FABPs, a family of 14-15 kDa proteins, act as chaperonins of FFA and bind with high affinity to hydrophobic ligands such as saturated and unsaturated long-chain fatty acids and eicosanoids. With the assistance of a variety of proteins, FABPs, such as FABP2, FABP3, FABP4 and FABP5 can transfer FFA to the target areas in order to regulate the oxidation power and further esterification of FFA. These target areas include the endoplasmic reticulum, mitochondria, peroxide multiplication enzyme and cell nucleus. Z-protein in rat liver was the first report ever to give the complete amino acid sequence of a fatty acid binding protein (FABP). So far 9 different FABPs, with tissue-specific distribution, have been identified: L (liver), I (intestinal), H (muscle and heart), A (adipocyte), E (epidermal), Il (ileal), B (brain), M (myelin) and T (testis). One group of the transcription factors cooperating with FABPs is the PPAR family. PPAR is a key transcription factor in preadipocyte differentiation. FABP also have an effect on ligand-dependent transactivation of PPARs, i.e. A-FABP and E-FABP selectively interact with PPAR and PPAR , respectively and L-FABP with PPAR and PPAR.


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