FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells

J Lipid Res. 2002 Sep;43(9):1380-9. doi: 10.1194/jlr.m200130-jlr200.


Biosynthesis of lipids was investigated in growing 293 cells stably expressing fatty acid (FA) transport protein 1 (FATP1), a bifunctional polypeptide with FA transport as well as fatty acyl-CoA synthetase activity. In short-term (30 s) incubations, FA uptake was increased in FATP1 expressing cells (C8 cells) compared with the vector (as determined by BODIPY 3823 staining and radioactive FA uptake). In long-term (4 h) incubations, incorporation of [(14)C]acetate, [3H]oleic acid, or [(14)C]lignoceric acid into 1,2,3-triacyl-sn-glycerol (TG) was elevated in C8 cells compared with vector, whereas incorporation of radiolabel into glycerophospholipids was unaltered. The increase in TG biosynthesis correlated with an increase in 1,2-diacyl-sn-glycerol acyltransferase activity in C8 cells compared with vector. In contrast, incorporation of [(14)C]acetate into sphingomyelin (SM) and cholesterol, and [3H]oleic acid or [(14)C]lignoceric acid into SM was reduced due to a reduction in de novo biosynthesis of these lipids in C8 cells compared with vector. The results indicate that exogenously supplied FAs, and their subsequently produced acyl-CoAs, are preferentially channeled by an FATP1 linked mechanism into the TG biosynthetic pathway and that such internalized lipids down-regulate de novo SM and cholesterol metabolism in actively growing 293 cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biological Transport
  • Carrier Proteins / metabolism*
  • Caveolin 1
  • Caveolins
  • Cell Division
  • Cell Line
  • Cell Membrane / metabolism
  • Cholesterol / metabolism*
  • Coenzyme A Ligases / metabolism
  • Fatty Acid Transport Proteins
  • Fatty Acids / metabolism*
  • Humans
  • Membrane Proteins / metabolism*
  • Membrane Transport Proteins*
  • Oleic Acid / metabolism
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Sphingomyelins / metabolism*
  • Triazenes / pharmacology
  • Triglycerides / metabolism*


  • Carrier Proteins
  • Caveolin 1
  • Caveolins
  • Fatty Acid Transport Proteins
  • Fatty Acids
  • Membrane Proteins
  • Membrane Transport Proteins
  • Repressor Proteins
  • SLC27A1 protein, human
  • Saccharomyces cerevisiae Proteins
  • Sphingomyelins
  • Triazenes
  • Triglycerides
  • Oleic Acid
  • triacsin C
  • Cholesterol
  • Coenzyme A Ligases
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase