Intestinal fatty acid binding protein regulates mitochondrion β-oxidation and cholesterol uptake

The role of intestinal fatty acid binding protein (I-FABP) in lipid metabolism remains elusive. To address this issue, normal human intestinal epithelial cells (HIEC-6) were transfected with cDNA to overexpress I-FABP and compared with cells treated with empty pQCXIP vector. I-FABP overexpression stimulated mitochondrial [U-14C]oleate oxidation to CO2 and acid-soluble metabolites via mechanisms including the upregulation of protein expression and the activity of carnitine palmitoyltransferase 1, a critical enzyme controlling the entry of fatty acid (FA) into mitochondria, and increased activity of 3-hydroxyacyl-CoA dehydrogenase, a mitochondrial β-oxidation enzyme. On the other hand, the gene and protein expression of the key enzymes FA synthase and acetyl-coenzyme A carboxylase 2 was decreased, suggesting diminished lipogenesis. Furthermore, I-FABP overexpression caused a decline in [14C]free cholesterol (CHOL) incorporation. Accordingly, a significant lessening was observed in the gene expression of Niemann Pick C1-Like 1, a mediator of CHOL uptake, along with an increase in the transcripts and protein content of ABCA1 and ABCG5/ABCG8, acting as CHOL efflux pumps. Furthermore, I-FABP overexpression resulted in increased levels of mRNA, protein mass, and activity of HMG-CoA reductase, the rate-limiting step in CHOL synthesis. Scrutiny of the nuclear receptors revealed augmented peroxisome proliferator-activated receptor α,γ and reduced liver X receptor-α in HIEC-6 overexpressing I-FABP. Finally, I-FABP overexpression did not influence acyl-coenzyme A oxidase 1, which catalyzes the first rate-limiting step in peroxisomal FA β-oxidation. Overall, our data suggest that I-FABP may influence mitochondrial FA oxidation and CHOL transport by regulating gene expression and interaction with nuclear receptors. The role of intestinal fatty acid binding protein (I-FABP) in lipid metabolism remains elusive. To address this issue, normal human intestinal epithelial cells (HIEC-6) were transfected with cDNA to overexpress I-FABP and compared with cells treated with empty pQCXIP vector. I-FABP overexpression stimulated mitochondrial [U-14C]oleate oxidation to CO2 and acid-soluble metabolites via mechanisms including the upregulation of protein expression and the activity of carnitine palmitoyltransferase 1, a critical enzyme controlling the entry of fatty acid (FA) into mitochondria, and increased activity of 3-hydroxyacyl-CoA dehydrogenase, a mitochondrial β-oxidation enzyme. On the other hand, the gene and protein expression of the key enzymes FA synthase and acetyl-coenzyme A carboxylase 2 was decreased, suggesting diminished lipogenesis. Furthermore, I-FABP overexpression caused a decline in [14C]free cholesterol (CHOL) incorporation. Accordingly, a significant lessening was observed in the gene expression of Niemann Pick C1-Like 1, a mediator of CHOL uptake, along with an increase in the transcripts and protein content of ABCA1 and ABCG5/ABCG8, acting as CHOL efflux pumps. Furthermore, I-FABP overexpression resulted in increased levels of mRNA, protein mass, and activity of HMG-CoA reductase, the rate-limiting step in CHOL synthesis. Scrutiny of the nuclear receptors revealed augmented peroxisome proliferator-activated receptor α,γ and reduced liver X receptor-α in HIEC-6 overexpressing I-FABP. Finally, I-FABP overexpression did not influence acyl-coenzyme A oxidase 1, which catalyzes the first rate-limiting step in peroxisomal FA β-oxidation. Overall, our data suggest that I-FABP may influence mitochondrial FA oxidation and CHOL transport by regulating gene expression and interaction with nuclear receptors. Fatty acid binding proteins (FABPs) display a high affinity for long-chain fatty acids (LCFA) and appear to function in the metabolism and intracellular transport of lipids (1.Agellon L.B. Toth M.J. Thomson A.B. Intracellular lipid binding proteins of the small intestine.Mol. Cell. Biochem. 