Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Lagakos, William S.; Guan, Xudong; Ho, Shiu Ying; Sawicki, Luciana Rodriguez; Córsico, Betina; Kodukula, Sarala; Murota, Kazuo; Stark, Ruth E.; Storch, Judith

doi:10.1074/jbc.m113.473579

Cited by 37 publications

(33 citation statements)

References 49 publications

(61 reference statements)

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“…Studies from our laboratory have shown that LFABP, but not IFABP, is a 2-MG-binding protein in vitro and in vivo (9,37). In keeping with this binding function, we found alterations in intestinal 2-MG metabolism in chow-fed LFABP Ϫ/Ϫ mice but not in the IFABP Ϫ/Ϫ mice (25).…”

Section: B-d) the Lfabpsupporting

confidence: 68%

“…In particular, the decreased incorporation of diet-derived MG into TG relative to PL observed in chow-fed mice (25) was also found in this study for both low fat and high fat-fed mice. Thus, LFABP is involved in trafficking of dietderived MG under all dietary conditions examined, consistent with it being the MG binding and transport protein in cytosol (9). Analysis of ILBP ablated mice demonstrated a defect in mucosal to serosal transport of taurocholic acid in everted gut sacs and supports the idea that FABPs are involved in the cellular transport of their respective ligands (72).…”

Section: Discussionsupporting

confidence: 52%

“…For example, although all the FABPs have a highly conserved tertiary structure containing a 10-strand ␤-barrel within which the ligands are bound, IFABP is typical of the FABP family in that it has a single high affinity binding site for FA, whereas LFABP can bind two FA as well as other lipids, including lysophospholipids, prostaglandins, and MG (8,9). In vitro FA transfer mechanisms are also different, with LFABP transferring FA to membranes via an aqueous diffusional mechanism, whereas FA transfer from IFABP occurs during direct protein-membrane collisional interactions (10 -12).…”

mentioning

confidence: 99%

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Direct Comparison of Mice Null for Liver or Intestinal Fatty Acid-binding Proteins Reveals Highly Divergent Phenotypic Responses to High Fat Feeding

Gajda

Zhou

Agellon

et al. 2013

Journal of Biological Chemistry

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Background:Intestinal and liver fatty acid-binding proteins (IFABP and LFABP) are coexpressed in the enterocyte, but their individual functions are not known. Results: High fat feeding promotes different phenotypes in IFABP-and LFABP-null mice. Conclusion: IFABP and LFABP have unique intracellular functions, which in turn produce divergent whole body effects. Significance: Enterocyte FABP ablation modulates intestinal lipid metabolism, which contributes to altered systemic energy homeostasis.

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Section: B-d) the Lfabpsupporting

confidence: 68%

Section: Discussionsupporting

confidence: 52%

mentioning

confidence: 99%

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Direct Comparison of Mice Null for Liver or Intestinal Fatty Acid-binding Proteins Reveals Highly Divergent Phenotypic Responses to High Fat Feeding

Gajda

Zhou

Agellon

et al. 2013

Journal of Biological Chemistry

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“…In addition to their disparate expression patterns, they also have different structures and ligand binding properties ( 40 ). LFABP also binds other hydrophobic ligands, including MAG and acyl-CoA ( 41,42 ), and can mediate the budding of prechylomicron transport vesicles from the ER ( 43 ). Studies using mice defi cient in either FABP support the proposition that IFABP channels fatty acids for TAG synthesis, while LFABP channels MAG for TAG synthesis and may be involved in fatty acid oxidation ( 41 ).…”

Section: Enzymatic Pathways Mediating Intestinal Tag Synthesismentioning

confidence: 75%

“…LFABP also binds other hydrophobic ligands, including MAG and acyl-CoA ( 41,42 ), and can mediate the budding of prechylomicron transport vesicles from the ER ( 43 ). Studies using mice defi cient in either FABP support the proposition that IFABP channels fatty acids for TAG synthesis, while LFABP channels MAG for TAG synthesis and may be involved in fatty acid oxidation ( 41 ). These mice do not show overt fat malabsorption, indicating that either these FABPs play minor roles in fat absorption or their functions in the process can be compensated for when they are absent.…”

Section: Enzymatic Pathways Mediating Intestinal Tag Synthesismentioning

confidence: 99%

Intestinal triacylglycerol synthesis in fat absorption and systemic energy metabolism

