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The Role of Fatty Acid Binding Proteins in Pain and Inflammation
Martin Kaczocha, PhD

  One of the primary goals of my laboratory is to understand the interplay between fatty acid binding proteins (FABPs) and bioactive lipids especially as it relates to pain and inflammation. FABPs constitute a family of small, widely expressed, intracellular lipid transport proteins that shuttle diverse lipids to their sites of signaling and catabolism. Recent work from our laboratory has demonstrated that FABPs regulate the transport of endocannabinoids and related N-acylethanolamines, lipids that activate cannabinoid receptors and nuclear PPARα receptors, respectively. Projects in the laboratory focus upon understanding the role of FABPs in endocannabinoid metabolism, regulation of pain and inflammation by endocannabinoid and non-endocannabinoid lipids, and the role of FABPs in diverse pathophysiological conditions.

 

As shown in the figure above, the endocannabinoid anandamide (AEA) is transported intracellularly by FABPs and is subsequently hydrolyzed by the enzyme fatty acid amide hydrolase (FAAH). The endocannabinoid 2-arachidonoylglycerol (2-AG) is hydrolyzed by monoacylglycerol lipase (MAGL). Inhibition of FABPs elevates AEA levels and potentiates AEA signaling at cannabinoid receptors. Palmitoylethanolamide (PEA) and oleoylethanolamide (OEA) activate nuclear PPARα receptors and are likewise transported by FABPs. The interplay between these proteins as it relates to endocannabinoid/N-acylethanolamine signaling is a primary focus of my laboratory.

 

 


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