2002; 239: 79-82Crossref PubMed Scopus (72) Google Scholar). Two distinct FABPs are expressed in the small intestine: the liver (L)-FABP encoded by the FABP1 gene and the intestinal (I)-FABP encoded by the FABP2 gene (2.Gordon J.I. Elshourbagy N. Lowe J.B. Liao W.S. Alpers D.H. Taylor J.M. Tissue specific expression and developmental regulation of two genes coding for rat fatty acid binding proteins.J. Biol. Chem. 1985; 260: 1995-1998Abstract Full Text PDF PubMed Google Scholar). The function of these proteins is still under investigation. The presence of two structurally distinct, independently regulated FABPs in the intestine has led to the speculation that these proteins assume unique roles in intestinal fatty acid (FA) metabolism (2.Gordon J.I. Elshourbagy N. Lowe J.B. Liao W.S. Alpers D.H. Taylor J.M. Tissue specific expression and developmental regulation of two genes coding for rat fatty acid binding proteins.J. Biol. Chem. 1985; 260: 1995-1998Abstract Full Text PDF PubMed Google Scholar, 3.Bass N.M. Manning J.A. Ockner R.K. Gordon J.I. Seetharam S. Alpers D.H. Regulation of the biosynthesis of two distinct fatty acid-binding proteins in rat liver and intestine. Influences of sex difference and of clofibrate.J. Biol. Chem. 1985; 260: 1432-1436Abstract Full Text PDF PubMed Google Scholar). Because targeted gene disruption studies may shed light on the physiological importance of these proteins, Vassileva et al. (4.Vassileva G. Huwyler L. Poirier K. Agellon L.B. Toth M.J. The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice.FASEB J. 2000; 14: 2040-2046Crossref PubMed Scopus (151) Google Scholar) invalidated mouse FABP2 and studied the impact on intestinal lipid transport. The results of their experiments suggest that I-FABP knockout does not produce a detrimental effect on dietary fat absorption but may cause weight gain and hyperinsulinemia. Additionally, our observations using normal human intestinal epithelial cells (HIEC-6) overexpressing sizeable amounts of I-FABP demonstrated a negligible influence of this transporter on lipid synthesis, apolipoprotein biogenesis, and lipoprotein exocytosis (5.Montoudis A. Delvin E. Menard D. Beaulieu J.F. Jean D. Tremblay E. Bendayan M. Levy E. Intestinal-fatty acid binding protein and lipid transport in human intestinal epithelial cells.Biochem. Biophys. Res. Commun. 2006; 339: 248-254Crossref PubMed Scopus (19) Google Scholar). Conversely, examination of the human intestinal cell line Caco-2 overexpressing human I-FABP showed minimal effects on FA incorporation (6.Darimont C. Gradoux N. Persohn E. Cumin F. Pover A.De Effects of intestinal fatty acid-binding protein overexpression on fatty acid metabolism in Caco-2 cells.J. Lipid Res. 2000; 41: 84-92Abstract Full Text Full Text PDF PubMed Google Scholar). Because no in vivo or in vitro function can be definitively put forward for I-FABP, a puzzling and interesting question pertaining to its specific role in the enterocyte persists. Findings from I-Fabp−/− mice (4.Vassileva G. Huwyler L. Poirier K. Agellon L.B. Toth M.J. The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice.FASEB J. 2000; 14: 2040-2046Crossref PubMed Scopus (151) Google Scholar) and the Ala54Thr human mutation (7.Baier L.J. Sacchettini J.C. Knowler W.C. Eads J. Paolisso G. Tataranni P.A. Mochizuki H. Bennett P.H. 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. 1995; 95: 1281-1287Crossref PubMed Scopus (345) Google Scholar, 8.Agren J.J. Valve R. Vidgren H. Laakso M. Uusitupa M. Postprandial lipemic response is modified by the polymorphism at codon 54 of the fatty acid-binding protein 2 gene.Arterioscler. Thromb. Vasc. Biol. 1998; 18: 1606-1610Crossref PubMed Scopus (95) Google Scholar, 9.Stan S. Lambert M. Delvin E. Paradis G. O'Loughlin J. Hanley J.A. Levy E. Intestinal fatty acid binding protein and microsomal triglyceride transfer protein polymorphisms in French-Canadian youth.J. Lipid Res. 2005; 46: 320-327Abstract Full Text Full Text PDF PubMed Scopus (28) Google Scholar) suggest that I-FABP functions physiologically as a lipid-sensing component of energy homeostasis and not as a direct part of dietary FA absorption. Vassileva et al. (4.Vassileva G. Huwyler L. Poirier K. Agellon L.B. Toth M.J. The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice.FASEB J. 2000; 14: 2040-2046Crossref PubMed Scopus (151) Google Scholar) proposed that “I-FABP likely feeds information about dietary lipid status into mechanisms that universally control energy utilization, energy storage, and eventually body weight.” Therefore, I-FABP is in the of FA to specific other the β-oxidation in in the metabolism of other lipid as cholesterol and is associated with the of expression in the were in HIEC-6 with expression of I-FABP. HIEC-6 was with the of the enzyme as N. of the enzyme to human normal intestinal epithelial cell Res. PubMed Scopus Google Scholar). were and modified and at two or in the cell were at in and and from was by were 2 The experiments were at cDNA by J. H. was by and using and with the to the The was by and and of the in the and by The was into the of pQCXIP from using and and to in the The and empty pQCXIP were to produce in cells in with as D. Delvin E. Bendayan M. Menard D. Beaulieu J.F. Levy E. and role of in cholesterol absorption in human Lipid Res. