The binding affinity of fatty acid-binding proteins from human, pig and rat liver for different fluorescent fatty acids and other ligands

Peeters, Roger A.; Groen, Monique A.P.M. in't; Moel, Mariëlle P. De; Moerkerk, H.T.B. van; Veerkamp, J.H.

doi:10.1016/0020-711x(89)90365-0

Cited by 62 publications

(56 citation statements)

References 48 publications

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“…Binding of 4 nmot palmitate per milligram delipidated protein from liver cytosol (Glatz and Veerkamp 1983), 1 mol fatty acid per mole heart FABP protein (Glatz et al 1985), and 2 mol fatty acid (oleic or palmitic acid) per mole liver or heart protein (Offner et al 1986) have been reported. Maximal binding capacities were 79, 52, and 54 nmol oleic acid per milligram protein for human, pig, and rat liver FABPs, and the molar ratio was 1 mol fatty acid per mole c-FABP (Peeters et al 1989). Others have suggested that one or two arginine residues (Arg126 and/or Argl06) form hydrogen bonds with the carboxyt group of the bound fatty acid and have suggested them as determinants of fatty acid ligand specificity (Jones et al 1988).…”

Section: Cytosolic Fatty Acid Binding Proteins In the Hepatocytementioning

confidence: 99%

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Petzinger¹

1994

Reviews of Physiology, Biochemistry and Pharmacology

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Section: Cytosolic Fatty Acid Binding Proteins In the Hepatocytementioning

confidence: 99%

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Petzinger¹

1994

Reviews of Physiology, Biochemistry and Pharmacology

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“…FABP‐bound palmitate was prepared by incubation of 18 mg human H‐FABP or L‐FABP with 1.8 µmol [1‐ 14 C]palmitate and removal of free palmitate with the Lipidex procedure [24]. Rat heart mitochondria (80–100 µg protein) or rat liver mitochondria (200–300 µg protein) were incubated with 29 and 20 nmol palmitate bound to 1200 µg L‐FABP or H‐FABP, respectively, in 1 mL oxidation buffer A at 37 °C.…”

Section: Methodsmentioning

confidence: 99%

Effect of fatty acid‐binding proteins on intermembrane fatty acid transport

Veerkamp

and

Zimmerman

2000

European Journal of Biochemistry

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Liposomes of different charge fixed to nitrocellulose filters were used to study the transfer of fatty acids to rat heart or liver mitochondria in the presence of fatty acid-binding protein (FABP) or albumin. [ 14 C]Palmitate oxidation was used as a parameter. Different FABP types and heart FABP mutants were tested. The charge of the liposomes did not influence the solubilization and mitochondrial oxidation of palmitate without FABP and the amount of solubilized palmitate in the presence of FABP. Mitochondria did not show a preference for oxidation of FABP-bound palmitate over their tissue-specific FABP type. All FABP types increased palmitate oxidation by heart and liver mitochondria with neutral, positive and negative liposomes by 2.5-fold, 3.2-fold and twofold, respectively. Ileal lipid-binding protein and H-FABP mutants that do not bind fatty acid had no effect. Other H-FABP mutants had different effects, dependent on the site of mutation. The effect of albumin was similar to, but not dependent on, liposome charge. The ionic strength had only a slight effect. In conclusion, the transfer of palmitate from liposomal membranes to mitochondria was increased by all FABP types to a similar extent. The membrane charge had a large effect in contrast to the origin of the mitochondria.Keywords: fatty acid oxidation; heart mitochondria; liver mitochondria; fixed liposomes; membrane charge.Fatty acid binding proteins (FABPs) have been isolated from cytosols of tissues of vertebrates and invertebrates as 13± 15 kDa proteins. Nine FABP types have been named up to now after the first tissue from which they were isolated. They show a characteristic tissue and cellular distribution [1]. In spite of the large amount of knowledge on their molecular structure, their binding properties and their genes, the functions of these different FABP types are still unclear. They are postulated to be involved in fatty acid uptake and targeting, in modulation of fatty acid concentration and, in this way, in regulation of metabolism, signal transduction, gene transcription and detoxification [1,2]. Theoretical considerations ascribed a role to FABPs in fatty acid transport in hepatocytes [3] and cardiomyocytes [4]. In model systems of liposomes, monolayers, mitochondria and microsomes, fatty acid transfer was demonstrated from FABP to membranes, from membranes to FABP and from membranes via FABP to membranes by use of radiolabeled or fluorescent fatty acids, or NMR ([1,2,5±8] and references therein). FABP facilitated the diffusion of oleate in a model cytosol system [9]. Photoactivatable radiolabeled fatty acids were taken up and labeled FABP in hepatocytes and adipocytes [10±11]. FABP-bound fatty acids were oxidized by mitochondria [8,12±14] and peroxisomes [14] or used for acyl-CoA synthesis by microsomes [15]. The technique of fluorescence recovery after photobleaching was used to measure the intracellular transport of a fluorescent fatty acid (12-N-methyl-(7-nitrobenzo-2-oxa-1,3-diazol)aminostearate; NBDstearate) [16,17]. Inhibition of ...

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“…The COX metabolites of ARA, such as prostaglandin (PG)E 2 , TxB 2 and LTB 4 do not bind L-FABP, whereas cyclopentenone PG, PGA 1 , PGA 2 , PGJ 2 , and D12-PGJ 2 , bind more avidly than oleic acid to L-FABP. PGD 2 , PGE 2 and PGF 2a are poor competitors, whereas PGE 1 is intermediate [103][104][105][106]. It has been demonstrated that L-FABP transports these ligands to PPAR through protein-protein interaction and thus may play an important role in gene expression [107,108].…”

Section: Fatty Acid Uptake By the Placenta: Roles Of Pparmentioning

confidence: 98%

Fatty acid‐activated nuclear transcription factors and their roles in human placenta

Duttaroy

2006

Eur. J. Lipid Sci. Technol.

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Fatty acid-activated nuclear transcription factors and their roles in human placentaEmerging evidence indicates that fatty acid-activated nuclear transcription factors play very important and complex roles in placental biology. These fatty acid-activated receptors are involved at a number of different levels such as differentiation, proliferation, and hormone synthesis in the feto-placental unit. Since these receptors are also fatty acid sensors, they may be involved in placental fatty acid transport and metabolism. The present article is a review of the complex roles of peroxisome proliferatoractivated receptors, sterol regulatory element-binding proteins and liver X receptors in placental biology.

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The binding affinity of fatty acid-binding proteins from human, pig and rat liver for different fluorescent fatty acids and other ligands

Cited by 62 publications

References 48 publications

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Effect of fatty acid‐binding proteins on intermembrane fatty acid transport

Fatty acid‐activated nuclear transcription factors and their roles in human placenta

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