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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Mangroo D, Trigatti BL, Gerber GE: Membrane permeation and intracellular trafficking of long-chain fatty acids: Insights from Escherichia coli and 3T3-L1 adipocytes. Biochem Cell Biol 73: 223–234, 1995
Berk PD: How do long-chain free fatty acids cross cell membrane? Proc Soc Exp Biol Med 212: 1–4, 1996
Fitscher BA, Elsing C, Riedel HD, Gorski J, Stremmel W: Protein-mediated facilitated uptake processes for fatty acids, bilirubin, and other amphipathic compounds. Proc Soc Exp Biol Med 212: 15–23, 1996
Zakim D: Fatty acids enter cells by simple diffusion. Proc Soc Exp Biol Med 212: 5–14, 1996
Glatz JFC, Luiken JJFP, van Nieuwenhoven FA, van der Vusse GJ: Molecular mechanism of cellular uptake and intracellular translocation of fatty acids. Prost Leuk Essent Fatty Acids 57: 3–9, 1997
Abumrad N, Harmon C, Ibrahimi A: Membrane transport of longchain fatty acids: Evidence for a facilated process. J Lipid Res 39: 2309–2318, 1998
Hamilton JA: Fatty acid transport: Difficult or easy? J Lipid Res 39: 467–481, 1998
McArthur MJ, Atshaves BP, Frolov A, Foxworth WD, Kier AB, Schroeder F: Cellular uptake and intracellular trafficking of longchain fatty acids. J Lipid Res 40: 1371–1383, 1999
Besnard P, Niot I: Role of lipid-binding proteins in intestinal absorption of long-chain fatty acid. In: A.B. Christophe, S. De Vriese (eds). Fat Digestion and Absorption. AOCS Press, Champaign, IL, USA, 2000, pp 96–118
Kramer W, Girbig F, Gutjahr U, Kowalewski S, Jouvenal K, Müller G, Tripier D, Wess G: Intestinal bile acid absorption. Na+-dependent bile acid transport activity in rabbit small intestine correlates with the coexpression of an integral 93-kDa and a peripheral 14-kDa bile acid-binding membrane protein along the duodenum-ileum axis. J Biol Chem 268: 18035–18046, 1993
Veerkamp JH, Maatman RGHJ: Cytoplasmic fatty acid-binding proteins: Their structures and genes. Prog Lipids Res 34: 17–52, 1995
Inokuchi A, Hinoshita E, Iwamoto Y, Kohno K, Kuwano M, Uchiumi T: Enhanced expression of the human multidrug resistance protein 3 by bile salt in human enterocytes: A transcriptional control of a plausible bile acid transporter. J Biol Chem 4: 4, 2001
Weinberg SL, Burckhardt G, Wilson FA: Taurocholate transport by rat intestinal basolateral membrane vesicles. J Clin Invest 78: 44–50, 1996
Abe T, Kakyo M, Sakagami H, Tokui T, Nishio T, Tanemoto M, Nomura H, Hebert SC, Matsuno S, Kondo H, Yawo H: Molecular characterization and tissue distribution of a new organic anion transporter subtype (oatp3) that transports thyroid hormones and taurocholate and comparison with oatp2. J Biol Chem 273: 22395–22401, 1998
Russell DW, Setchell KD: Bile acid biosynthesis. Biochemistry 31: 4737–4749, 1992
Poirier H, Niot I, Degrace P, Monnot MC, Bernard A, Besnard P: Fatty acid regulation of fatty acid-binding proteins expression in the small intestine. Am J Physiol 273: G289–G295, 1997
Richieri GV, Ogata RT, Kleinfeld AM: Kinetics of fatty acid interactions with fatty acid-binding proteins from adipocyte, heart and intestine. J Biol Chem 271: 11291–11300, 1996
Sacchettini JC, Scapin G, Gopaul D, Gordon JI: Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75 A resolution. J Biol Chem 267: 23534–23545, 1992
Fujita M, Fujii H, Kanda T, Sato E, Hatakeyama K, Ono T: Molecular cloning, expression, and characterization of a human intestinal 15-kDa protein. Eur J Biochem 233: 406–413, 1995
