The role of membranes and intracellular binding proteins in cytoplasmic transport of hydrophobic molecules: Fatty acid-binding proteins

Storch, Judith; Herr, Fiona; Hsu, Kuo Tung; Kim, Hye Kyung; Liou, Heng Ling; Smith, Elizabeth

doi:10.1016/s0305-0491(96)00180-0

Cited by 34 publications

(25 citation statements)

References 31 publications

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“…They increase FA solubility and facilitate transport of FA from the plasma membrane to sites of FA oxidation (mitochondria, peroxisomes), to sites of FA esterification into triacylglycerols (TGs) or phospholipids, or to the nucleus, possibly for regulatory functions ( fig. 4) with the concentration of I-FABP, in agreement with the data of Storch et al [131]. Experimental data of different investigators led to paradoxical conclusions about intermembrane FA transport by L-FABP.…”

Section: Fa Uptake and Transportsupporting

confidence: 88%

“…The transfer rates differ markedly between different FABP types. With 12-(9-anthroyloxy)oleic acid, the transfer rate is A-FABP > H-FABP >> I-FABP >> L-FABP [131]. When membranes contain anionic phospholipids, the AOFA transfer rate from H-FABP and A-FABP increases, suggesting that positively charged amino acid residues on the FABP surface are involved in the interaction between FABP and membrane.…”

Section: Function Of Fabps In Modulation Of Signal Transduction and Gmentioning

confidence: 99%

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New insights into the structure and function of fatty acid-binding proteins

Zimmerman¹,

Veerkamp²

2002

Cellular and Molecular Life Sciences (CMLS)

475

360

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Fatty acid-binding proteins (FABPs) are members of a superfamily of lipid-binding proteins, and occur intracellularly in vertebrates and invertebrates. This review presents recent findings on the diversity of these FABPs and their proposed roles in fatty acid (FA) metabolism and other cellular processes. Special attention is paid to the structural features of the different mammalian FABP types and the physiological role of these proteins in FA transport, cell growth and differentiation, cellular signalling, gene transcription and cytoprotection. Additionally, data on FABP knockout mice and the implication of FABP in medicine are discussed.

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Section: Fa Uptake and Transportsupporting

confidence: 88%

Section: Function Of Fabps In Modulation Of Signal Transduction and Gmentioning

confidence: 99%

New insights into the structure and function of fatty acid-binding proteins

Zimmerman¹,

Veerkamp²

2002

Cellular and Molecular Life Sciences (CMLS)

475

360

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“…We have elucidated distinct mechanisms by which different members of this protein family transfer fatty acids to phospholipid membranes in vitro, and it is hypothesized that these mechanisms play relevant physiological roles in the intracellular transport and utilization of fatty acids (27). IFABP was shown to use direct collisions with phospholipid membranes to transfer fatty acids, and the presence of anionic phospholipids in the acceptor membranes was found to dramatically increase the rate of fatty acid transfer (12).…”

Section: Discussionmentioning

confidence: 99%

The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes

Córsico

Cistola

Frieden

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

125

152

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Fatty acid binding proteins (FABPs) exhibit a ␤-barrel topology, comprising 10 antiparallel ␤-sheets capped by two short ␣-helical segments. Previous studies suggested that fatty acid transfer from several FABPs occurs during interaction between the protein and the acceptor membrane, and that the helical domain of the FABPs plays an important role in this process. In this study, we employed a helix-less variant of intestinal FABP (IFABP-HL) and examined the rate and mechanism of transfer of f luorescent anthroyloxy fatty acids (AOFA) from this protein to model membranes in comparison to the wild type (wIFABP). In marked contrast to wIFABP, IFABP-HL does not show significant modification of the AOFA transfer rate as a function of either the concentration or the composition of the acceptor membranes. These results suggest that the transfer of fatty acids from IFABP-HL occurs by an aqueous diffusionmediated process, i.e., in the absence of the helical domain, effective collisional transfer of fatty acids to membranes does not occur. Binding of wIFABP and IFABP-HL to membranes was directly analyzed by using a cytochrome c competition assay, and it was shown that IFABP-HL was 80% less efficient in preventing cytochrome c from binding to membranes than the native IFABP. Collectively, these results indicate that the ␣-helical region of IFABP is involved in membrane interactions and thus plays a critical role in the collisional mechanism of fatty acid transfer from IFABP to phospholipid membranes.

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“…Several reviews have focused on cytoplasmic lipid-binding proteins, i.e. cytoplasmic fattyacid-binding protein (FABP), cellular retinoic acidbinding proteins (CRABPs), cellular retinol-binding proteins (CRBPs), h-tocopherol-binding proteins (TBPs), and acylCoA-binding protein (ACBP) [9][10][11][12][13][14]. This review will concentrate on the membrane-associated fatty-acid-binding/transport proteins and their important roles in fatty acid uptake and metabolism, especially in the feto-placental unit.…”

Section: Multi-author Review Articlementioning

confidence: 99%

Cellular uptake of long-chain fatty acids: role of membrane-associated fatty-acid-binding/transport proteins

Duttaroy¹

2000

CMLS, Cell. Mol. Life Sci.

130

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The critical importance of long-chain fatty acids in cellular homeostasis demands an efficient uptake system for these fatty acids and their metabolism in tissues. Increasing evidence suggests that the plasma-membrane-associated and cytoplasmic fatty-acid-binding proteins are involved in cellular fatty acid uptake, transport and metabolism in tissues. These binding proteins may also function in the fine tuning of cellular events by modulating the metabolism of long-chain fatty acids implicated in the regulation of cell growth and various cellular functions. Several membrane-associated fatty-acid-binding/transport proteins such as plasma membrane fatty-acid-binding protein (FABPpm, 43 kDa), fatty acid translocase (FAT, 88 kDa) and fatty acid transporter protein (FATP, 63 kDa) have been identified. In the feto-placental unit, preferential transport of maternal plasma arachidonic and docosahexaenoic acids across the placenta is of critical importance for fetal growth and development. Our studies have shown that arachidonic and docosahexaenoic acids are preferentially taken up by placental trophoblasts for fetal transport. The existence of a fatty-acid-transport system comprising multiple membrane-binding proteins (FAT, FATP and FABPpm) in human placenta may be essential to facilitate the preferential transport of maternal plasma fatty acids in order to meet the requirements of the growing fetus. The preferential uptake of arachidonic and docosahexaenoic acids by the human placenta has the net effect of shunting these maternal plasma fatty acids towards the fetus. The roles of plasma membrane-associated binding/transport proteins (FABPpm, FAT and FATP) in tissue-specific fatty acid uptake and metabolism are discussed.

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The role of membranes and intracellular binding proteins in cytoplasmic transport of hydrophobic molecules: Fatty acid-binding proteins

Cited by 34 publications

References 31 publications

New insights into the structure and function of fatty acid-binding proteins

New insights into the structure and function of fatty acid-binding proteins

The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes

Cellular uptake of long-chain fatty acids: role of membrane-associated fatty-acid-binding/transport proteins

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