Characterization of a BODIPY-labeled fluorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism

  • Mol Cell Biochem. 2007 May;299(1-2):67-73. doi: 10.1007/s11010-005-9041-2.
Alfred E Thumser  1 ,  Judith Storch
Affiliations
  • 1. School of Biomedical and Molecular Sciences, University of Surrey, Guildford, Surrey, GU2 7XH, UK. [email protected]
PMID: 16645726 DOI: 10.1007/s11010-005-9041-2
Abstract

The BODIPY-labeled fatty acid analogues are a useful addition to the tools employed to study the cellular uptake and metabolism of lipids. In this study, we show that BODIPY FL C(16) binds to purified liver and intestinal fatty acid-binding proteins with high affinity at a site similar to that for the physiological fatty acid oleic acid. Further, in human intestinal Caco-2 cells BODIPY FL C(16) co-localizes extensively with mitochondria, endoplasmic reticulum/Golgi, and L-FABP. Virtually no esterification of BODIPY FL C(16) was observed under the experimental conditions employed. We conclude that BODIPY FL C(16) may be a useful tool for studying the distribution and function of FABPs in a cellular environment.

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