rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2004-5-18
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pubmed:abstractText |
Here, we identify ADP-ribosylation factor (ARF)-like 7 (ARL7) as the only ARF- and ARL-family member whose mRNA-expression is induced by liver X-receptor/retinoid X-receptor agonists or cholesterol loading in human macrophages. Moreover, subcellular distribution of mutant and wild type ARL7-enhanced green fluorescent protein (EGFP) supports that ARL7 may be involved in a vesicular transport step between a perinuclear compartment and the plasma membrane. Therefore, we investigated the effect of ARL7 over-expression on the cholesterol secretory pathway. We found that expression of wild type and dominant active ARL7-EGFP stimulated the rate of apolipoprotein AI-specific cholesterol efflux 1.7- and 2.8-fold. In contrast, expression of the dominant negative form of ARL7-EGFP led to approximately 50% inhibition of cholesterol efflux. This data is consistent with a model in which ARL7 is involved in transport between a perinuclear compartment and the plasma membrane apparently linked to the ABCA1-mediated cholesterol secretion pathway.
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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/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
pubmed-author:AssmannGerdG,
pubmed-author:BodeGüntherG,
pubmed-author:CullenPaulP,
pubmed-author:EngelThomasT,
pubmed-author:HobohmUweU,
pubmed-author:LorkowskiStefanS,
pubmed-author:LuekenAloysA,
pubmed-author:PechMichaelM,
pubmed-author:RustStephanS,
pubmed-author:SchlueterBernhardB,
pubmed-author:SeedorfUdoU
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
566
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
241-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15147902-ADP-Ribosylation Factors,
pubmed-meshheading:15147902-Apolipoprotein A-I,
pubmed-meshheading:15147902-Biological Transport,
pubmed-meshheading:15147902-Cholesterol,
pubmed-meshheading:15147902-Gene Expression,
pubmed-meshheading:15147902-Green Fluorescent Proteins,
pubmed-meshheading:15147902-HeLa Cells,
pubmed-meshheading:15147902-Humans,
pubmed-meshheading:15147902-Luminescent Proteins,
pubmed-meshheading:15147902-Macrophages,
pubmed-meshheading:15147902-Monocytes,
pubmed-meshheading:15147902-RNA, Messenger,
pubmed-meshheading:15147902-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:15147902-Receptors, Retinoic Acid,
pubmed-meshheading:15147902-Recombinant Fusion Proteins,
pubmed-meshheading:15147902-Subcellular Fractions,
pubmed-meshheading:15147902-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
ADP-ribosylation factor (ARF)-like 7 (ARL7) is induced by cholesterol loading and participates in apolipoprotein AI-dependent cholesterol export.
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pubmed:affiliation |
Institut für Arterioskleroseforschung, Westfälische Wilhelms-Universität, Domagkstr. 3, D-48149 Münster, Germany. engeltho@uni-muenster.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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