Identification of Caveolin-1 as a Fatty Acid Binding Protein

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1999-02, Vol.255 (1), p.34-39
Main Authors: Trigatti, Bernardo L., Anderson, Richard G.W., Gerber, Gerhard E.
Format: Article
Language:English
Subjects:
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
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Summary: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 α and β 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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.0123