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lüll The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism Chmurzynska AJ Appl Genet 2006[]; 47 (1): 39-48Fatty acid-binding proteins (FABPs) are members of the superfamily of lipid-binding proteins (LBP). 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). The primary role of all the FABP family members is regulation of fatty acid uptake and intracellular transport. The structure of all FABPs is similar - the basic motif characterizing these proteins is beta-barrel, and a single ligand (e.g. a fatty acid, cholesterol, or retinoid) is bound in its internal water-filled cavity. Despite the wide variance in the protein sequence, the gene structure is identical. The FABP genes consist of 4 exons and 3 introns and a few of them are located in the same chromosomal region. For example, A-FABP, E-FABP and M-FABP create a gene cluster. Because of their physiological properties some FABP genes were tested in order to identify mutations altering lipid metabolism. Furthermore, the porcine A-FABP and H-FABP were studied as candidate genes with major effect on fatness traits.|*Fatty Acid-Binding Proteins/chemistry/genetics/physiology[MESH]|*Multigene Family[MESH]|*Polymorphism, Genetic[MESH]|Animals[MESH]|Biological Transport[MESH]|Body Weight/*genetics[MESH]|Fatty Acids/metabolism[MESH]|Humans[MESH]|Tissue Distribution[MESH] |