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar). using was at the of for to experiments were of and HIEC-6 was for with in with an were with of acid for was to to and to was as by et al. J.F. F. J. and regulation of in from J. PubMed Scopus Google Scholar). was from by of acid and in the with were for a at to increase of which the were in and for in a To the presence of proteins, cells were and for as D. Delvin E. Bendayan M. Menard D. Beaulieu J.F. Levy E. and role of in cholesterol absorption in human Lipid Res. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar). were in and by and binding of the were using proteins by the of the targeted I-FABP in our carnitine palmitoyltransferase acetyl-coenzyme A carboxylase 2 HMG-CoA Niemann Pick C1-Like receptor and ABCA1 and binding protein 2 and acyl-coenzyme A oxidase The of was with were and the of proteins was using a with a and for protein content by were expressed as the for as as for a control were using the as D. Delvin E. Bendayan M. Menard D. Beaulieu J.F. Levy E. and role of in cholesterol absorption in human Lipid Res. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar). of were at for for and for were on these to to the of the The microsomal activity of and was as by and from liver and PubMed Scopus Google that of was as in fat that the and are functions of a microsomal Biol. Chem. Full Text PDF PubMed Google Scholar). in the and were of and lipid were on a in acid at of activity was as F. C. M. E. Levy E. the of Caco-2 cells to and J. 2000; PubMed Google Scholar, E. N. L. D. Delvin E. Menard D. Lipid and lipoprotein by the human J. Google Scholar). The of and of of the was by the of for at The was into by the of by and using an to for the of HMG-CoA reductase, the were and The activity of was by of activity of to the of protein to the in a of and for at the was by by cholesterol and as The and were by and the of the were and A for the of activity was as by and The mitochondrial carnitine palmitoyltransferase to J. Biochem. PubMed Scopus Google Scholar). the was at and was by the of of mitochondrial to of the reduced and with of and a of The was with the of was in in a with and to the in which the was activity was to of The activity of A was at by the of the of to and A from and Biol. Chem. Full Text PDF PubMed Google Scholar). The was in and are as and the of the the of and was using To gain into I-FABP function in intestinal transfected HIEC-6 that expressed I-FABP in amounts The I-FABP protein expression was by and to a specific showed that I-FABP into a protein of the with a increase in its expression compared with normal HIEC-6 transfected with empty pQCXIP The overexpression to in HIEC-6 the I-FABP protein in human intestinal as protein expression I-FABP overexpression showed that I-FABP expression in HIEC-6 no effects on FA into and (5.Montoudis A. Delvin E. Menard D. Beaulieu J.F. Jean D. Tremblay E. Bendayan M. Levy E. Intestinal-fatty acid binding protein and lipid transport in human intestinal epithelial cells.Biochem. Biophys. Res. Commun. 2006; 339: 248-254Crossref PubMed Scopus (19) Google Scholar). the the status of the enzymes controlling via the which for the of in intestinal epithelial observed in and were in from transfected and cells transfected with empty which is the first that is to be in no were in the activity of this critical enzyme cells overexpressing I-FABP and cells treated with empty pQCXIP the of I-FABP to influence the Because critical roles pertaining to intracellular FA associated with that I-FABP be of the oxidation of To this HIEC-6 to I-FABP expression their oxidation HIEC-6 was with the overexpression of I-FABP resulted in an increased of into CO2 and augmented the incorporation of into acid-soluble metabolites which β-oxidation that the of FA be to mitochondrial the mechanisms by first the protein expression and activity of that the of from long-chain and a step their mitochondrial with the oxidation of to CO2 and increased levels of protein expression and activity were in HIEC-6 overexpressing I-FABP. the activity of an enzyme that in FA in in the activity of the was increased in HIEC-6 overexpressing I-FABP. Overall, our