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Food additive may one day help control blood lipids and reduce disease risk
Date:7/30/2009

could perform that task. Reporting in the Aug. 7 issue of the journal Cell, the Washington University research team describes how it found the link between lecithin and PPAR-alpha.

They first created a strain of mice that could not make fatty acid synthase in the liver. When humans or animals eat, we take in sugars. Fatty acid synthase converts those sugars to fatty acids in the liver, where they play important roles in energy metabolism.

"To our surprise, animals missing fatty acid synthase in the liver were just like animals that couldn't make PPAR-alpha. They had lower fasting insulin levels, and they were prone to develop fatty liver disease," says senior investigator Clay F. Semenkovich, M.D., the Herbert S. Gasser Professor and chief of the Division of Endocrinology, Metabolism and Lipid Research. "When we gave the animals fibrate drugs that activated PPAR-alpha, the mice returned to normal, leading us to suspect that fatty acid synthase also was involved in the activation of PPAR-alpha. Although we knew that fibrate drugs would regulate PPAR-alpha, we also knew that our ability to regulate the metabolism of fats and sugars was in place long before humans started making drugs. But until now, no one had identified how it worked."

Semenkovich, Lodhi, John Turk, M.D. Ph.D., professor of medicine and of pathology, and the rest of the team used mass spectrometry and gene expression studies to isolate the phosphatidylcholine, or lecithin compound, that activated PPAR-alpha in the liver.

One reason fatty acid synthase had never been connected to PPAR-alpha function was the distance of the two proteins from each other, according to Semenkovich. PPAR-alpha is a nuclear receptor. That is, it's housed in the nucleus of the cell. Fatty acid synthase, on the other hand, lives out in the cell body, or cytoplasm.

"The neighborhoods where PPAR-alpha and fatty acid synthase live aren't very close together," says Semenkovich. "The synthase is wa
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Contact: Jim Dryden
jdryden@wustl.edu
314-286-0110
Washington University School of Medicine
Source:Eurekalert

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