Fatty acid binding protein removes fatty acids but not phospholipids from microsomes liposomes and sonicated vesicles

Zanetti, Rosana; Catalá, Ángel

doi:10.1007/bf00230804

Cited by 6 publications

(6 citation statements)

References 16 publications

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“…(i) Fluorescence quenching of DAUDA fluorescence by phospholipids is unlikely as it is hard to imagine a major structural change within the binding cavity of the protein that might cause quenching (e.g., change in polarity) but not release of DAUDA. (ii) A direct displacement by monomeric anionic phospholipids under conditions of low ionic strength is unlikely as (a) there is no evidence for phospholipids as ligands for L-FABP ( , ) and (b) the monomer concentration of the phospholipids that were used would be too low (<10 -9 M) to allow significant binding unless the K d for phospholipid binding was similarly low (<10 -9 M), in which case the protein would be primarily a phospholipid binding protein. (iii) The differential partitioning of DAUDA between the lipid binding protein and the phospholipid vesicles will vary according to the nature and concentration of the phospholipid aggregate to produce a change in fluorescence (see Materials and Methods).…”

Section: Resultsmentioning

confidence: 99%

Binding of Recombinant Rat Liver Fatty Acid-Binding Protein to Small Anionic Phospholipid Vesicles Results in Ligand Release: A Model for Interfacial Binding and Fatty Acid Targeting

1999

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A number of intracellular proteins bind to negatively charged phospholipid membranes, and this interfacial binding results in a conformational change that modulates the activity of the protein. Using a fluorescent fatty acid analogue, 11-[5-(dimethylamino)naphthalenesulfonyl]undecanoic acid (DAUDA), it is possible to demonstrate the release of this ligand from recombinant rat liver FABP in the presence of phospholipid vesicles that contain a significant proportion of anionic phospholipids. The ligand release that is observed with anionic phospholipids is sensitive to the ionic strength of the assay conditions and the anionic charge density of the phospholipid at the interface, indicating that nonspecific electrostatic interactions play an important role in the process. The stoichiometric relationship between anionic phospholipid and liver FABP suggests that the liver FABP coats the surface of the phospholipid vesicle. The most likely explanation for ligand release is that interaction of FABP with an anionic membrane interface induces a rapid conformational change, resulting in a reduced affinity of DAUDA for the protein. The nature of this interaction involves both electrostatic and nonpolar interactions as maximal release of liver FABP from phospholipid vesicles with recovery of ligand binding cannot be achieved with high salt and requires the presence of a nonionic detergent. The precise interfacial mechanism that results in the rapid release of ligand from L-FABP remains to be determined, but studies with two mutants, F3W and F18W, suggest the possible involvement of the amino-terminal region of the protein in the process. The conformational change linked to interfacial binding of this protein could provide a mechanism for fatty acid targeting within the cell.

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Section: Resultsmentioning

confidence: 99%

Binding of Recombinant Rat Liver Fatty Acid-Binding Protein to Small Anionic Phospholipid Vesicles Results in Ligand Release: A Model for Interfacial Binding and Fatty Acid Targeting

1999

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“…Using sonicated vesicles as fatty acid or phospholipid donors, mouse liver fatty acid binding protein was capable of binding palmitic acid but not phospholipids. These studies suggest that liver fatty acid binding protein can interact with different kinds of membranes increasing specifically desorption of fatty acids [21]. …”

Section: Fatty Acid Binding Protein Studiesmentioning

confidence: 99%

Five Decades with Polyunsaturated Fatty Acids: Chemical Synthesis, Enzymatic Formation, Lipid Peroxidation and Its Biological Effects