suggest that I-FABP an role in the of of I-FABP overexpression on carnitine palmitoyltransferase and A in were and for protein expression and for and activity are for cells transfected with empty the of a key enzyme in the as as that of a critical enzyme to the mitochondrial which a of that is the rate-limiting enzyme in the fatty transport for FA β-oxidation L. L. G. The of carboxylase 2000; PubMed Scopus Google Scholar). a critical role for the regulation of mitochondrial FA the of gene and protein expression that I-FABP the biosynthesis of in these as as of gene and protein expression that and The of experiments was at I-FABP overexpression the intracellular of of CHOL was in control and modified intestinal I-FABP overexpression caused a of HIEC-6 to decreased, the intracellular of into its was not the impact of I-FABP expression on the HMG-CoA reductase, the rate-limiting step in CHOL synthesis, and an protein in the which catalyzes the of from and fatty of I-FABP in HIEC-6 led to an increase in transcripts protein expression and activity of HMG-CoA On the other hand, the of and activity of were not of I-FABP overexpression on HMG-CoA gene protein mass, and The levels of HMG-CoA transcripts and protein content were by and as in and were for activity are for cells transfected with empty of I-FABP overexpression on gene expression and The of was as in and were for are for to on the proteins that control CHOL including that to intestinal CHOL transport D. Delvin E. Bendayan M. Menard D. Beaulieu J.F. Levy E. and role of in cholesterol absorption in human Lipid Res. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar, M. E. D. G. H. of receptors and in in the small PubMed Scopus Google Scholar). I-FABP overexpression in HIEC-6 resulted in diminished levels of and the protein of the of the protein expression of and that of revealed an increase Because and as efflux the CHOL of their The I-FABP overexpression resulted in a significant increase in ABCA1 and gene expression levels Furthermore, the protein of ABCA1 and increased under the influence of I-FABP overexpression and protein expression of ABCA1 and in HIEC-6 overexpressing I-FABP. Intestinal epithelial cells were with to and for levels by and for protein by of ABCA1 and are for cells transfected with empty Finally, on the nuclear and that the of a of genes associated with lipid first which CHOL gene and protein expression did to I-FABP overexpression the status of peroxisome proliferator-activated receptor liver X receptor and X receptor The data in the of and the of and the of and in HIEC-6 overexpressing of I-FABP overexpression on the gene expression of the nuclear receptors peroxisome proliferator-activated receptor X receptor and liver X receptor from intestinal epithelial cells was by specific for the gene were to the of the are for cells transfected with empty the of in FA interesting to I-FABP overexpression influence which catalyzes the rate-limiting step in peroxisomal FA β-oxidation. in or protein of control cells with empty and epithelial cells overexpressing I-FABP. has with to the and of in the presence and roles of the two FABPs in the on the of I-FABP to lipid the overexpression in demonstrated that I-FABP is to lipid by with specific that I-FABP overexpression results in the a of influence of as by activity of enzymes controlling the and acid CHOL uptake, which was by the gene and protein expression of the transporter as as the increased gene and protein expression of ABCA1 along with the augmented protein of in the protein and activity of HMG-CoA in upregulation of mitochondrial FA by the of the of and the of the and of the gene and protein expression of and in of the nuclear receptors that the effects of at the and gene and protein expression of which that FA β-oxidation in is not by I-FABP To address the influence of I-FABP on an essential for lipoprotein the activity of the enzymes biosynthesis in the intestine via the which for and via the or R. A. of Lipid Res. PubMed Scopus Google Scholar). the FA and are to and by and for lipids to be into the by is from or via and can in a of J.M. Lipid in Scholar). this catalyzes the step by to which is to by to The two the which of the of to by the not to but to of and their Lipid Res. PubMed Scopus Google Scholar). The experiments using modified HIEC-6 to the of I-FABP to the and the of I-FABP to influence lipid and which has in our (5.Montoudis A. Delvin E. Menard D. Beaulieu J.F. Jean D. Tremblay E. Bendayan M. Levy E. Intestinal-fatty acid binding protein and lipid transport in human intestinal epithelial cells.Biochem. Biophys. Res. Commun. 