weight,
pubmed-meshheading:8288634-Oxidation-Reduction,
pubmed-meshheading:8288634-Rats,
pubmed-meshheading:8288634-Rats, Wistar,
pubmed-meshheading:8288634-Receptors, Cell Surface,
pubmed-meshheading:8288634-Receptors, Immunologic,
pubmed-meshheading:8288634-Receptors, Lipoprotein,
pubmed-meshheading:8288634-Receptors, Scavenger,
pubmed-meshheading:8288634-Scavenger Receptors, Class B
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pubmed:year |
1994
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pubmed:articleTitle |
Rat liver Kupffer and endothelial cells express different binding proteins for modified low density lipoproteins. Kupffer cells express a 95-kDa membrane protein as a specific binding site for oxidized low density lipoproteins.
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pubmed:affiliation |
Division of Biopharmaceutics, Leiden-Amsterdam Center for Drug Research, Sylvius Laboratories, University of Leiden, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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