Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D

Science. 1991 Apr 19;252(5004):446-8. doi: 10.1126/science.2017684.


A phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) that specifically hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol-glycans (PI-Gs) has recently been purified from human and bovine sera. The primary structure of bovine PI-G PLD has now been determined and the functional activity of the enzyme has been studied. Expression of PI-G PLD complementary DNA in COS cells produced a protein that specifically hydrolyzed the inositol phosphate linkage of the PI-G anchor. Cotransfection of PI-G PLD with a PI-G-anchored protein resulted in the secretion of the PI-G-anchored protein. The results suggest that the expression of PI-G PLD may influence the expression and location of PI-G-anchored proteins.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Cell Line
  • Cloning, Molecular
  • DNA / genetics
  • Gene Expression
  • Glycosylphosphatidylinositols
  • Humans
  • Hydrolysis
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Phosphatidylinositols / metabolism
  • Phospholipase D / chemistry*
  • Phospholipase D / genetics
  • Phospholipase D / metabolism
  • Polysaccharides / metabolism
  • Sequence Homology, Nucleic Acid
  • Transfection
  • Trypsin


  • Glycosylphosphatidylinositols
  • Peptide Fragments
  • Phosphatidylinositols
  • Polysaccharides
  • DNA
  • Phospholipase D
  • glycoprotein phospholipase D
  • Trypsin

Associated data

  • GENBANK/M60804
  • GENBANK/M61954
  • GENBANK/M61955
  • GENBANK/M61956
  • GENBANK/M61957
  • GENBANK/M61958
  • GENBANK/M61959
  • GENBANK/M61960
  • GENBANK/M61961
  • GENBANK/M61962