Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-1-15
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
1047
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-8
pubmed:dateRevised
2008-11-21
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
pubmed:year
1990
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.
pubmed:affiliation
Lawrence Berkeley Laboratory, University of California 94702.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.