Modelling intracellular fatty acid transport: possible mechanistic role of cytoplasmic fatty acid-binding protein

Vork, M; Glatz, Jan F. C.; Vusse, Ger J.

doi:10.1016/s0952-3278(97)90486-5

Cited by 27 publications

(13 citation statements)

References 20 publications

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“…Rat heart contains about 50 µM of FABP with a K d of 14 nM for fatty acid [21,60]. Despite FABP’s high affinity for fatty acid, many unresolved questions still surround the hypothesis that FABP alone facilitates fatty acid transport in the cell [22,44,69,71,75]. …”

Section: Discussionmentioning

confidence: 99%

Palmitate interaction with physiological states of myoglobin

Shih

Chung

Sriram

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background Previous studies have shown that palmitate (PA) can bind specifically and non-specifically to Fe (III) MbCN. The present study has observed PA interaction with physiological states of Fe (II) Mb, and the observations support the hypothesis that Mb may have a potential role in facilitating intracellular fatty acid transport. Methods 1H NMR spectra measurements of the Mb signal during PA titration show signal changes consistent with specific and non-specific binding. Results Palmitate (PA) interacts differently with physiological states of Mb. Deoxy Mb does not interact specifically or non-specifically with PA, while the carbonmonoxy myoglobin (MbCO) interaction with PA decreases the intensity of selective signals and produces a 0.15 ppm upfield shift of the PA methylene peak. The selective signal change upon PA titration provides a basis to determine an apparent PA binding constant, which serves to create a model comparing the competitive PA binding and facilitated fatty acid transport of Mb and fatty acid binding protein (FABP). Conclusions Given contrasting PA interaction of ligated vs. unligated Mb, the cellular fatty acid binding protein (FABP) and Mb concentration in the cell, the reported cellular diffusion coefficients, the PA dissociation constants from ligated Mb and FABP, a fatty acid flux model suggests that Mb can compete with FABP transporting cellular fatty acid. General Significance Under oxygenated conditions and continuous energy demand, Mb, dependent fatty acid transport could influence the cell’s preference for carbohydrate or fatty acid as a fuel source and regulate fatty acid metabolism.

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Section: Discussionmentioning

confidence: 99%

Palmitate interaction with physiological states of myoglobin

Shih

Chung

Sriram

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…This notion is supported by mathematical studies performed by Vork and coworkers. 51) Recent unpublished pilot studies from our laboratory suggest that interplay between plasma and interstitial albumin is critical in the transfer of FA from plasma to interstitium and vice versa. These experiments may point to a rapid equilibration of FA between the high affinity binding sites of plasma albumin on the one side and interstitial albumin on the other, followed by relatively slow diffusion of the interstitial albumin/FA complex in the direction of the cardiomyocyte.…”

Section: Uptake Of Fatty Acids By Organs: Possibles Roles Of Plasma Amentioning

confidence: 98%

Albumin as Fatty Acid Transporter

Vusse¹

2009

Drug Metabolism and Pharmacokinetics

369

269

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Fatty acids play critical roles in mammalian energy metabolism. Moreover, they are important substrates for the synthesis of membrane phospholipids and biologically active compounds like eicosanoids and leukotrienes. Because of their low solubility in aqueous solutions such as blood plasma and interstitial fluid, fatty acids are in need of binding proteins to increase their concentration in vascular and interstitial compartments. Albumin acts as main fatty acid binding protein in extracellular fluids. Plasma albumin possesses about 7 binding sites for fatty acids with moderate to high affinity, enhancing the concentration of fatty acids by a several orders of magnitude. Despite the high affinity of albumin for fatty acids, uptake of fatty acids by parenchymal cells such as skeletal and cardiac myocytes seems not to be hampered by albumin. In contrast, experimental findings suggest that albumin may facilitate the uptake of fatty acids by organs in need of these substrates. In the present overview the following issues will be briefly discussed: (i) transport and storage of fatty acids in the mammalian body, (ii) biosynthesis of albumin in the liver, (iii) localization and concentration of albumin in body fluids, (iv) interactions between albumin and fatty acids, (v) albumin structure and fatty acid binding sites, (vi) uptake of fatty acids by organs and roles for plasma albumin and (vii) lessons from patients and experimental animals lacking plasma albumin.

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“…The proposed role for FABPs as intracellular FAs transporters theoretically requires their direct interaction with ligand donor and acceptor membranes and/or proteins [12, 13]. Thus, FABPs may serve not only to deliver FAs to target organelles, but also to remove membrane bound FAs.…”

Section: Introductionmentioning

confidence: 99%

Interaction of enterocyte FABPs with phospholipid membranes: Clues for specific physiological roles

Falomir-Lockhart

Franchini

Guerbi

et al. 2011

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Intestinal and liver fatty acid binding proteins (IFABP and LFABP, respectively), are cytosolic soluble proteins with the capacity to bind and transport hydrophobic ligands between different sub-cellular compartments. Their functions are still not clear but they are supposed to be involved in lipid trafficking and metabolism, cell growth, and regulation of several other processes, like cell differentiation. Here we investigated the interaction of these proteins with different models of phospholipid membrane vesicles in order to achieve further insight into their specificity within the enterocyte. A combination of biophysical and biochemical techniques allowed us to determine affinities of these proteins to membranes, the way phospholipid composition and vesicle size and curvature modulate such interaction, as well as the effect of protein binding on the integrity of the membrane structure. We demonstrate here that, beside their apparently opposite ligand transfer mechanisms, both LFABP and IFABP are able to interact with phospholipid membranes, but the factors that modulate such interactions are different for each protein, further implying different roles for IFABP and LFABP in the intracellular context. These results contribute to the proposed central role of intestinal FABPs in the lipid traffic within enterocytes as well as in the regulation of more complex cellular processes.

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Modelling intracellular fatty acid transport: possible mechanistic role of cytoplasmic fatty acid-binding protein

Cited by 27 publications

References 20 publications

Palmitate interaction with physiological states of myoglobin

Palmitate interaction with physiological states of myoglobin

Albumin as Fatty Acid Transporter

Interaction of enterocyte FABPs with phospholipid membranes: Clues for specific physiological roles

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