A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases

Biochem J. 1997 Sep 1;326 ( Pt 2)(Pt 2):455-61. doi: 10.1042/bj3260455.


A novel human homologue of Escherichia coli, yeast and plant 1-acylglycerol-3-phosphate acyltransferase has been isolated from U937 cell cDNA. Expression of the cloned sequence in 1-acylglycerol-3-phosphate acyltransferase-deficient E. coli resulted in increased incorporation of oleic acid into cellular phospholipids. Membranes made from COS7 cells transfected with the cDNA exhibited higher acyltransferase activity towards a range of donor fatty acyl-CoAs and lysophosphatidic acid. Northern-blot analysis of the cDNA sequence indicated high levels of expression in immune cells and epithelium. Rapid amplification of cDNA ends revealed differentially expressed splice variants, which suggests regulation of the enzyme by alternative splicing. This cDNA therefore represents the first described sequence of a mammalian gene homologous to non-mammalian lysophosphatidic acid acyltransferases.

MeSH terms

  • Acyltransferases / chemistry*
  • Acyltransferases / genetics*
  • Acyltransferases / isolation & purification
  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • COS Cells
  • Cell Line
  • Cloning, Molecular
  • Conserved Sequence
  • DNA, Complementary / chemistry*
  • DNA, Complementary / isolation & purification
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Gene Amplification
  • Genetic Vectors / metabolism
  • Humans
  • Macrophages
  • Membrane Lipids / chemistry
  • Membrane Lipids / genetics
  • Molecular Sequence Data
  • Open Reading Frames
  • Plant Proteins / genetics
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Sequence Homology, Amino Acid*


  • DNA, Complementary
  • Membrane Lipids
  • Plant Proteins
  • Acyltransferases
  • 2-acylglycerophosphate acyltransferase

Associated data

  • GENBANK/U75971