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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2004-11-16
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pubmed:abstractText |
A 70-75 kDa high-density lipoprotein (HDL) particle with pre-beta-electrophoretic migration (pre-beta(1)-HDL) has been identified in several studies as an early acceptor of cell-derived cholesterol. However, the further metabolism of this complex has not been determined. Here we sought to identify the mechanism by which cell-derived cholesterol was esterified and converted to mature HDL as part of reverse cholesterol transport (RCT). Human plasma selectively immunodepleted of pre-beta(1)-HDL was used to study factors regulating pre-beta(1)-HDL production. A major role for phospholipid transfer protein (PLTP) in the recycling of pre-beta(1)-HDL was identified. Cholesterol binding, esterification by lecithin/cholesterol acyltransferase (LCAT) and transfer by cholesteryl ester transfer protein (CETP) were measured using (3)H-cholesterol-labeled cell monolayers. LCAT bound to (3)H-free cholesterol (FC)-labeled pre-beta(1)-HDL generated cholesteryl esters at a rate much greater than the rest of HDL. The cholesteryl ester produced in pre-beta(1)-HDL in turn became the preferred substrate of CETP. Selective LCAT-mediated reactivity with pre-beta(1)-HDL represents a novel mechanism increasing the efficiency of RCT.
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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/CETP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Ester Transfer Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/High-Density Lipoproteins, Pre-beta,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholine-Sterol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14811-20
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15544352-Apolipoprotein A-I,
pubmed-meshheading:15544352-Carrier Proteins,
pubmed-meshheading:15544352-Cells, Cultured,
pubmed-meshheading:15544352-Cholesterol,
pubmed-meshheading:15544352-Cholesterol, HDL,
pubmed-meshheading:15544352-Cholesterol Ester Transfer Proteins,
pubmed-meshheading:15544352-Cholesterol Esters,
pubmed-meshheading:15544352-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:15544352-Fibroblasts,
pubmed-meshheading:15544352-Glycoproteins,
pubmed-meshheading:15544352-High-Density Lipoproteins, Pre-beta,
pubmed-meshheading:15544352-Humans,
pubmed-meshheading:15544352-Lipoproteins, HDL,
pubmed-meshheading:15544352-Membrane Proteins,
pubmed-meshheading:15544352-Models, Chemical,
pubmed-meshheading:15544352-Molecular Weight,
pubmed-meshheading:15544352-Phosphatidylcholine-Sterol O-Acyltransferase,
pubmed-meshheading:15544352-Phospholipid Transfer Proteins,
pubmed-meshheading:15544352-Protein Transport
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pubmed:year |
2004
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pubmed:articleTitle |
Molecular mechanism of reverse cholesterol transport: reaction of pre-beta-migrating high-density lipoprotein with plasma lecithin/cholesterol acyltransferase.
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pubmed:affiliation |
Cardiovascular Research Institute, University of California, San Francisco, California 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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