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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
1984-12-27
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pubmed:abstractText |
Apolipoprotein (apo) E-deficient rat high-density lipoproteins (HDL) bind to isolated rat hepatocytes at 4 degrees C by a process shown to be saturable and competed for by an excess of unlabeled HDL. Uptake (binding and internalization) at 37 degrees C was also saturable and competed for by an excess of unlabeled HDL. At 37 degrees C the HDL apoprotein was degraded as evidenced by the appearance of trichloroacetic acid-soluble radioactivity in the incubation media. The binding of a constant amount of 125I-apo-E-deficient HDL was measured in the presence of increasing concentrations of various lipoproteins. HDL and dimyristoyl phosphatidylcholine (DMPC) X apo-A-I complexes decreased binding by 80 and 65%, respectively. Human low-density lipoproteins, DMPC X apo-E complexes, and DMPC vesicles alone did not compete for apo-E-deficient HDL binding. However, DMPC X apo-E complexes did compete for the binding of the total HDL fraction that contained apo-E but to a lesser extent than did DMPC X apo-A-I. DMPC X 125I-apo-A-I complexes also bound to hepatocytes, and this binding was competed for by excess HDL (70%) and DMPC X apo-A-I complexes (65%), but there was no competition for binding by DMPC vesicles or DMPC X apo-E complexes. It thus appears that hepatocytes have a specific receptor for HDL and that apo-A-I is the ligand for this receptor.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Monensin,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lipoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/high density lipoprotein binding...,
http://linkedlifedata.com/resource/pubmed/chemical/high density lipoprotein receptors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13814-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6094531-Animals,
pubmed-meshheading:6094531-Apolipoprotein A-I,
pubmed-meshheading:6094531-Apolipoproteins A,
pubmed-meshheading:6094531-Carrier Proteins,
pubmed-meshheading:6094531-Dimyristoylphosphatidylcholine,
pubmed-meshheading:6094531-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6094531-Lipoproteins, HDL,
pubmed-meshheading:6094531-Liver,
pubmed-meshheading:6094531-Male,
pubmed-meshheading:6094531-Monensin,
pubmed-meshheading:6094531-RNA-Binding Proteins,
pubmed-meshheading:6094531-Rats,
pubmed-meshheading:6094531-Rats, Inbred Strains,
pubmed-meshheading:6094531-Receptors, Cell Surface,
pubmed-meshheading:6094531-Receptors, Lipoprotein,
pubmed-meshheading:6094531-Substrate Specificity,
pubmed-meshheading:6094531-Time Factors
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pubmed:year |
1984
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pubmed:articleTitle |
A hepatocyte receptor for high-density lipoproteins specific for apolipoprotein A-I.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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