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Characterization of a BODIPY-labeled {fl}uorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism

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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 C16 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 C16 co-localizes extensively with mitochondria, endoplasmic reticulum/Golgi, and L-FABP. Virtually no esterification of BODIPY FL C16 was observed under the experimental conditions employed. We conclude that BODIPY FL C16 may be a useful tool for studying the distribution and function of FABPs in a cellular environment.

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Abbreviations

BODIPY FL C16 :

4,4-difluoro-5, 7-dimethyl-4-bora-3a, 4adiaza-s-indacene-3-hexadecanoic acid

FABP:

fatty acid-binding protein

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Correspondence to Alfred E. Thumser.

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Thumser, A.E., Storch, J. Characterization of a BODIPY-labeled {fl}uorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism. Mol Cell Biochem 299, 67–73 (2007). https://doi.org/10.1007/s11010-005-9041-2

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