Identification of caveolin-1 as a fatty acid binding protein

Biochem Biophys Res Commun. 1999 Feb 5;255(1):34-9. doi: 10.1006/bbrc.1998.0123.


In an attempt to identify high affinity, fatty acid binding proteins present in 3T3-L1 adipocytes plasma membranes, we labeled proteins in purified plasma membranes with the photoreactive fatty acid analogue, 11-m-diazirinophenoxy[11-3H]undecanoate. A single membrane protein of 22 kDa was covalently labeled after photolysis. This protein fractionated with caveolin-1 containing caveolae and was immunoprecipitated by an anti-caveolin-1 monoclonal antibody. Furthermore, 2D-PAGE analysis revealed that both the alpha and beta isoforms of caveolin-1 could be labeled by the photoreactive fatty acid upon photolysis, indicating that both bind fatty acids. The saturable binding of the photoreactive fatty acid suggests caveolin-1 has a lipid binding site that may either operate during intracellular lipid traffic or regulate caveolin-1 function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipocytes
  • Animals
  • Binding Sites
  • Biological Transport
  • Caveolin 1
  • Caveolins*
  • Cell Line
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Fatty Acids / chemistry*
  • Fatty Acids / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Mice
  • Protein Binding


  • Cav1 protein, mouse
  • Caveolin 1
  • Caveolins
  • Fatty Acids
  • Membrane Proteins