2006; 339: 248-254Crossref PubMed Scopus (19) Google Scholar). catalyzes of the in the of and to Because is essential for its gene and protein expression and that I-FABP overexpression to the observations of the of HIEC-6 to of lipids and to transport in the of of this was with our observations to the decline of gene and protein expression as a function of I-FABP is to the mitochondrial via a unique that amino acids L. L. G. The of carboxylase 2000; PubMed Scopus Google Scholar, L. A. carboxylase and for two Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). on the mitochondrial which a of carnitine these the of into the and their β-oxidation L. fatty acid oxidation and reduced fat in mice carboxylase PubMed Scopus Google Scholar). of the that HIEC-6 is to for β-oxidation I-FABP is Because FA has not in HIEC-6 high levels of I-FABP, that may be for via β-oxidation. to be our data a significant increase in the of to CO2 and which are a of β-oxidation J.F. is no of acid Biol. PubMed Scopus (72) Google Scholar). was by a of protein and in the mitochondrial catalyzes the of from long-chain and carnitine The mitochondrial carnitine palmitoyltransferase to J. Biochem. PubMed Scopus Google which the rate-limiting regulated step of FA to is for FA entry into and β-oxidation The mitochondrial carnitine palmitoyltransferase to J. Biochem. PubMed Scopus Google Scholar, of and Lipid Res. PubMed Scopus Google Scholar). observed an increase in of the enzymes in mitochondria, in the mitochondrial which catalyzes the step of long-chain FA in the presence of to and is the first that high mitochondrial in response to the expression of I-FABP. Therefore, from an I-FABP for its role in regulating FA via β-oxidation overexpression of was to be associated with β-oxidation activity in cells D. K. J. C. L. L. M. J. of peroxisome proliferator-activated receptor on the intracellular and of apolipoprotein and Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). Conversely, mice were by FA oxidation H. E. M. F. liver fatty acid binding and liver lipid in mice the liver fatty acid-binding protein Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, S. J. triglyceride and fatty acid in mice with of the liver fatty acid-binding protein Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). the is to that I-FABP for of the two FABPs in HIEC-6 and that its overexpression has not resulted in upregulation of are to FA and the first is by an which is as the step controlling the the lipid and peroxisomal PubMed Scopus Google Scholar). in mitochondrial and peroxisomal β-oxidation as from the but and associated with in mitochondrial β-oxidation lipid and peroxisomal PubMed Scopus Google Scholar, D. Bennett M.J. Fatty acid oxidation 2002; PubMed Scopus Google Scholar). mitochondrial β-oxidation is to the to the of in peroxisomal β-oxidation is and long-chain fatty its function is to or into a that can be by mitochondrial enzymes and into the mitochondria, β-oxidation is lipid and peroxisomal PubMed Scopus Google Scholar, H. of fatty acids in mitochondria, and a of Lipid Res. 1995; PubMed Scopus Google Scholar, and peroxisome proliferator-activated receptor an PubMed Scopus Google Scholar). our the overexpression of I-FABP did not gene and protein which that in to mitochondria, are not regulated by I-FABP. data the and of the from our experiments was that I-FABP overexpression in HIEC-6 led to reduced CHOL the mechanisms this of CHOL in and efflux were gene expression of and as as levels of ABCA1 and were the of key mediator of CHOL and the upregulation of ABCA1 and which the efflux of enterocyte CHOL E. S. D. N. F. Delvin E. Lambert M. Intestinal cholesterol transport an and 18: PubMed Scopus Google Scholar, A. J.J. C. ABCA1 is essential for cholesterol efflux the absorption of dietary cholesterol in Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, S. E. efflux of cholesterol in cells.J. Lipid Res. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, J.J. J.A. J. L. K. J.M. Regulation of absorption and efflux of cholesterol by 2000; PubMed Scopus Google Scholar, L. J. J.C. of and cholesterol and absorption of dietary Clin. Invest. 2002; PubMed Scopus Google Scholar). the by which CHOL from the intestinal into the the small intestine D. Delvin E. Bendayan M. Menard D. Beaulieu J.F. Levy E. and role of in cholesterol absorption in human Lipid Res. