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A more recent version of this article appeared on May 1, 2005

Papers In Press, published online ahead of print February 16, 2005
J. Lipid Res., doi:10.1194/jlr.M400476-JLR200
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Submitted on December 3, 2004
Revised on February 16, 2005
Accepted on February 3, 2005

Trans-10, cis-12 CLA increases adipocyte lipolysis and alters lipid droplet-associated proteins: Role of mTOR and ERK signaling

Soonkyu Chung, Jonathan Mark Brown, Maria Sandberg Boysen, and Michael McIntosh

Nutrition, University of North Carolina at Greensboro, Greensboro, NC 27402-6170

Corresponding Author: mkmcinto{at}uncg.edu

Lipid droplet-associated proteins play an important role in adipocyte triglyceride (TG) metabolism. Here, we show that trans-10, cis-12 conjugated linoleic acid (CLA), but not cis-9, trans-11 CLA, increased lipolysis and altered human adipocyte lipid droplet morphology. Prior to this change in morphology, there was a rapid trans-10, cis-12 CLA-induced increase in the accumulation of perilipin A in the cytosol, followed by the disappearance of perilipin A protein. In contrast, protein levels of adipose differentiation-related protein (ADRP) were elevated in cultures treated with trans-10, cis-12 CLA. Immunostaining revealed that ADRP localized to the surface of small lipid droplets, displacing perilipin. Intriguingly, trans-10, cis-12 CLA increased ADRP protein expression to a much greater extent than ADRP mRNA without affecting stability, suggesting translational control of ADRP. To this end, we found that trans-10, cis-12 CLA increased activation of the mammalian target of rapamycin/p70S6 kinase/S6 ribosomal (mTOR/p70S6K/S6) pathway. Collectively, these data demonstrate that the trans-10, cis-12 CLA-mediated reduction of human adipocyte TG content is associated with differential localization and expression of lipid droplet-associated proteins. This process involves both the translational control of ADRP through activation of mTOR/p70S6K/S6 signaling and transcriptional control of perilipin A.


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