Fatty acid ethyl esters (FAEEs), nonoxidative by-products of ethanol metabolism, are found in various tissues and plasma after ethanol ingestion and may be responsible for some of the pathological changes observed in alcohol-consuming individuals. Previous studies demonstrated that several different enzymes, including lipoprotein lipase (LPL), can catalyze FAEE synthesis in vitro. We report that LPL catalyzes FAEE synthesis in isolated rat hearts perfused with chylomicrons in the presence of ethanol. Most of the FAEEs accumulated in the perfusate, suggesting that in vivo, plasma FAEEs derive from LPL-mediated synthesis. Our results are the first demonstration of the direct involvement of a specific enzyme, LPL, in FAEE synthesis under physiological conditions.
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Article Synopsis
- Ferulic acid ethyl ester (FAEE) is key for developing drugs for heart and blood vessel diseases, as well as for food flavoring due to its strong pharmacological properties.
- This study examined how FAEE interacts with human proteins, specifically Human serum albumin (HSA) and Lysozyme (LZM), using various testing methods at different temperatures, and looked into how metal ions affect these interactions.
- The findings suggest that FAEE changes the environment and structure of these proteins, offering insights that could enhance its use in cosmetics, food safety, and pharmaceutical applications.
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