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

J Appl Genet. 2006;47(1):39-48. doi: 10.1007/BF03194597.


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 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biological Transport
  • Body Weight / genetics*
  • Fatty Acid-Binding Proteins* / chemistry
  • Fatty Acid-Binding Proteins* / genetics
  • Fatty Acid-Binding Proteins* / physiology
  • Fatty Acids / metabolism
  • Humans
  • Multigene Family*
  • Polymorphism, Genetic*
  • Tissue Distribution


  • Fatty Acid-Binding Proteins
  • Fatty Acids