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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1991-1-15
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pubmed:abstractText |
Chinese hamster ovary cells transfected with the human apolipoprotein A-I gene linked to the human metallothionein gene promoter region secrete large quantities of apolipoprotein A-I (7.1 +/- 0.4% total secreted protein) in the presence of zinc. Approx. 16% of the secreted apolipoprotein A-I is complexed with lipid and can be isolated ultracentrifugally at d less than or equal to 1.21 g/ml. The latter complexes are composed of discs and vesicles as judged by electron microscopy and can be further separated by column chromatography into three fractions: fraction I, mostly vesicles (60-260 nm) and large discs (18-20 nm diameter); fraction II, discs 14.2 +/- 2.6 nm diameter; and fraction III, nonresolvable by electron microscopy. The latter fraction is extremely lipid-poor (94% protein, 6% phospholipid); in contrast, the protein, phospholipid and unesterified cholesterol content for the other fractions are 43, 33 and 24%, respectively, for fraction I and 53, 33 and 14%, respectively, for fraction II. Fraction II particles contain three and four apolipoprotein A-Is per particle as determined by protein crosslinking while large structures in fraction I contain primarily six to seven apolipoprotein A-Is per particle. Following incubation with purified lecithin: cholesterol acyltransferase, discoidal particles were transformed into apparent spherical particles 12.9 +/- 3.4 nm diameter; this transformation coincided with 19-21% conversion of unesterified cholesterol to esterified cholesterol. The apolipoprotein A-I-lipid complexes isolated from Chinese hamster ovary cell media are similar to nascent HDL found in plasma of lecithin:cholesterol acyltransferase-deficient patients and those secreted by the human hepatoma line, Hep G2. The ability of the Chinese hamster ovary cell nascent HDL-like particles to undergo transformation in the presence of purified lecithin:cholesterol acyltransferase indicates that they are functional particles.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
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/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Metallothionein,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholine-Sterol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
1047
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2123400-Animals,
pubmed-meshheading:2123400-Apolipoprotein A-I,
pubmed-meshheading:2123400-Apolipoproteins A,
pubmed-meshheading:2123400-Cell Line,
pubmed-meshheading:2123400-Cholesterol,
pubmed-meshheading:2123400-Chromatography,
pubmed-meshheading:2123400-Cricetinae,
pubmed-meshheading:2123400-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2123400-Female,
pubmed-meshheading:2123400-Humans,
pubmed-meshheading:2123400-Lipid Metabolism,
pubmed-meshheading:2123400-Lipids,
pubmed-meshheading:2123400-Macromolecular Substances,
pubmed-meshheading:2123400-Metallothionein,
pubmed-meshheading:2123400-Microscopy, Electron,
pubmed-meshheading:2123400-Ovary,
pubmed-meshheading:2123400-Phosphatidylcholine-Sterol O-Acyltransferase,
pubmed-meshheading:2123400-Phospholipids,
pubmed-meshheading:2123400-Promoter Regions, Genetic,
pubmed-meshheading:2123400-Proteins,
pubmed-meshheading:2123400-Transfection,
pubmed-meshheading:2123400-Ultracentrifugation
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pubmed:year |
1990
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pubmed:articleTitle |
Physical and chemical characteristics of apolipoprotein A-I-lipid complexes produced by Chinese hamster ovary cells transfected with the human apolipoprotein A-I gene.
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pubmed:affiliation |
Lawrence Berkeley Laboratory, University of California 94702.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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