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar, L.J. G. M. A. M. et protein is critical for intestinal cholesterol PubMed Scopus Google Scholar, M. J. P.A. et of is C1-Like 2005; PubMed Scopus Google Scholar). proteins, and F. D. M. C. J. C. S. R. et lipid absorption in mice overexpressing intestinal Biol. Chem. 2006; Full Text Full Text PDF PubMed Scopus Google Scholar, E. Menard D. Delvin E. L. L. Bendayan M. and function of in the human PubMed Scopus Google but their function in intestinal CHOL investigation. to our I-FABP to CHOL and to CHOL of results showed an increase in the nuclear and which the of FA oxidation in HIEC-6 overexpressing I-FABP. is in with studies that the mouse has a specific to a E. of an PubMed Scopus Google Scholar). were to be for the of and an interaction was the and unique response in the part of the H. C. of receptors and in and of the gene liver protein in the liver and the small J. PubMed Scopus Google Scholar). Because I-FABP is to a role in the binding and of in and to be an for the regulation of genes the of the intracellular of long-chain is to suggest that I-FABP a protein in the of in the of genes in the intestine. in the with nuclear as and the mouse in genes with are direct by a of for increased proliferator-activated nuclear control of PubMed Scopus Google Scholar). A of or were as the the and insulin are and which the role of as J. The mechanisms of of 2002; PubMed Scopus Google Scholar, C. J. proliferator-activated for in from and PubMed Scopus Google Scholar, A.B. S. D. S. The effects of on insulin and and triglyceride content in with 2 2002; PubMed Scopus Google Scholar). that is expressed at high levels in that significant FA and as the and intestine S. M. S. proliferator-activated receptor PubMed Scopus Google and is in and lipid metabolism an of insulin and a lipid and metabolism M. M. et from in the nuclear receptor peroxisome proliferator-activated PubMed Scopus Google Scholar, N. H. H. K. S. R. C. et and insulin Cell. Full Text Full Text PDF PubMed Scopus Google their gene expression and augmented in HIEC-6 overexpressing I-FABP. our results that the overexpression of I-FABP was to which activity and the β-oxidation of Conversely, targeted I-FABP gene disruption I-FABP FA and their in the which may insulin as is the in mice (1.Agellon L.B. Toth M.J. Thomson A.B. Intracellular lipid binding proteins of the small intestine.Mol. Cell. Biochem. 2002; 239: 79-82Crossref PubMed Scopus (72) Google Scholar, G. Huwyler L. Poirier K. Agellon L.B. Toth M.J. The intestinal fatty acid binding protein is not essential for dietary fat absorption in mice.FASEB J. 2000; 14: 2040-2046Crossref PubMed Scopus (151) Google Scholar). the I-FABP overexpression did not the of and studies are to is in amounts for or the for is for and and control the of a of specific genes in the in CHOL and J.J. nuclear receptors as and of Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, N. H. J.C. proliferator-activated receptors and of gene expression in Res. PubMed Scopus Google and the are and that with are as in the of and 2 J. J. K. E. J.C. of of on lipid and lipoprotein 1998; PubMed Scopus Google Scholar). our I-FABP overexpression resulted in the expression of intestinal CHOL and in the increased of HMG-CoA and are of CHOL to the nuclear receptor and controlling lipid metabolism and the of Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar, L.J. J.C. X receptors and the control of cholesterol for the of Biophys. PubMed Scopus Google Scholar). intestinal CHOL absorption in mice J.J. J.A. J. L. K. J.M. Regulation of absorption and efflux of cholesterol by 2000; PubMed Scopus Google Scholar) the of transporter including and which are for CHOL efflux J.J. C. J.A. H. Regulation of and by the liver X receptors and Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, A. J.C. of proteins and their transport to the Clin. Invest. 2002; PubMed Scopus Google Scholar). Furthermore, the gene for a protein critical for intestinal CHOL is under the control of levels in human C. A. J.C. C. S. gene expression is by in the Biophys. Res. Commun. 2006; PubMed Scopus Google Scholar). this for the first the role of I-FABP in FA and CHOL our the that I-FABP is not for the of or for their intracellular to in its intestinal CHOL transport and FA to for β-oxidation. A in I-FABP may in CHOL absorption and FA oxidation, which may increase FA and CHOL in the was by the of and the of The for

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.