Characterization of a BODIPY-labeled fluorescent fatty acid analogue. Binding to fatty acid-binding proteins, intracellular localization, and metabolism
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 t...
Saved in:
Published in | Molecular and cellular biochemistry Vol. 299; no. 1-2; pp. 67 - 73 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Netherlands
01.05.2007
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0300-8177 |
DOI: | 10.1007/s11010-005-9041-2 |