New insights into the fatty acid-binding protein (FABP) family in the small intestine

Abstract : The fatty acid-binding protein (FABP) superfamily is constituted by 14-15 kDa soluble proteins which bind with a high affinity either long-chain fatty acids (LCFAs), bile acids (BAs) or retinoids. In the small intestine, three different FABP isoforms exhibiting a high affinity for LCFAs and/or BAs are expressed: the intestinal and the liver-type (I-FABP and L-FABP) and the ileal bile acid-binding protein (I-BABP). Despite of extensive investigations, their respective physiological function(s) are not clearly established. In contrast to the I-FABP, L-FABP and I-BABP share several common structural features (shape, size and volume of the hydrophobic pocket). Moreover, L-FABP and I-BABP genes are also specifically regulated by their respective preferential ligands through a very similar molecular mechanism. Although, they exhibit differences in their binding specificities and location along the small intestine supporting a specialization, it is likely that L-FABP and I-BABP genes exert the same type of basic function(s) in the enterocyte, in contrast to I-FABP.
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Journal articles
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Submitted on : Friday, November 9, 2018 - 10:46:35 AM
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Philippe Besnard, Isabelle Niot, Hélène Poirier, Lionel Clémént, André Bernard. New insights into the fatty acid-binding protein (FABP) family in the small intestine. Molecular and Cellular Biochemistry, Springer Verlag, 2002, 239 (1-2), pp.139 - 147. ⟨10.1023/A:1020505512364⟩. ⟨hal-01917155⟩

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