Catalá

2013

Journal of Lipids

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I have been involved in research on polyunsaturated fatty acids since 1964 and this review is intended to cover some of the most important aspects of this work. Polyunsaturated fatty acids have followed me during my whole scientific career and I have published a number of studies concerned with different aspects of them such as chemical synthesis, enzymatic formation, metabolism, transport, physical, chemical, and catalytic properties of a reconstructed desaturase system in liposomes, lipid peroxidation, and their effects. The first project I became involved in was the organic synthesis of [1-14C] eicosa-11,14-dienoic acid, with the aim of demonstrating the participation of that compound as a possible intermediary in the biosynthesis of arachidonic acid “in vivo.” From 1966 to 1982, I was involved in several projects that study the metabolism of polyunsaturated fatty acids. In the eighties, we studied fatty acid binding protein. From 1990 up to now, our laboratory has been interested in the lipid peroxidation of biological membranes from various tissues and different species as well as liposomes prepared with phospholipids rich in PUFAs. We tested the effect of many antioxidants such as alpha tocopherol, vitamin A, melatonin and its structural analogues, and conjugated linoleic acid, among others.

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“…in ref. 12 (22,77). In contrast, both L-FABP and I-FABP shift the equilibrium partitioning of LCFA from microsomal membranes to the aqueous such that as much as 38% of microsomal bound LCFA is solubilized as aqueous FABP-LCFA complexes (22,77,78).…”

Section: Step 6 Desorption Of Fatty Acids From the Plasma Membrane Into The Cytoplasm: A Role For Cytosolic Fatty Acid Binding Proteins (mentioning

confidence: 99%

“…12 (22,77). In contrast, both L-FABP and I-FABP shift the equilibrium partitioning of LCFA from microsomal membranes to the aqueous such that as much as 38% of microsomal bound LCFA is solubilized as aqueous FABP-LCFA complexes (22,77,78). Finally, in intact cells, the soluble fraction of LCFA is determined by the FABP c concentration in the cytoplasm (42,79).…”

Section: Step 6 Desorption Of Fatty Acids From the Plasma Membrane Into The Cytoplasm: A Role For Cytosolic Fatty Acid Binding Proteins (mentioning

confidence: 99%

Cellular uptake and intracellular trafficking of long chain fatty acids

McArthur

Atshaves

Frolov

et al. 1999

Journal of Lipid Research

331

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While aspects of cellular fatty acid uptake have been studied as early as 50 years ago, recent developments in this rapidly evolving field have yielded new functional insights on the individual mechanistic steps in this process. The extremely low aqueous solubility of long chain fatty acids (LCFA) together with the very high affinity of serum albumin and cytoplasmic fatty acid binding proteins for LCFA have challenged the limits of technology in resolving the individual steps of this process. To date no single mechanism alone accounts for regulation of cellular LCFA uptake. Key regulatory points in cellular uptake of LCFA include: the aqueous solubility of the LCFA; the driving force(s) for LCFA entry into the cell membrane; the relative roles of diffusional and protein mediated LCFA translocation across the plasma membrane; cytoplasmic LCFA binding protein-mediated uptake and/or intracellular diffusion; the activity of LCFA-CoA synthetase; and cytoplasmic protein mediated targeting of LCFA or LCFA-CoAs toward specific metabolic pathways. The emerging picture is that the cell has multiple, overlapping mechanisms that assure adequate uptake and directed intracellular movement of LCFA required for maintenance of physiological functions. The upcoming challenge is to take advantage of new advances in this field to elucidate the differential interactions between these pathways in intact cells and in tissues. -McArthur, M.

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Fatty acid binding protein removes fatty acids but not phospholipids from microsomes liposomes and sonicated vesicles

Cited by 6 publications

References 16 publications

Binding of Recombinant Rat Liver Fatty Acid-Binding Protein to Small Anionic Phospholipid Vesicles Results in Ligand Release: A Model for Interfacial Binding and Fatty Acid Targeting

Binding of Recombinant Rat Liver Fatty Acid-Binding Protein to Small Anionic Phospholipid Vesicles Results in Ligand Release: A Model for Interfacial Binding and Fatty Acid Targeting

Five Decades with Polyunsaturated Fatty Acids: Chemical Synthesis, Enzymatic Formation, Lipid Peroxidation and Its Biological Effects

Cellular uptake and intracellular trafficking of long chain fatty acids

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