Acetyl-CoA carboxylase 1 regulates endothelial cell migration by shifting the phospholipid composition.
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Authors
Glatzel, Daniel KKoeberle, Andreas
Pein, Helmut
Löser, Konstantin
Stark, Anna
Keksel, Nelli
Werz, Oliver
Müller, Rolf

Bischoff, Iris
Fürst, Robert
Issue Date
2018-02
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Show full item recordAbstract
The enzyme acetyl-CoA carboxylase (ACC) plays a crucial role in fatty acid metabolism. In recent years, ACC has been recognized as a promising drug target for treating different diseases. However, the role of ACC in vascular endothelial cells (ECs) has been neglected so far. To characterize the role of ACC, we used the ACC inhibitor, soraphen A, as a chemical tool, and also a gene silencing approach. We found that ACC1 was the predominant isoform in human umbilical vein ECs as well as in human microvascular ECs and that soraphen A reduced the levels of malonyl-CoA. We revealed that ACC inhibition shifted the lipid composition of EC membranes. Accordingly, membrane fluidity, filopodia formation, and migratory capacity were reduced. The antimigratory action of soraphen A depended on an increase in the cellular proportion of PUFAs and, most importantly, on a decreased level of phosphatidylglycerol. Our study provides a causal link between ACC, membrane lipid composition, and cell migration in ECs. Soraphen A represents a useful chemical tool to investigate the role of fatty acid metabolism in ECs and ACC inhibition offers a new and valuable therapeutic perspective for the treatment of EC migration-related diseases.Citation
Acetyl-CoA carboxylase 1 regulates endothelial cell migration by shifting the phospholipid composition. 2018, 59 (2):298-311 J. Lipid Res.Affiliation
HIPS, Helmholtz-Institute für pharmazeutische Forschung Saarland, Universitätscampus E8.1, 66123 Saarbrücken, Germany.Journal
Journal of lipid researchPubMed ID
29208696Type
ArticleLanguage
enISSN
1539-7262ae974a485f413a2113503eed53cd6c53
10.1194/jlr.M080101
Scopus Count
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