Linked Life Data

15994327

Source:http://linkedlifedata.com/resource/pubmed/id/15994327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2005-8-22
pubmed:abstractText
ATP binding cassette transporter G1 (ABCG1) mediates the transport of cholesterol from cells to high density lipoprotein (HDL) but not to lipid-depleted apolipoprotein A-I. Here we show that human ABCG1 overexpressed in baby hamster kidney cells in the absence of lipoproteins traffics to the plasma membrane and redistributes membrane cholesterol to cell-surface domains accessible to treatment with the enzyme cholesterol oxidase. Cholesterol removed by HDL was largely derived from these domains in ABCG1 transfectants but not in cells lacking ABCG1. Overexpression of ABCG1 also increased cholesterol esterification, which was decreased by the addition of HDL, suggesting that a proportion of the cell-surface cholesterol not removed by HDL is transported to the intracellular esterifying enzyme acyl-CoA:cholesterol acyltransferase. A 638-amino acid ABCG1, which lacked the 40 N-terminal amino acids of the predicted full-length protein, was fully functional and of a similar size to ABCG1 expressed by cholesterol-loaded human monocyte-derived macrophages. Mutating an essential glycine residue in the Walker A motif abolished ABCG1-dependent cholesterol efflux and esterification and prevented localization of ABCG1 to the cell surface, indicating that the ATP binding domain in ABCG1 is essential for both lipid transport activity and protein trafficking. These studies show that ABCG1 redistributes cholesterol to cell-surface domains where it becomes accessible for removal by HDL, consistent with a direct role of ABCG1 in cellular cholesterol transport.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30150-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15994327-ATP-Binding Cassette Transporters, pubmed-meshheading:15994327-Amino Acid Motifs, pubmed-meshheading:15994327-Animals, pubmed-meshheading:15994327-Apolipoprotein A-I, pubmed-meshheading:15994327-Apolipoproteins, pubmed-meshheading:15994327-Biological Transport, pubmed-meshheading:15994327-Cell Membrane, pubmed-meshheading:15994327-Cholesterol, pubmed-meshheading:15994327-Cricetinae, pubmed-meshheading:15994327-Cross-Linking Reagents, pubmed-meshheading:15994327-DNA, Complementary, pubmed-meshheading:15994327-Dose-Response Relationship, Drug, pubmed-meshheading:15994327-Glycine, pubmed-meshheading:15994327-Humans, pubmed-meshheading:15994327-Immunoblotting, pubmed-meshheading:15994327-Kidney, pubmed-meshheading:15994327-Lipid Metabolism, pubmed-meshheading:15994327-Lipoproteins, HDL, pubmed-meshheading:15994327-Macrophages, pubmed-meshheading:15994327-Mifepristone, pubmed-meshheading:15994327-Monocytes, pubmed-meshheading:15994327-Mutation, pubmed-meshheading:15994327-Protein Structure, Tertiary, pubmed-meshheading:15994327-Sterol O-Acyltransferase, pubmed-meshheading:15994327-Time Factors, pubmed-meshheading:15994327-Transfection
pubmed:year
2005
pubmed:articleTitle
ABCG1 redistributes cell cholesterol to domains removable by high density lipoprotein but not by lipid-depleted apolipoproteins.
pubmed:affiliation
Department of Medicine, Division of Metabolism, Endocrinology and Nutrition, University of Washington, Seattle, Washington 98195-6426, USA. smashie@u.washington.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural