Output of liver fatty acid-binding protein (L-FABP) in bile
Identifieur interne : 000111 ( France/Analysis ); précédent : 000110; suivant : 000112Output of liver fatty acid-binding protein (L-FABP) in bile
Auteurs : Laurent Foucaud [France] ; Joël Grillasca [France] ; Isabelle Niot [France] ; Nicole Domingo [France] ; Huguette Lafont [France] ; Richard Planells [France] ; Philippe Besnard [France]Source :
- BBA - Molecular and Cell Biology of Lipids [ 1388-1981 ] ; 1998.
Abstract
Liver fatty acid-binding protein (L-FABP) is a small cytoplasmic molecule highly expressed in the liver. Since L-FABP exhibits affinities for several biliary components, its presence in bile was explored by Western blotting and competitive ELISA in various mammalian species. A L-FABP-like immunoreactivity was consistently found in both hepatic and gallbladder bile. A close molecular identity between this 14 kDa biliary protein and the purified L-FABP was assessed by immunological analyses and high performance capillary electrophoresis. Pharmacological induction of hepatic L-FABP biosynthesis led to a similar increase in biliary L-FABP levels showing a close relationships between the cytosolic and biliary contents of this protein. Finally, a correlation between the presence of L-FABP in bile and both bile flow and bile acid release was found. These data suggest an output of L-FABP in bile in normal conditions which might be coupled with the physiological release of biliary components.
Url:
DOI: 10.1016/S0005-2760(98)00171-4
Affiliations:
Links toward previous steps (curation, corpus...)
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- to stream Istex, to step Curation: 000579
- to stream Istex, to step Checkpoint: 002394
- to stream Main, to step Merge: 002C67
- to stream Main, to step Curation: 002B89
- to stream Main, to step Exploration: 002B89
- to stream France, to step Extraction: 000111
Links to Exploration step
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<front><div type="abstract" xml:lang="en">Liver fatty acid-binding protein (L-FABP) is a small cytoplasmic molecule highly expressed in the liver. Since L-FABP exhibits affinities for several biliary components, its presence in bile was explored by Western blotting and competitive ELISA in various mammalian species. A L-FABP-like immunoreactivity was consistently found in both hepatic and gallbladder bile. A close molecular identity between this 14 kDa biliary protein and the purified L-FABP was assessed by immunological analyses and high performance capillary electrophoresis. Pharmacological induction of hepatic L-FABP biosynthesis led to a similar increase in biliary L-FABP levels showing a close relationships between the cytosolic and biliary contents of this protein. Finally, a correlation between the presence of L-FABP in bile and both bile flow and bile acid release was found. These data suggest an output of L-FABP in bile in normal conditions which might be coupled with the physiological release of biliary components.</div>
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