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Papers In Press, published online ahead of print February 17, 2006
J. Lipid Res., doi:10.1194/jlr.M500459-JLR200
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Department of Nutrition, Institute of Basic Medical Science, Faculty of Medicine, University of Oslo, Oslo 0316
Corresponding Author: knutd{at}medisin.uio.no
The adipose differentiation-related protein (ADFP)/adipophilin belongs to a family of PAT (perilipin, ADFP, TIP47) proteins that associate on the surface of lipid droplets. Except for lipid droplet association, a clear role for ADFP has not been found. We demonstrate that ADFP is transcriptionally regulated by PPAR
Revised on January 27, 2006
Accepted on February 17, 2006
PPAR
activators and fasting induce the expression of adipose differentiation-related protein in liver
in mouse liver and rat and human hepatoma cells through a highly conserved DR-1 element. Although the ADFP mRNA is highly increased by a synthetic PPAR agonist, the ADFP protein is only substantially increased in cells containing lipid droplets, such as hepatocytes incubated with fatty acids and in livers of fasted mice. ADFP is induced by fasting even in the absence of a functional PPAR, in marked contrast to the PPAR target gene ACO-1. Activation of LXRs, which stimulates lipid droplet formation through activation of lipogenesis, does not affect ADFP mRNA levels. TIP47, another PAT member known to be expressed in liver, was unaffected by all treatments. This constitutively expressed PAT member seems to be less transcriptionally regulated than ADFP. These observations suggest that ADFP is primarily a fasting induced protein in liver that coats the newly synthesized triacylglycerol containing lipid droplets formed during fasting.
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