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

• Published in: Biochimica et biophysica acta 1999-01, Vol.1436 (3), p.593-599
• Main Authors: Foucaud, Laurent, Grillasca, Joël, Niot, Isabelle, Domingo, Nicole, Lafont, Huguette, Planells, Richard, Besnard, Philippe
• Format: Article
• Language: English
• Subjects: Animals; Bile - metabolism; Biliary secretion; Carrier Proteins - chemistry; Carrier Proteins - isolation & purification; Carrier Proteins - metabolism; Cellular Biology; Cytosol - metabolism; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids - metabolism; Gallbladder - metabolism; Humans; Immunochemistry; Life Sciences; Liver - metabolism; Liver fatty acid-binding protein; Male; Mice; Molecular Weight; Myelin P2 Protein - chemistry; Myelin P2 Protein - isolation & purification; Myelin P2 Protein - metabolism; Neoplasm Proteins; Nerve Tissue Proteins; Rats; Rats, Wistar; Tumor Suppressor Proteins
• ISSN: 1388-1981; 0006-3002; 1879-2618
• DOI: 10.1016/S0005-2760(98)00171-4

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.