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September 1, 2000Journal of Lipid ResearchOpen Access

Ligand-dependent interaction of hepatic fatty acid-binding protein with the nucleus

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Authors

JLJeffrey LawrenceCarilion ClinicDKDavid J. KrollUniversity of Colorado Anschutz Medical CampusPEPatrick I. EachoEli Lilly (United States)

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Implication

Randomized trial investigates L-FABP's role in fatty acid transport to the nucleus, suggesting metabolic signaling mechanisms.

Key Points

  • This research aims to understand how L-FABP mediates fatty acid transport to the nucleus and its interactions with nuclear proteins.
  • Purified rat L-FABP was used to study its interaction with [(3)H]oleic acid in nuclei.
  • Nuclease and proteinase treatments were performed to assess the binding interactions.
  • Far-Western blotting was utilized to identify proteins interacting with L-FABP in rat hepatocyte nuclei.
  • Oleic acid increased nuclear association with L-FABP, while complexing with unlabeled oleic acid reduced it (p<0.05).
  • Nuclease treatment did not alter binding; however, proteinase treatment eliminated it, indicating L-FABP's reliance on nuclear proteins for binding.
  • Analysis revealed that oleic acid enhanced L-FABP's interaction with a 33-kDa nuclear protein, suggesting a specific regulatory role.

Cite This Study

Lawrence et al. (2000) studied this question.

synapsesocial.com/papers/6a20dde234bef10fdaeb157dhttps://doi.org/10.1016/s0022-2275(20)33451-9
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