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214Fat-specific protein 27 regulates storage of triacylglycerol.
Keller P; Petrie JT; De Rose P; Gerin I; Wright WS; Chiang SH; Nielsen AR; Fischer CP; Pedersen BK; Macdougald OA
J Biol Chem 2008; 294(2): E371-9
PubMed ID: 18334488

Fat-specific protein 27 (FSP27) is a member of the CIDE family. While Cidea and Cideb were initially characterized as activators of apoptosis, recent studies have demonstrated important metabolic roles for these proteins. In this study, we investigated the function of another member of this family, FSP27 (Cidec), in apoptosis and adipocyte metabolism. While overexpression of FSP27 is sufficient to increase apoptosis of 293T and 3T3-L1 cells, more physiological levels of expression stimulate spontaneous lipid accumulation in several cell types without induction of adipocyte genes. Increased triacylglycerol is likely due to decreased ss-oxidation of non-esterified fatty acids. Altered flux of fatty acids into triacylglycerol may be a direct effect of FSP27 function, which is localized to lipid droplets in 293T cells and 3T3-L1 adipocytes. Stable knockdown of FSP27 during adipogenesis of 3T3-L1 cells substantially decreases lipid droplet size, increases mitochondrial and lipid droplet number, and modestly increases glucose uptake and lipolysis. Expression of FSP27 in subcutaneous adipose tissue of a human diabetes cohort decreases with total fat mass, but is not associated with measures of insulin resistance (e.g. HOMA). Together, these data indicate that FSP27 binds to lipid droplets and regulates their enlargement.

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