Lücke C, Zhang F, Rüterjans H, Hamilton JA, Sacchettini JC: Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Structure 4: 785–800, 1996
Kramer W, Corsiero D, Friedrich M, Girbig F, Stengelin S, Weyland C: Intestinal absorption of bile acids: Paradoxical behaviour of the 14 kDa ileal lipid-binding protein in differential photoaffinity labelling. Biochem J 333: 335–341, 1998
Sacchettini JC, Gordon JI: Rat intestinal fatty acid-binding protein. A model system for analyzing the forces that can bind fatty acids to proteins. J Biol Chem 268: 18399–18402, 1993
Thompson J, Ory J, Reese-Wagoner A, Banaszak L: The liver fatty acid-binding protein: Comparison of cavity properties of intracellular lipid-binding proteins. Mol Cell Biochem 192: 9–16, 1999
Lücke C, Fushman D, Ludwig C, Hamilton JA, Sacchettini JC, Rüterjans HA: Comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Mol Cell Biochem 192: 109–121, 1999
Lücke C, Zhang F, Hamilton JA, Sacchettini JC, Ruterjans H: Solution structure of ileal lipid binding protein in complex with glycocholate. Eur J Biochem 267: 2929–2938, 2000
Thompson J, Winter N, Terwey D, Bratt J, Banaszak L: The crystal structure of the liver fatty acid-binding protein. J Biol Chem 272: 7140–7150, 1997
Santomé JA, Di Pietro SM, Cavagnari BM, Cordoba OL, Dell’ Angelica EC: Fatty acid-binding proteins. Chronological description and discussion of hypotheses involving their molecular evolution. Trends Comp Biochem Physiol 4: 23–38, 1998
Poirier H, Niot I, Monnot MC, Braissant O, Meunier-Durmort C, Costet P, Pineau T, Wahli W, Willson TM, Besnard P: Differential involvement of peroxisome-proliferator-activated receptors alpha and delta in fibrate and fatty-acid-mediated inductions of the gene encoding liver fatty-acid-binding protein in the liver and the small intestine. Biochem J 355: 481–488, 2001
Poirier H, Braissant O, Niot I, Wahli W, Besnard P: 9-cis-retinoic acid enhances fatty acid-induced expression of the liver fatty acidbinding protein gene. FEBS Lett 412: 480–484, 1997
Grober J, Zaghini I, Fujii H, Jones SA, Kliewer SA, Willson TM, Ono T, Besnard P: Identification of a bile acid-responsive element in the human ileal bile acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis-retinoic acid receptor heterodimer J Biol Chem 274: 29749–29754, 1999
Hallden G, Holehouse EL, Dong X, Aponte GW: Expression of intestinal fatty acid-binding protein in intestinal epithelial cell lines, hBRIE 380 cells. Am J Physiol 267: G730–G743, 1994
Le Beyec J, Delers F, Jourdant F, Schreider C, Chambaz J, Cardot P, Pinçon-Raymond MA: Complete epithelial organization of Caco-2 cells induces I-FABP and potentializes apolipoprotein gene expression. Exp Cell Res 236: 311–320, 1997
Hallden G, Aponte GW: Evidence for a role of the gut hormone PYY in the regulation of intestinal fatty acid-binding protein transcripts in differentiated subpopulations of intestinal epithelial cell hybrids. J Biol Chem 272: 12591–12600, 1997
Aponte GW, Park K, Hess R, Garcia R, Taylor IL: Meal-induced peptide tyrosine tyrosine inhibition of pancreatic secretion in the rat. Faseb J 3: 1949–1955, 1989
Laburthe M, Chenut B, Rouyer-Fessard C, Tatemoto K, Couvineau A, Servin A, Amiranoff B: Interaction of peptide YY with rat intestinal epithelial plasma membranes: Binding of the radioiodinated peptide. Endocrinology 118: 1910–1917, 1986
Bass NM: The cellular fatty acid-binding proteins: Aspects of structure, regulation, and function. Int Rev Cytol 111: 143–184, 1988
