Similar mechanisms of fatty acid transfer from human anal rodent fatty acid-binding proteins to membranes: Liver, intestine, heart muscle, and adipose tissue FABPs

  • Judith Storch
  • Jacques H. Veerkamp
  • Kuo-Tung Hsu
Part of the Developments in Molecular and Cellular Biochemistry book series (DMCB, volume 38)


The mammalian fatty acid-binding proteins (FABPs) are thought to be important for the transport and metabolism of fatty acids in numerous cell types. The transfer of FA from different members of the FABP family to membranes has been shown to occur by two distinct mechanisms, an aqueous diffusion-based mechanism and a collisional mechanism, wherein the FABP interacts directly with membrane acceptors. Much of the work that underlies this concept comes from efforts using rodent FABPs. Given the increasing awareness of links between FABPs and several chronic diseases in humans, it was important to establish the mechanisms of FA transfer for human FABPs. In the present studies, we examined the rate and mechanism of fatty acid transfer from four pairs of human and rodent (rat or mouse, as specified) FABPs: hLFABP and rLFABP, hIFABP and rIFABP, hHFABP and rHFABP, and hAFABP and mAFABP. In the case of human IFABP, both the Ala54and Thr54 forms were examined. The results show clearly that for all FABPs examined, the mechanisms of ligand transfer observed for rodent proteins hold true for their human counterparts. Moreover, it appears that the Ala to Thr substitution at residue 54 of the human IFABP does not alter the fundamental mechanism of ligand transfer to membranes, but nevertheless causes a consistent decrease in the rate of transfer. (Mol Cell Biochem 239: 25–33, 2002)

Key words

fatty acid-binding protein fatty acid lipid transport phospholipid membranes gene polymorphism 



fatty acid


fatty acid-binding protein


liver FABP


intestinal FABP


adipose tissue FABP


heart muscle FABP


rat FABP


mouse FABP


human FABP


anthroyloxy-labeled FA


12-(9-anthroyloxy)-oleic acid


2-(9-anthroyloxy)-palmitric acid


small unilamellar vesicles


egg phosphatidylcholine


brain phosphatidylserine


bovine heart cardiolipin




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Copyright information

© Springer Science+Business Media Dordrecht 2002

Authors and Affiliations

  • Judith Storch
    • 1
    • 3
  • Jacques H. Veerkamp
    • 2
  • Kuo-Tung Hsu
    • 1
  1. 1.Department of Nutritional SciencesRutgers UniversityNew BrunswickUSA
  2. 2.Department of BiochemistryUniversity of NijmegenNijmegenThe Netherlands
  3. 3.Department of Nutritional SciencesRutgers UniversityNew BrunswickUSA

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