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Fatty acid binding protein isoforms: structure and function

F Schroeder1, C A Jolly, T H Cho

  • 1Department of Physiology and Pharmacology, Texas A & M University, TVMC, College Station 77843-4466, USA. FSCHROEDER@CVM.TAMU.EDU

Chemistry and Physics of Lipids
|June 19, 1998
PubMed
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Fatty acid binding proteins (FABPs) exhibit complex isoform heterogeneity. This review critically evaluates true FABP isoforms versus operationally defined forms, exploring their molecular basis and potential functions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Cytosolic fatty acid binding proteins (FABPs) have well-understood structures but unclear physiological functions.
  • The FABP family comprises nearly twenty members, complicating functional analysis.
  • Operational definitions of FABP isoforms via chromatography may be too broad.

Purpose of the Study:

  • To critically evaluate which FABPs form true isoforms versus operationally defined isoforms.
  • To examine the molecular basis of FABP isoform formation.
  • To explore potential functions of FABP isoforms.

Main Methods:

  • Literature review and critical analysis of existing FABP research.
  • Comparison of biochemical and operational definitions of isoforms.

Related Experiment Videos

  • Evaluation of evidence for true FABP isoforms in various species.

    • Main Results:

    • Distinction between true FABP isoforms (differing by amino acids) and putative isoforms (due to ligands, modifications, or conformers).
    • Evidence suggests true isoforms exist for human intestinal I-FABP, bovine/mouse heart H-FABP, rabbit myelin P2, and bovine liver L-FABP.
    • Rat liver L-FABP putative isoforms likely arise from non-genetic factors.

    Conclusions:

    • Clarifying FABP isoform definitions is crucial for understanding their diverse roles.
    • Further research is needed to elucidate the in vitro and in vivo functions of distinct FABP isoforms.
    • Understanding FABP heterogeneity is key to advancing knowledge of lipid metabolism and cellular signaling.