Characterization of a BODIPY-labeled {fl} uorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism
AE Thumser, J Storch - Molecular and cellular biochemistry, 2007 - Springer
AE Thumser, J Storch
Molecular and cellular biochemistry, 2007•SpringerThe 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 …
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 …
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.
Springer