Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids,
eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds
bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding
proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the
acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR
ligands may be regulated by lipid-binding proteins. In this report we show by transient …