Yen

Nelson

Yen

2015

Journal of Lipid Research

120

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cell membranes. The biosynthesis of TAG thus serves many physiological functions. Because it is highly reduced and anhydrous, TAG is the primary energy substrate stored in adipose tissues to sustain animals during fasting. TAG is also synthesized in the liver for the assembly and secretion of VLDL to transport neutral lipids to other tissues, as well as in the mammary gland for the formation of milk fat globules to deliver fatty acids and other lipid-soluble nutrients to mammalian neonates.In the intestine, TAG synthesis is prominent for its role in the absorption of dietary fat ( 2, 3 ). TAG forms the bulk of animal fats and plant oils. It accounts for approximately 95% of dietary fat, depending on the food sources, with the rest as phospholipids and trace amounts of sterols, lipid-soluble vitamins, and other lipophilic components. Because of its hydrophobicity, TAG does not traverse the cellular membrane. Its absorption involves hydrolysis to fatty acids and monoacylglycerol (MAG) in the intestinal lumen, lipid uptake by the enterocytes, resynthesis of TAG, and assembly and secretion of ApoB-containing chylomicrons for delivery of TAG and other lipid-soluble nutrients. Like with most nutrients, the absorption of TAG occurs mostly in the proximal half of the intestine and less so in the distal intestine, where specifi c compounds, such as bile acids and vitamin B12, are absorbed. The activity of TAG synthesis coincides with the absorption of dietary fat along the length of the intestine, and it is more active in Press, September 17, 2014 DOI 10.1194 Abbreviations: ACSL, acyl-CoA synthetase; AGPAT, 1-acylglycerol-3-phosphate acyltransferase; ATGL, adipose triglyceride lipase; CD36, cluster of differentiation; CGI-58, comparative gene identifi cation-58; Cideb, cell death-inducing DNA fragmentation factor 45 (DFF45) -like effector b; DAG, diacylglycerol; DGAT, acyl-CoA:diacylglycerol acyltransferase; ER, endoplasmic reticulum; FABP, fatty acid binding protein; GLP-1, glucagon-like peptide 1; GPAT, glycerol-3-phosphate acyltransferase; G3P, glycerol-3-phosphate; IFABP, intestine-type fatty acid binding protein; LFABP, liver-type fatty acid binding protein; MAG, monoacylglycerol; MBOAT, membrane-bound O-acyltransferase; MGAT, acylCoA:monoacylglycerol acyltransferase; MTP, microsomal triacylglycerol transfer protein; PA, phosphatidic acid; PAP, phosphatidic acid phosphatase; TAG, triacylglycerol (triglyceride ). Published, JLR Papers in

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Intestinal CD36 and Other Key Proteins of Lipid Utilization: Role in Absorption and Gut Homeostasis

Cifarelli

Abumrad

2018

Comprehensive Physiology

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Several proteins have been implicated in fatty acid (FA) transport by enterocytes including the scavenger receptor CD36 (SR-B2), the scavenger receptor B1 (SR-B1) a member of the CD36 family and the FA transport protein 4 (FATP4). Here, we review the regulation of enterocyte FA uptake and its function in lipid absorption including prechylomicron formation, assembly and transport. Emphasis is given to CD36, which is abundantly expressed along the digestive tract of rodents and humans and has been the most studied. We also address the pleiotropic functions of CD36 that go beyond lipid absorption and metabolism to include recent evidence of its impact on intestinal homeostasis and barrier maintenance. Areas of progress involving contribution of membrane phospholipid remodeling and of cytosolic FA-binding proteins, FABP1 and FABP2 to fat absorption will be covered.

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Liver Fatty Acid-binding Protein Binds Monoacylglycerol in Vitro and in Mouse Liver Cytosol

Cited by 37 publications

References 49 publications

Direct Comparison of Mice Null for Liver or Intestinal Fatty Acid-binding Proteins Reveals Highly Divergent Phenotypic Responses to High Fat Feeding

Direct Comparison of Mice Null for Liver or Intestinal Fatty Acid-binding Proteins Reveals Highly Divergent Phenotypic Responses to High Fat Feeding

Intestinal triacylglycerol synthesis in fat absorption and systemic energy metabolism

Intestinal CD36 and Other Key Proteins of Lipid Utilization: Role in Absorption and Gut Homeostasis

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