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ZFIN ID: ZDB-PUB-151216-13
Fatty acid-binding proteins have the potential to channel dietary fatty acids into enterocyte nuclei
Esteves, A., Knoll-Gellida, A., Canclini, L., Silvarrey, M.C., André, M., Babin, P.J.
Date: 2016
Source: Journal of Lipid Research   57(2): 219-32 (Journal)
Registered Authors: Babin, Patrick J.
Keywords: Diet and dietary lipids, Electron microscopy, Fatty acid, Fatty acid/Binding protein, Fluorescence microscopy, Gene expression, Intestine, Nucleus, Zebrafish
MeSH Terms:
  • Animals
  • Cell Nucleus/genetics
  • Cell Nucleus/metabolism
  • Cytosol/metabolism
  • Enterocytes/metabolism
  • Fatty Acid-Binding Proteins/genetics
  • Fatty Acid-Binding Proteins/metabolism*
  • Fatty Acids/metabolism*
  • Gene Expression Regulation
  • Humans
  • Intestinal Mucosa/metabolism
  • Lipid Metabolism/genetics
  • Zebrafish/genetics*
  • Zebrafish/metabolism
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 26658423 Full text @ J. Lipid Res.
Intracellular-lipid-binding proteins, including fatty acid-binding proteins 1 (FABP1) and 2 (FABP2), are highly expressed in tissues involved in the active lipid metabolism. A zebrafish model was used to demonstrate differential expression levels of fabp1b.1, fabp1b.2, and fabp2 transcripts in liver, anterior intestine, and brain. Transcription levels of fabp1b.1 and fabp2 in the anterior intestine were upregulated after feeding and modulated according to diet formulation. Immunofluorescence and electron microscopy immunodetection with gold particles localized these FABPs in the microvilli, cytosol, and nuclei of most enterocytes in the anterior intestinal mucosa. Nuclear localization was mostly in the interchromatin space outside the condensed chromatin clusters. Native PAGE-binding assay of BODIPY-FL labeled fatty acids (FAs) demonstrated binding of BODIPY-FLC12 but not BODIPY-FLC5 to recombinant Fabp1b.1 and Fabp2. The binding of BODIPY-FLC12 to Fabp1b.1 was fully displaced by oleic acid. In vivo experiments demonstrated, for the first time, that intestinal absorption of dietary BODIPY-FLC12 was followed by co-localization of the labeled FA with Fabp1b and Fabp2 in the nuclei. These data suggest that dietary FAs complexed with FABPs are able to reach the enterocyte nucleus with the potential to modulate nuclear activity.