Reversible Binding of Long-chain Fatty Acids to Purified FAT, the Adipose CD36 Homolog

@article{Baillie1996ReversibleBO,
  title={Reversible Binding of Long-chain Fatty Acids to Purified FAT, the Adipose CD36 Homolog},
  author={A. G. S. Baillie and Chris T. Coburn and Nada A. Abumrad},
  journal={The Journal of Membrane Biology},
  year={1996},
  volume={153},
  pages={75-81}
}
Abstract. Transport of long-chain fatty acids into rat adipocytes was previously shown to be inhibited by the reactive derivative sulfosuccinimidyl oleate consequent to its binding to a membrane protein FAT, which is homologous to CD36. In this report, the ability of the purified protein to bind native fatty acids was investigated. CD36 was isolated from rat adipocytes by phase partitioning into Triton X-114 followed by chromatography on DEAE and then on wheat germ agglutinin. Fatty acid… 
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Fatty acid translocase/CD36 mediates the uptake of palmitate by type II pneumocytes.
TLDR
It is concluded that FAT/CD36 is expressed in type II pneumocytes and mediates the uptake of palmitate in a saturable and energy-dependent manner and suggests that the uptake process is independent of the formation of coated pits and endocytotic vesicles.
Fatty acid translocase/CD36 mediates the uptake of palmitate by type II pneumocytes.
TLDR
FAT/CD36 is expressed in type II pneumocytes and mediates the uptake of palmitate in a saturable and energy-dependent manner, and the data suggest that the uptake process is independent of the formation of coated pits and endocytotic vesicles.
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TLDR
The data support the interpretation that FAT/CD36 functions as a high-affinity membrane receptor/transporter for long-chain fatty acids.
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TLDR
The results suggest that the major substrate for fatty acylation in adipocytes is a cell surface membrane protein related to CD36 and that this acylations has the unusual properties of being independent of intracellular metabolic energy and of occurring on an exofacial epitope of the protein.
Uptake of oleate by isolated rat adipocytes is mediated by a 40-kDa plasma membrane fatty acid binding protein closely related to that in liver and gut.
TLDR
Data indicate that the uptake of oleate by rat adipocytes is mediated by a 40-kDa plasma membrane fatty acid binding protein closely related to that in liver and gut.
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TLDR
It is concluded that the uptake measurements were valid estimates of the influx of fatty acid, and that permeation by long chain fatty acids is facilitated by a saturable, phloretin-inhibitable mechanism that is presumably protein in nature.
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TLDR
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TLDR
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A membrane protein (FAT) homologous to CD36 has recently been implicated in the binding and transport of long-chain fatty acids (FA). Expression of this protein in rat heart, skeletal muscles and in
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TLDR
Immunocytochemistry and subcellular fractionation of 3T3-L1 adipocytes show that FATP is localized to the plasma membrane, and it is proposed thatfatP is a plasma membrane transporter for LCFAs.
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