Darimont C, Gradoux N, De Pover A: Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. Am J Physiol 276: G606–G612, 1999
Baier LJ, Sacchettini JC, Knowler WC, Eads J, Paolisso G, Tataranni PA, Mochizuki H, Bennett PH, Bogardus C, Prochazka M: An amino acid substitution in the human intestinal fatty acid-binding protein is associated with increased fatty acid binding, increased fat oxidation, and insulin resistance. J Clin Invest 95: 1281–1287, 1995
Hegele RA, Harris SB, Hanley AJG, Sadikian S, Connelly PW, Zinman B: Genetic variation of intestinal fatty acid-binding protein associated with variation in body mass in aboriginal canadians. J Clin Endocrinol Metab 81: 4334–4337, 1996
Baier LJ, Bogardus C, Sacchettini JC: A polymorphism in the human intestinal fatty acid-binding protein alters fatty acid transport across Caco-2 cells. J Biol Chem 271: 10892–10896, 1996
Levy E, Menard D, Delvin E, Stan S, Mitchell G, Lambert M, Ziv E, Feoli-Fonseca JC, Seidman E: The polymorphism at codon 54 of the FABP2 gene increases fat absorption in human intestinal explants. J Biol Chem 276: 39679–39684, 2001
Prows DR, Schroeder F: Metallothionein-IIA promoter induction alters rat intestinal fatty acid-binding protein expression, fatty acid uptake, and lipid metabolism in transfected L-cells. Arch Biochem Biophys 340: 135–143, 1997
Atshaves BP, Foxworth WB, Frolov A, Roths JB, Kier AB, Oetama BK, Piedrahita JA, Schroeder F: Cellular differentiation and I-FABP protein expression modulate fatty acid uptake and diffusion. Am J Physiol 274: C633–C644, 1998
Holehouse E, Liu M-L, Aponte GW: Oleic acid distribution in small intestinal epithelial cells expressing intestinal-fatty acid binding protein. Biochim Biophys Acta 1390: 52–64, 1998
Wolfrum C, Buhlmann C, Rolf B, Börchers T, Spener F: Variation of liver-type fatty acid-binding protein content in the human hepatoma cell line HepG2 by peroxisome proliferators and antisense RNA affects the rate of fatty acid uptake. Biochim Biophys Acta 1437: 194–201, 1999
Hsu K-T, Storch J: Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J Biol Chem 271: 13317–13323, 1996
Corsico B, Cistola DP, Frieden C, Storch J: The helical domain of intestinal fatty acid-binding protein is critical for collisional transfer of fatty acid to phospholipid membranes. Proc Natl Acad Sci USA 95: 12174–12178, 1998
Hodsdon ME, Cistola DP: Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acidbinding protein: Implications for the mechanism of ligand entry. Biochemistry 36: 1450–1460, 1997
Alpers DH, Bass NM, Engle MJ, DeSchryver-Kecskemeti K: Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine. Biochim Biophys Acta 1483: 352–362, 2000
Vassileva G, Huwyler L, Poirier K, Agellon LB, Toth MJ: The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice. Faseb J 14: 2040–2046, 2000
Wolfrum C, Borrmann CM, Borchers T, Spener F: Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors alpha-and gamma-mediated gene expression via liver fatty acid binding protein: A signaling path to the nucleus. Proc Natl Acad Sci USA 98: 2323–2328, 2001
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Besnard, P., Niot, I., Poirier, H. et al. New insights into the fatty acid-binding protein (FABP) family in the small intestine. Mol Cell Biochem 239, 139–147 (2002). https://doi.org/10.1023/A:1020505512364
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DOI: https://doi.org/10.1023/A:1020505512364