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Output of liver fatty acid-binding protein (L-FABP) in bile

Identifieur interne : 000111 ( France/Analysis ); précédent : 000110; suivant : 000112

Output 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 :

RBID : ISTEX:54AACECDE74BEA4445121A0073BAC60680CDAA30

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:


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ISTEX:54AACECDE74BEA4445121A0073BAC60680CDAA30

Le document en format XML

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<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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