Characterization of a BODIPY-labeled {fl}uorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism |
| |
| Authors: | Alfred E Thumser Judith Storch |
| |
| Institution: | (1) School of Biomedical and Molecular Sciences, University of Surrey, Guildford, Surrey, GU2 7XH, UK;(2) Department of Nutritional Sciences, Cook College, Rutgers University, 96 Lipman Drive, New Brunswick, New Jersey 08901-8525, USA |
| |
| 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. |
| |
| Keywords: | BODIPY fatty acid-binding protein FABP fluorescence microscopy |
| 本文献已被 PubMed SpringerLink 等数据库收录！ |
|
