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ADP‐ribosylation factor (ARF)‐like 7 (ARL7) is induced by cholesterol loading and participates in apolipoprotein AI‐dependent cholesterol export
Author(s) -
Engel Thomas,
Lueken Aloys,
Bode Günther,
Hobohm Uwe,
Lorkowski Stefan,
Schlueter Bernhard,
Rust Stephan,
Cullen Paul,
Pech Michael,
Assmann Gerd,
Seedorf Udo
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.048
Subject(s) - cholesterol , adp ribosylation factor , apolipoprotein b , secretion , efflux , abca1 , liver x receptor , microbiology and biotechnology , reverse cholesterol transport , biology , mutant , wild type , receptor , chemistry , biochemistry , transcription factor , lipoprotein , golgi apparatus , transporter , nuclear receptor , gene , endoplasmic reticulum
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 ∼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.