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The multigene family of fatty acid-binding proteins (FABPs): Function, structure and polymorphism

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Abstract

Fatty 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 β-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 andM-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 porcineA-FABP andH-FABP were studied as candidate genes with major effect on fatness traits.

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  1. Department of Animal Genetics and Breeding, August Cieszkowski Agricultural University of Poznań, Wołyńska 33, 60-637, Poznań, Poland

    Agata Chmurzyńska

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Chmurzyńska, A. The multigene family of fatty acid-binding proteins (FABPs): Function, structure and polymorphism. J Appl Genet 47, 39–48 (2006). https://doi.org/10.1007/BF03194597

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